Cited by 240Immune Response and InflammationImmunotherapy and Immune ResponsesImmune responses and vaccinations

The DOI matches its Crossref record; 204 of the 205 references it cites were found in a registry or an index.

Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology

Open access

Mahla, Ranjeet Singh·2013·Frontiers in Immunology

DOI 10.3389/fimmu.2013.00248PMC PMC3759294

Open this paper in CoChat — free account Open PDF

Abstract

Innate sensors play a critical role in the early innate immune responses to invading pathogens through sensing of diverse biochemical signatures also known as pathogen associated molecular patterns (PAMPs). These biochemical signatures primarily consist of a major family of biomolecules such as proteins, lipids, nitrogen bases, and sugar and its complexes, which are distinct from host molecules and exclusively expressed in pathogens and essential to their survival. The family of sensors known as pattern recognition receptors (PRRs) are germ-line encoded, evolutionarily conserved molecules, and consist of Toll-like receptors (TLRs), RIG-I-like receptors (RLRs), NOD-like receptors (NLRs), C-type lectin-like receptors (CLRs), and DNA sensors. Sensing of PAMP by PRR initiates the cascade of signaling leading to the activation of transcription factors, such as NF-κB and interferon regulatory factors (IRFs), resulting in a variety of cellular responses, including the production of interferons (IFNs) and pro-inflammatory cytokines. In this review, we discuss sensing of different types of glycosylated PAMPs such as β-glucan (a polymeric sugar) or lipopolysaccharides, nucleic acid, and so on (sugar complex PAMPs) by different families of sensors, its role in pathogenesis, and its application in development of potential vaccine and vaccine adjuvants.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.3389/fimmu.2013.00248

Cites

204 of 204 references verified0 citation errors · 0 not checkable

Statistics

Figure 1 Sensing of SCPs through membrane associated PRRs, TLRs, and CLRs. In macrophages and dendritic cells plasma membrane localized TLRs (TLR1, TLR2, TLR4, and TLR6) and endosomal localized TLRs (TLR3, TLR7, TLR8, and TLR9) and TLR13 sense various SCPs as homo or heterodimer (shown in Table 1). TLR recruits MyD88, TRIFs, TIRAP, and TRAM adaptors for induction of inflammatory cytokines and type-I IFNs through activation of NF-κB and IRFs (IRF3 and IRF7) via IKKα/β and TBK1/IKK1, respectively. Dectin-1, Dectin-2, Mincle, and MCL are representative CLRs of Dectin-1 and Dectin-2 clusters. Sensing of various SCPs by Dectin-1 and Dectin-2 (shown in Table 1) recruits, Syk adaptor which further recruits PLCγ and activate cascade of signaling for induction of inflammatory cytokines via NF-κB and MAP kinases.CC BY · PubMed Central

Figure 2 Sensing of SCPs through cytosolic PRRs, RLRs, NLRs, and cytosolic DNA sensors. RLRs family member, RIG-I and MDA5 sense viral dsRNA (shown in Table 2), recruits an adaptor IPS-1 for induction of type-I IFNs and inflammatory cytokines. STING, a molecule plays a pivotal role in sensing of RNA. Several DNA sensors induce inflammatory cytokine and type-I IFNs in STING dependent and independent manner. NLRs family member, NOD1, NOD2, and inflammasome (mainly NLRP1 and NLRP3 and AIM2) induces inflammatory cytokine. NOD1 and NOD2 sense various SCPs (shown in Table 2) recruit an adaptor RIP2 and CARD9 for induction of inflammatory cytokines. Activation of inflammasome complex after stimulation with appropriate SCPs (shown in Table 2) process an inactive, proIL-1 family cytokine to active IL-1 family cytokine.CC BY · PubMed Central

Figure 3 Role of SCPs in vaccine biology. Immunization of host (mice or human) with vaccine or vaccine adjuvant formulation PTC (PAMPs therapeutic complex) activates innate immune pathways (TLRs, CLRs, RLRs, NLRs, and DNA sensors), induce secretion of inflammatory cytokines and type-I IFNs. These cytokines further activate adaptive immune components through B and T lymphocytes. Adaptive immune memory cells protects host from infection.CC BY · PubMed Central

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Yaşlı Kadınlarda Üreme Sağlığı
Kokanalı, D., & Engin Üstün, Y. (n.d.) · DergiPark (Istanbul University) · Cited by 170,090
Two new Later Stone Age sites from the Final Pleistocene in the Falémé Valley, eastern Senegal
Ndiaye, M., Lespez, L., Tribolo, C., Rassé, M., Hadjas, I., Davidoux, S., Huysecom, É., & Douze, K. (2024) · Monash University Research Portal (Monash University) · doi:10.3929/ethz-b-000667478 · Cited by 24,214
The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
Kawai, T., & Akira, S. (2010) · Nature Immunology · doi:10.1038/ni.1863 · Cited by 9,304
Toll-like receptor signalling
Akira, S., & Takeda, K. (2004) · Nature reviews. Immunology · doi:10.1038/nri1391 · Cited by 8,312
Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene
Poltorak, A., He, X., Smirnova, I., Liu, M.-Y., Huffel, C. V., Du, X., Birdwell, D., Alejos, E., Silva, M., Galanos, C., et al. (1998) · Science · doi:10.1126/science.282.5396.2085 · Cited by 7,631
A Toll-like receptor recognizes bacterial DNA
Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491 · cited 1×
“The cellular responses to CpG are mediated through its sensing by the TLR9 receptor (29).”
Background
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
Science
(2023) · doi:10.1126/science · Cited by 6,063
Adult sibling experience, roles, relationshhips and future concerns - a review of the literature in learning disabilities
(1996) · Institutional Research Information System University of Turin (University of Turin) · doi:10.1111/j · Cited by 5,486
Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996
Untitled work
Colman (2022) · doi:10.1073/pnas · Cited by 4,370
The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S., & Fujita, T. (2004) · Nature Immunology · doi:10.1038/ni1087 · Cited by 4,022
Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., et al. (2006) · Nature · doi:10.1038/nature04734 · Cited by 3,888
Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components.
Takeuchi, O., Hoshino, K., Kawai, T., Sanjo, H., Takada, H., Ogawa, T., Takeda, K., & Akira, S. (1999) · Immunity · doi:10.1016/s1074-7613(00)80119-3 · Cited by 3,680
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
Ishikawa, H., & Barber, G. N. (2008) · Nature · doi:10.1038/nature07317 · Cited by 3,576
CpG motifs in bacterial DNA trigger direct B-cell activation
Krieg, A. M., Yi, A.-K., Matson, S., Waldschmidt, T. J., Bishop, G. A., Teasdale, R., Koretzky, G. A., & Klinman, D. M. (1995) · Nature · doi:10.1038/374546a0 · Cited by 3,508
Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S., & Reis e Sousa, C. (2004) · Science · doi:10.1126/science.1093616 · Cited by 3,444
Journal of Biological Chemistry
Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,427
Cutting Edge: Toll-Like Receptor 4 (TLR4)-Deficient Mice Are Hyporesponsive to Lipopolysaccharide: Evidence for TLR4 as the Lps Gene Product
Hoshino, K., Takeuchi, O., Kawai, T., Sanjo, H., Ogawa, T., Takeda, Y., Takeda, K., & Akira, S. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.7.3749 · Cited by 3,374
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Hornung, V., Ablasser, A., Charrel-Dennis, M., Bauernfeind, F., Horvath, G., Caffrey, D. R., Latz, E., & Fitzgerald, K. A. (2009) · Nature · doi:10.1038/nature07725 · Cited by 2,627
Small anti-viral compounds activate immune cells via the TLR7 MyD88–dependent signaling pathway
Hemmi, H., Kaisho, T., Takeuchi, O., Sato, S., Sanjo, H., Hoshino, K., Horiuchi, T., Tomizawa, H., Takeda, K., & Akira, S. (2002) · Nature Immunology · doi:10.1038/ni758 · Cited by 2,577
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
Kawai, T., Takahashi, K., Sato, S., Coban, C., Kumar, H., Kato, H., Ishii, K. J., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1243 · Cited by 2,562
5'-Triphosphate RNA Is the Ligand for RIG-I
Hornung, V., Ellegast, J., Kim, S., Brzózka, K., Jung, A., Kato, H., Poeck, H., Akira, S., Conzelmann, K.-K., Schlee, M., et al. (2006) · Science · doi:10.1126/science.1132505 · Cited by 2,474
RIG-I-mediated antiviral responses to single-stranded RNA bearing 5’-phosphates
Pichlmair, A., Schulz, O., Tan, C. P., Näslund, T. I., Liljeström, P., Weber, F., & Reis e Sousa, C. (2006) · Science · doi:10.1126/science.1132998 · Cited by 2,210
MD-2, a Molecule that Confers Lipopolysaccharide Responsiveness on Toll-like Receptor 4
Shimazu, R., Akashi, S., Ogata, H., Nagai, Y., Fukudome, K., Miyake, K., & Kimoto, M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1777 · Cited by 2,187
Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production
Saitoh, T., Fujita, N., Jang, M. H., Uematsu, S., Yang, B., Satoh, T., Omori, H., Noda, T., Yamamoto, N., Komatsu, M., et al. (2008) · Nature · doi:10.1038/nature07383 · Cited by 2,064
Vaccine Adjuvants: Putting Innate Immunity to Work
Coffman, R. L., Sher, A., & Seder, R. A. (2010) · Immunity · doi:10.1016/j.immuni.2010.10.002 · Cited by 1,927
Immune Signaling by RIG-I-like Receptors
Loo, Y.-M., & Gale, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.003 · Cited by 1,875
The history of toll-like receptors - redefining innate immunity
O'Neill, L. A. J., Golenbock, D., & Bowie, A. G. (2013) · Nature reviews. Immunology · doi:10.1038/nri3446 · Cited by 1,765
The roles of TLRs, RLRs and NLRs in pathogen recognition
Kawai, T., & Akira, S. (2009) · International Immunology · doi:10.1093/intimm/dxp017 · Cited by 1,725
Peptidoglycan- and Lipoteichoic Acid-induced Cell Activation Is Mediated by Toll-like Receptor 2
Schwandner, R., Dziarski, R., Wesche, H., Rothe, M., & Kirschning, C. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17406 · Cited by 1,704
DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
Takaoka, A., Wang, Z., Choi, M. K., Yanai, H., Negishi, H., Ban, T., Lu, Y., Miyagishi, M., Kodama, T., Honda, K., et al. (2007) · Nature · doi:10.1038/nature06013 · Cited by 1,704
CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING.
Ablasser, A., Goldeck, M., Cavlar, T., Deimling, T., Witte, G., Röhl, I., Hopfner, K.-P., Ludwig, J., & Hornung, V. (2013) · Nature · doi:10.1038/nature12306 · Cited by 1,695
Shared and Unique Functions of the DExD/H-Box Helicases RIG-I, MDA5, and LGP2 in Antiviral Innate Immunity
Yoneyama, M., Kikuchi, M., Matsumoto, K., Imaizumi, T., Miyagishi, M., Taira, K., Foy, E. M., Loo, Y., Gale, M., Akira, S., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2851 · Cited by 1,691
IFI16 is an innate immune sensor for intracellular DNA
Unterholzner, L., Keating, S. E., Baran, M., Horan, K. A., Jensen, S. B., Sharma, S., Sirois, C. M., Jin, T., Latz, E., Xiao, T. S., et al. (2010) · Nature Immunology · doi:10.1038/ni.1932 · Cited by 1,643
Nod1 Detects a Unique Muropeptide from Gram-Negative Bacterial Peptidoglycan
Girardin, S. E., Boneca, I. G., Carneiro, L. A. M., Antignac, A., Jéhanno, M., Viala, J., Tedin, K., Taha, M., Labigne-Roussel, A., Zäthringer, U., et al. (2003) · Science · doi:10.1126/science.1084677 · Cited by 1,625
The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases
Davis, B. K., Wen, H., & Ting, J. P.-Y. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101405 · Cited by 1,618
A new receptor for β-glucans
Brown, G. D., & Gordon, S. (2001) · Nature · doi:10.1038/35092620 · Cited by 1,579
CpG motifs present in bacteria DNA rapidly induce lymphocytes to secrete interleukin 6, interleukin 12, and interferon gamma.
Klinman, D., Yi, A., Beaucage, S., Conover, J., & Krieg, A. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.7.2879 · Cited by 1,543
Signalling through C-type lectin receptors: shaping immune responses
Geijtenbeek, T. B. H., & Gringhuis, S. I. (2009) · Nature reviews. Immunology · doi:10.1038/nri2569 · Cited by 1,449
Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin
Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442
The C‐type lectin‐like domain superfamily
Zelensky, A. N., & Gready, J. E. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05031.x · Cited by 1,411
Cell Type-Specific Involvement of RIG-I in Antiviral Response
Kato, H., Sato, S., Yoneyama, M., Yamamoto, M., Uematsu, S., Matsui, K., Tsujimura, T., Takeda, K., Fujita, T., Takeuchi, O., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.04.010 · Cited by 1,368
The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
Rathinam, V. A. K., Jiang, Z., Waggoner, S. N., Sharma, S., Cole, L. E., Waggoner, L., Vanaja, S. K., Monks, B. G., Ganesan, S., Latz, E., et al. (2010) · Nature Immunology · doi:10.1038/ni.1864 · Cited by 1,331
An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
Chamaillard, M., Hashimoto, M., Horie, Y., Masumoto, J., Qiu, S., Saab, L., Ogura, Y., Kawasaki, A., Fukase, K., Kusumoto, S., et al. (2003) · Nature Immunology · doi:10.1038/ni945 · Cited by 1,323
Toll-like Receptor 9–mediated Recognition of Herpes Simplex Virus-2 by Plasmacytoid Dendritic Cells
Lund, J. M., Sato, A., Akira, S., Medzhitov, R. M., & Iwasaki, A. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030162 · Cited by 1,197
Dectin-1 is required for β-glucan recognition and control of fungal infection
Taylor, P. R., Tsoni, S. V., Willment, J. A., Dennehy, K. M., Rosas, M., Findon, H., Haynes, K., Steele, C. H., Botto, M., Gordon, S., et al. (2006) · Nature Immunology · doi:10.1038/ni1408 · Cited by 1,185
Toll‐like Receptor and RIG‐1‐like Receptor Signaling
Kawai, T., & Akira, S. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1443.020 · Cited by 1,014
The NLR Gene Family: A Standard Nomenclature
Ting, J. P. ‐., Lovering, R. C., Alnemri, E. S., Bertin, J., Boss, J. M., Davis, B. K., Flavell, R. A., Girardin, S. E., Godzik, A., Harton, J. A., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.02.005 · Cited by 998
Function of Nod‐like receptors in microbial recognition and host defense
Franchi, L., Warner, N. E., Viani, K. L., & Núñez, G. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00734.x · Cited by 938
Type I Interferon Inhibits Interleukin-1 Production and Inflammasome Activation
Guarda, G., Braun, M., Staehli, F., Tardivel, A., Mattmann, C., Förster, I., Farlik, M., Decker, T., Pasquier, R. D., Romero, P. J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.006 · Cited by 924
CpG DNA as a vaccine adjuvant
Bode, C., Zhao, G., Steinhagen, F., Kinjo, T., & Klinman, D. M. (2011) · Expert Review of Vaccines · doi:10.1586/erv.10.174 · Cited by 916
Structural mechanism of cytosolic DNA sensing by cGAS
Çivril, F., Deimling, T., Mann, C. C. D. O., Ablasser, A., Moldt, M., Witte, G., Hornung, V., & Hopfner, K. (2013) · Nature · doi:10.1038/nature12305 · Cited by 916
The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
Zhang, Z., Yuan, B., Bao, M., Lu, N., Kim, T., & Liu, Y. (2011) · Nature Immunology · doi:10.1038/ni.2091 · Cited by 874
Peroxisomes Are Signaling Platforms for Antiviral Innate Immunity
Dixit, E., Boulant, S., Zhang, Y., Lee, A. S. Y., Odendall, C., Shum, B. O. V., Hacohen, N., Chen, Z. J., Whelan, S. P. J., Fransen, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.018 · Cited by 850
Tlr4: central component of the sole mammalian LPS sensor.
Beutler, B. (2000) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)00046-1 · Cited by 847
Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages
Underhill, D. M., Ozinsky, A., Smith, K. D., & Aderem, A. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14459 · Cited by 827
Human Toll-Like Receptors Mediate Cellular Activation by Mycobacterium tuberculosis
Means, T. K., Wang, S., Lien, E., Yoshimura, A., Golenbock, D. T., & Fenton, M. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.7.3920 · Cited by 804
Non-transcriptional Priming and Deubiquitination Regulate NLRP3 Inflammasome Activation
Juliana, C. A., Fernandes‐Alnemri, T., Kang, S., Farias, A., Qin, F., & Alnemri, E. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407130 · Cited by 803
Dectin-2 Recognition of α-Mannans and Induction of Th17 Cell Differentiation Is Essential for Host Defense against Candida albicans
Saijo, S., Ikeda, S., Yamabe, K., Kakuta, S., Ishigame, H., Akitsu, A., Fujikado, N., Kusaka, T., Kubo, S., Chung, S.-H., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.05.001 · Cited by 760
The Structural Biology of Toll-like Receptors
Botos, I., Segal, D. M., & Davies, D. R. (2011) · Structure · doi:10.1016/j.str.2011.02.004 · Cited by 740
LGP2 is a positive regulator of RIG-I– and MDA5-mediated antiviral responses
Satoh, T., Kato, H., Kumagai, Y., Yoneyama, M., Sato, S., Matsushita, K., Tsujimura, T., Fujita, T., Akira, S., & Takeuchi, O. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912986107 · Cited by 722
Selective proper name anomia in a patient with asymmetric cortical degeneration
Fadda, L., Turriziani, P., Carlesimo, G. A., Nocentini, U., & Caltagirone, C. (1998) · European Journal of Neurology · doi:10.1046/j.1468-1331.1998.540417.x · Cited by 716
Reconstituted NALP1 Inflammasome Reveals Two-Step Mechanism of Caspase-1 Activation
Faustin, B., Lartigue, L., Bruey, J., Luciano, F., Sergienko, E. A., Bailly‐Maitre, B., Volkmann, N., Hanein, D., Rouiller, I., & Reed, J. C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.032 · Cited by 709
CpG DNA Is a Potent Enhancer of Specific Immunity in Mice Immunized with Recombinant Hepatitis B Surface Antigen
Davis, H. L., Weeranta, R., Waldschmidt, T. J., Tygrett, L. T., Schorr, J., & Krieg, A. Μ. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.2.870 · Cited by 676
Microbial Stimulation Fully Differentiates Monocytes to DC-SIGN/CD209+ Dendritic Cells for Immune T Cell Areas
Cheong, C., de Matos, I. G., Choi, J., Dandamudi, D. B., Shrestha, E., Longhi, M. P., Jeffrey, K. L., Anthony, R. M., Kluger, C., Nchinda, G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.039 · Cited by 640
TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines
Ishii, K. J., Kawagoe, T., Koyama, S., Matsui, K., Kumar, H., Kawai, T., Uematsu, S., Takeuchi, O., Takeshita, F., Coban, C., et al. (2008) · Nature · doi:10.1038/nature06537 · Cited by 633
Drosophila Toll and IL-1 receptor
Gay, N. J., & Keith, F. J. (1991) · Nature · doi:10.1038/351355b0 · Cited by 623
Immunotherapeutic applications of CpG oligodeoxynucleotide TLR9 agonists
Vollmer, J., & Krieg, A. Μ. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.12.008 · Cited by 594
Activation of Toll-Like Receptor-2 by Glycosylphosphatidylinositol Anchors from a Protozoan Parasite
Campos, M. A., de Almeida, I. C., Takeuchi, O., Akira, S., Valente, E. P., Procópio, D. O., Travassos, L. R., Smith, J. A., Golenbock, D. T., & Gazzinelli, R. T. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.1.416 · Cited by 587
Structural Basis for dsRNA Recognition, Filament Formation, and Antiviral Signal Activation by MDA5
Wu, B., Peisley, A., Richards, C., Yao, H., Zeng, X., Lin, C., Feixia Chu, C., Walz, T., & Hur, S. (2012) · Cell · doi:10.1016/j.cell.2012.11.048 · Cited by 585
Structures of the Toll-like Receptor Family and Its Ligand Complexes
Jin, M. S., & Lee, J. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.007 · Cited by 573
Signaling by Myeloid C-Type Lectin Receptors in Immunity and Homeostasis
Sancho, D., & Sousa, C. R. E. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101352 · Cited by 557
RICK/RIP2 Mediates Innate Immune Responses Induced through Nod1 and Nod2 but Not TLRs
Park, J., Kim, Y., McDonald, C., Kanneganti, T., Hasegawa, M., Body–Malapel, M., Inohara, N., & Núñez, G. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.4.2380 · Cited by 532
A critical role of RICK/RIP2 polyubiquitination in Nod‐induced NF‐κB activation
Hasegawa, M., Fujimoto, Y., Lucas, P. C., Nakano, H., Fukase, K., Núñez, G., & Inohara, N. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601962 · Cited by 520
Immunostimulatory oligodeoxynucleotides containing the CpG motif are effective as immune adjuvants in tumor antigen immunization
Weiner, G. J., Liu, H.-M., Wooldridge, J. E., Dahle, C. E., & Krieg, A. Μ. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10833 · Cited by 516
Dectin-1 directs T helper cell differentiation by controlling noncanonical NF-κB activation through Raf-1 and Syk
Gringhuis, S. I., den Dunnen, J., Litjens, M., van der Vlist, M., Wevers, B. A., Bruijns, S. C. M., & Geijtenbeek, T. B. H. (2009) · Nature Immunology · doi:10.1038/ni.1692 · Cited by 507
Essential role of IPS-1 in innate immune responses against RNA viruses
Kumar, H., Kawai, T., Kato, H., Sato, S., Takahashi, K., Coban, C., Yamamoto, M., Uematsu, S., Ishii, K. J., Takeuchi, O., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20060792 · Cited by 503
The Ubiquitin Ligase TRIM56 Regulates Innate Immune Responses to Intracellular Double-Stranded DNA
Tsuchida, T., Zou, J. P., Saitoh, T., Kumar, H., Abe, T., Matsuura, Y., Kawai, T., & Akira, S. (2010) · Immunity · doi:10.1016/j.immuni.2010.10.013 · Cited by 500
Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis
Jones, J. W. M., Kayagaki, N., Brož, P., Henry, T., Newton, K., O’Rourke, K. M., Chan, S. B., Dong, J. J., Qu, Y., Roose-Girma, M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003738107 · Cited by 487
Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125
Arimoto, K., Takahashi, H., Hishiki, T., Konishi, H., Fujita, T., & Shimotohno, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611551104 · Cited by 482
Toll-Like Receptor SignalingPreprint
Lim, K., & Staudt, L. M. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011247 · Cited by 478
T-helper 1 cells facilitate the entry of T-helper 17 cells to the central nervous system during experimental autoimmune encephalomyelitis
MacLeod (2008) · Bristol Research (University of Bristol) · doi:10.4049/jimmunol · Cited by 448
The Macrophage-Inducible C-Type Lectin, Mincle, Is an Essential Component of the Innate Immune Response to Candida albicans
Wells, C. A., Salvage-Jones, J., Li, X., Hitchens, K., Butcher, S., Murray, R. Z., Beckhouse, A. G., Lo, Y.-L.-S., Manzanero, S., Cobbold, C., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7404 · Cited by 434
West Nile virus infection and immunity
Suthar, M. S., Diamond, M., & Gale, M. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2950 · Cited by 432
Dissecting negative regulation of Toll-like receptor signaling
Kondo, T., Kawai, T., & Akira, S. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.05.002 · Cited by 419
The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a β-catenin-dependent pathway
Yang, P., An, H., Liu, X., Wen, M., Zheng, Y., Rui, Y., & Cao, X. (2010) · Nature Immunology · doi:10.1038/ni.1876 · Cited by 409
Nitric oxide suppresses NLRP3 inflammasome activation and protects against LPS-induced septic shock
Mao, K., Chen, S., Chen, M., Ma, Y., Wang, Y., Huang, B., He, Z., Zeng, Y., Hu, Y., Sun, S., et al. (2013) · Cell Research · doi:10.1038/cr.2013.6 · Cited by 408
TLR13 Recognizes Bacterial 23 S rRNA Devoid of Erythromycin Resistance–Forming Modification
Oldenburg, M., Krüger, A., Ferstl, R., Kaufmann, A., Nees, G., Sigmund, A., Bathke, B., Lauterbach, H., Suter, M., Dreher, S., et al. (2012) · Science · doi:10.1126/science.1220363 · Cited by 405 · cited 1×
“The recently discovered TLR13 is involved in sensing of bacterial 23S rRNA (12).”
Background
Nucleic acid sensing at the interface between innate and adaptive immunity in vaccination
Desmet, C. J., & Ishii, K. J. (2012) · Nature reviews. Immunology · doi:10.1038/nri3247 · Cited by 404
Myeloid C-type Lectin Receptors in Pathogen Recognition and Host Defense
Osorio, F., & Sousa, C. R. E. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.001 · Cited by 388
Molecular basis for structural diversity in the core regions of the lipopolysaccharides of Escherichia coli and Salmonella enterica
Heinrichs, D. E., Yethon, J. A., & Whitfield, C. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.01063.x · Cited by 376
Structural Reorganization of the Toll-Like Receptor 8 Dimer Induced by Agonistic Ligands
Tanji, H., Ohto, U., Shibata, T., Miyake, K., & Shimizu, T. (2013) · Science · doi:10.1126/science.1229159 · Cited by 369
STUDIES ON THE O ANTIGEN OF SALMONELLA TYPHOSA
Johnson, A. G., Gaines, S., & Landy, M. (1956) · The Journal of Experimental Medicine · doi:10.1084/jem.103.2.225 · Cited by 360
DNA damage sensor MRE11 recognizes cytosolic double-stranded DNA and induces type I interferon by regulating STING trafficking
Kondo, T., Kobayashi, J., Saitoh, T., Maruyama, K., Ishii, K. J., Barber, G. N., Komatsu, K., Akira, S., & Kawai, T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222694110 · Cited by 357
Characterization of cationic liposomes based on dimethyldioctadecylammonium and synthetic cord factor from M. tuberculosis (trehalose 6,6′-dibehenate)—A novel adjuvant inducing both strong CMI and antibody responses
Davidsen, J. R., Rosenkrands, I., Christensen, D., Vangala, A., Kirby, D. J., Perrie, Y., Agger, E. M., & Andersen, P. L. (2005) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2005.10.011 · Cited by 341
RIG‐I‐like receptors: cytoplasmic sensors for non‐self RNA
Kato, H., Takahasi, K., & Fujita, T. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01052.x · Cited by 340
Development and Characterization of Synthetic Glucopyranosyl Lipid Adjuvant System as a Vaccine Adjuvant
Coler, R. N., Bertholet, S., Moutaftsi, M., Guderian, J. A., Windish, H. P., Baldwin, S. L., Laughlin, E. M., Duthie, M. S., Fox, C. B., Carter, D., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016333 · Cited by 322
MARCO, TLR2, and CD14 Are Required for Macrophage Cytokine Responses to Mycobacterial Trehalose Dimycolate and Mycobacterium tuberculosis
Bowdish, D. M. E., Sakamoto, K., Kim, M., Klaas, M., Mukhopadhyay, S., Leifer, C. A., Tryggvason, K., Gordon, S., & Russell, D. G. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000474 · Cited by 320
NLRP1 Inflammasome Activation Induces Pyroptosis of Hematopoietic Progenitor Cells
Masters, S. L., Gerlic, M., Metcalf, D., Preston, S., Pellegrini, M., O’Donnell, J. A., McArthur, K., Baldwin, T. M., Chevrier, S., Nowell, C. J., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.08.027 · Cited by 313
Function of RIG-I-like Receptors in Antiviral Innate Immunity
Yoneyama, M., & Fujita, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.r700007200 · Cited by 307
TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway
Michallet, M., Meylan, E., Ermolaeva, M., Vázquez, J., Rebsamen, M., Curran, J. A., Poeck, H., Bscheider, M., Hartmann, G., König, M. F., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.03.013 · Cited by 304
Glycobiology of immune responses
Rabinovich, G. A., van Kooyk, Y., & Cobb, B. A. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06492.x · Cited by 293
Innate immune DNA sensing pathways: STING, AIMII and the regulation of interferon production and inflammatory responses
Barber, G. N. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.12.015 · Cited by 287
(1,3)-β-Glucans Activate Both Dectin-1 and NLRP3 Inflammasome in Human Macrophages
Kankkunen, P., Teirilä, L., Rintahaka, J., Alenius, H. T., Wolff, H. J., & Matikainen, S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903019 · Cited by 282
Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I
Wang, Y., Ludwig, J., Schuberth, C., Goldeck, M., Schlee, M., Li, H., Juranek, S., Sheng, G., Micura, R., Tuschl, T., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1863 · Cited by 258
C-type lectin DC-SIGN: An adhesion, signalling and antigen-uptake molecule that guides dendritic cells in immunity
Švajger, U., Anderluh, M., Jeras, M., & Obermajer, N. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.018 · Cited by 256
Cytoplasmic DNA innate immune pathways
Barber, G. N. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01051.x · Cited by 254
Targeting C-type lectin receptors with multivalent carbohydrate ligands
Lepenies, B., Lee, J., & Sonkaria, S. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.05.007 · Cited by 251
The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA
Zhang, Z., Bao, M., Lu, N., Weng, L., Yuan, B., & Liu, Y. (2012) · Nature Immunology · doi:10.1038/ni.2492 · Cited by 249
Identification of Distinct Ligands for the C-type Lectin Receptors Mincle and Dectin-2 in the Pathogenic Fungus Malassezia
Ishikawa, T., Itoh, F., Yoshida, S., Saijo, S., Matsuzawa, T., Gonoi, T., Saito, T., Okawa, Y., Shibata, N., Miyamoto, T., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.03.008 · Cited by 247
1,25-Dihydroxyvitamin D Promotes Negative Feedback Regulation of TLR Signaling via Targeting MicroRNA-155–SOCS1 in Macrophages
Chen, Y., Liu, W., Sun, T., Huang, Y., Wang, Y., Deb, D. K., Yoon, D., Kong, J., Thadhani, R., & Li, Y. C. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1203273 · Cited by 241
Superior Immunogenicity of Inactivated Whole Virus H5N1 Influenza Vaccine is Primarily Controlled by Toll-like Receptor Signalling
Geeraedts, F., Goutagny, N., Hornung, V., Severa, M., de Haan, A., Pool, J., Wilschut, J., Fitzgerald, K. A., & Huckriede, A. L. W. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000138 · Cited by 237
Recognition of bacterial infection by innate immune sensors
Kumar, S., Ingle, H., Prasad, D. V. R., & Kumar, H. (2012) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2012.706249 · Cited by 232
C-type Lectin MCL Is an FcRγ-Coupled Receptor that Mediates the Adjuvanticity of Mycobacterial Cord Factor
Miyake, Y., Toyonaga, K., Mori, D., Kakuta, S., Hoshino, Y., Oyamada, A., Yamada, H., Ono, K.-I., Suyama, M., Iwakura, Y., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.03.010 · Cited by 230
The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways.
Lambert, A. A., Gilbert, C., Richard, M., Beaulieu, A., & Tremblay, M. (2008) · Blood · doi:10.1182/blood-2008-01-136473 · Cited by 214
C-Type Lectin-Like Receptors of the Dectin-1 Cluster: Ligands and Signaling Pathways
Plato, A., Willment, J. A., & Brown, G. D. (2013) · International Reviews of Immunology · doi:10.3109/08830185.2013.777065 · Cited by 212
Septic Shock Is Associated with Receptor for Advanced Glycation End Products Ligation of LPS
Yamamoto, Y., Harashima, A., Saito, H., Tsuneyama, K., Munesue, S., Motoyoshi, S., Han, D., Watanabe, T., Asano, M., Takasawa, S., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002253 · Cited by 207
Bacterial Teichoic Acids Reverse Predominant IL-12 Production Induced by Certain Lactobacillus Strains into Predominant IL-10 Production via TLR2-Dependent ERK Activation in Macrophages
Kaji, R., Kiyoshima‐Shibata, J., Nagaoka, M., Nanno, M., & Shida, K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901569 · Cited by 199
Of inflammasomes and pathogens – sensing of microbes by the inflammasome
Bauernfeind, F. G., & Hornung, V. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201771 · Cited by 198
Cutting Edge: Roles of Caspase-8 and Caspase-10 in Innate Immune Responses to Double-Stranded RNA
Takahashi, K., Kawai, T., Kumar, H., Sato, S., Yonehara, S., & Akira, S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4520 · Cited by 186
The Dectin-2 family of C-type lectin-like receptors: an update
Kerscher, B., Willment, J. A., & Brown, G. D. (2013) · International Immunology · doi:10.1093/intimm/dxt006 · Cited by 184
Protection against endotoxic shock and lipopolysaccharide-induced local inflammation by tetracycline: correlation with inhibition of cytokine secretion
Shapira, L., Soskolne, W. A., Houri‐Haddad, Y., Barak, V., Halabi, A., & Stabholz, A. (1996) · Infection and Immunity · doi:10.1128/iai.64.3.825-828.1996 · Cited by 182
Selective C-Rel Activation via Malt1 Controls Anti-Fungal TH-17 Immunity by Dectin-1 and Dectin-2
Gringhuis, S. I., Wevers, B. A., Kaptein, T. M., van Capel, T. M. M., Theelen, B., Boekhout, T., de Jong, E. C., & Geijtenbeek, T. B. H. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001259 · Cited by 179
Pathogen-associated molecular patterns on biomaterials: a paradigm for engineering new vaccines
Demento, S. L., Siefert, A. L., Bandyopadhyay, A., Sharp, F. A., & Fahmy, T. M. (2011) · Trends in biotechnology · doi:10.1016/j.tibtech.2011.02.004 · Cited by 177
The role of the β-glucan receptor Dectin-1 in control of fungal infection
Dennehy, K. M., & Brown, G. D. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206753 · Cited by 173
Combination of the Cationic Surfactant Dimethyl Dioctadecyl Ammonium Bromide and Synthetic Mycobacterial Cord Factor as an Efficient Adjuvant for Tuberculosis Subunit Vaccines
Holten-Andersen, L., Doherty, T. M., Korsholm, K. S., & Andersen, P. L. (2004) · Infection and Immunity · doi:10.1128/iai.72.3.1608-1617.2004 · Cited by 172
Peptidoglycan Signaling in Innate Immunity and Inflammatory Disease
McDonald, C., Inohara, N., & Núñez, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.r500001200 · Cited by 169
The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction
Kufer, T. A., Kremmer, E., Adam, A. C., Philpott, D. J., & Sansonetti, P. J. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.01062.x · Cited by 169
Phospholipase Cγ2 Is Critical for Dectin-1-mediated Ca2+ Flux and Cytokine Production in Dendritic Cells
Xu, S., Huo, J., Lee, K.-G., Kurosaki, T., & Lam, K.-P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806650200 · Cited by 166
Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at mitochondria
Xu, L., Xiao, N., Liu, F., Ren, H., & Gu, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811029106 · Cited by 159
The fungal pattern recognition receptor, Dectin-1, and the associated cluster of C-type lectin-like receptors
Huysamen, C., & Brown, G. D. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01418.x · Cited by 155
Poly(I:C) is an effective adjuvant for antibody and multi-functional CD4+ T cell responses to Plasmodium falciparum circumsporozoite protein (CSP) and αDEC-CSP in Non Human Primates
Tewari, K., Flynn, B., Boscardin, S., Kastenmueller, K., Salazar, A., Anderson, C., Soundarapandian, V., Ahumada, A., Keler, T., Hoffman, S., et al. (2010) · Vaccine · doi:10.1016/j.vaccine.2010.08.098 · Cited by 153
Roles of lipoarabinomannan in the pathogenesis of tuberculosis
Strohmeier, G. R., & Fenton, M. J. (1999) · Microbes and Infection · doi:10.1016/s1286-4579(99)80072-0 · Cited by 147
Adjuvant Activity of CpG Oligodeoxynucleotides
Klinman, D. M. (2006) · International Reviews of Immunology · doi:10.1080/08830180600743057 · Cited by 147
The Mincle-Activating Adjuvant TDB Induces MyD88-Dependent Th1 and Th17 Responses through IL-1R Signaling
Desel, C., Werninghaus, K., Ritter, M., Jozefowski, K., Wenzel, J., Russkamp, N. F., Schleicher, U., Christensen, D., Wirtz, S. J., Kirschning, C. J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053531 · Cited by 145
Hepatitis C Virus Targets DC-SIGN and L-SIGN To Escape Lysosomal Degradation
Ludwig, I. S., Lekkerkerker, A., Depla, E., Bosman, F., Musters, R. J. P., Depraetere, S., van Kooyk, Y., & Geijtenbeek, T. B. H. (2004) · Journal of Virology · doi:10.1128/jvi.78.15.8322-8332.2004 · Cited by 145
Virus-like glycodendrinanoparticles displaying quasi-equivalent nested polyvalency upon glycoprotein platforms potently block viral infection
Ribeiro-Viana, R., Sánchez‐Navarro, M., Luczkowiak, J., Koeppe, J. R., Delgado, R. B., Rojo, J., & Davis, B. G. (2012) · Nature Communications · doi:10.1038/ncomms2302 · Cited by 145
The role of dendritic cell C-type lectin receptors in HIV pathogenesis
Turville, S. G., Wilkinson, J. C., Cameron, P. U., Dable, J., & Cunningham, A. L. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0503208 · Cited by 142
Vaccine adjuvants aluminum and monophosphoryl lipid A provide distinct signals to generate protective cytotoxic memory CD8 T cells
MacLeod, M. K. L., McKee, A. S., David, A. P., Wang, J., Mason, R. J., Kappler, J. W., & Marrack, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104588108 · Cited by 137
Lipoteichoic Acid and Toll-like Receptor 2 Internalization and Targeting to the Golgi Are Lipid Raft-dependent
Triantafilou, M., Manukyan, M., Mackie, A. R., Morath, S., Härtung, T., Heine, H., & Triantafilou, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400466200 · Cited by 133
Glycosylations in the Globular Head of the Hemagglutinin Protein Modulate the Virulence and Antigenic Properties of the H1N1 Influenza Viruses
Medina, R., Stertz, S., Manicassamy, B., Zimmermann, P., Sun, X., Albrecht, R. A., Uusi-Kerttula, H. K., Zagordi, O., Belshe, R. B., Frey, S. E., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3005996 · Cited by 128
The interaction of macrophage receptors with bacterial ligands
Plüddemann, A., Mukhopadhyay, S., & Gordon, S. (2006) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399406000159 · Cited by 124
Regulation of RLR-mediated innate immune signaling – It is all about keeping the balance
Eisenächer, K., & Krug, A. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.01.011 · Cited by 123
Phosphodiester CpG oligonucleotides as adjuvants: polyguanosine runs enhance cellular uptake and improve immunostimulative activity of phosphodiester CpG oligonucleotides in vitro and in vivo
Dalpke, A. H., Zimmermann, S., Albrecht, I., & Heeg, K. M. (2002) · Immunology · doi:10.1046/j.1365-2567.2002.01410.x · Cited by 120
Glycan-based DC-SIGN targeting vaccines to enhance antigen cross-presentation
van Kooyk, Y., Unger, W. W. J., Fehres, C. M., Kalay, H., & García-Vallejo, J. J. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.10.031 · Cited by 119
The vesicle size of DDA:TDB liposomal adjuvants plays a role in the cell-mediated immune response but has no significant effect on antibody production
Henriksen‐Lacey, M., Devitt, A., & Perrie, Y. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.05.019 · Cited by 118
Gold nanorod delivery of an ssRNA immune activator inhibits pandemic H1N1 influenza viral replication
Chakravarthy, K. V., Bonoiu, A. C., Davis, W. G., Ranjan, P., Ding, H. Y., Hu, R., Bowzard, J. B., Bergey, E. J., Katz, J. M., Knight, P. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914561107 · Cited by 113
Glycomics, glycoproteomics and the immune system
Kolarich, D., Lepenies, B., & Seeberger, P. H. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.12.006 · Cited by 112
Serum Lipopolysaccharide Activity Is Associated With the Progression of Kidney Disease in Finnish Patients With Type 1 Diabetes
Nymark, M., Pussinen, P. J., Tuomainen, A. M., Forsblom, C. M., Groop, P., Lehto, M. J., & on behalf of the FinnDiane Study Group (2009) · Diabetes Care · doi:10.2337/dc09-0467 · Cited by 109
C-type lectin receptors and cytokines in fungal immunity
Vautier, S., MacCallum, D. M., & Brown, G. D. (2011) · Cytokine · doi:10.1016/j.cyto.2011.08.031 · Cited by 108
NOD‐like receptor (NLR) signaling beyond the inflammasome
Shaw, P. J., Lamkanfi, M., & Kanneganti, T. (2010) · European Journal of Immunology · doi:10.1002/eji.200940211 · Cited by 105
Activation of RIG-I-like receptor signal transduction
Bruns, A. M., & Horvath, C. M. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2011.630974 · Cited by 95
ATP Hydrolysis Enhances RNA Recognition and Antiviral Signal Transduction by the Innate Immune Sensor, Laboratory of Genetics and Physiology 2 (LGP2)
Bruns, A. M., Pollpeter, D., Hadizadeh, N., Myong, S., Marko, J. F., & Horvath, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424416 · Cited by 95
Identification of an N-Terminal Recognition Site in TLR9 That Contributes to CpG-DNA-Mediated Receptor Activation
Peter, M. E., Kubarenko, A. V., Weber, A. N. R., & Dalpke, A. H. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900819 · Cited by 90
A β-glucan-conjugate vaccine and anti-β-glucan antibodies are effective against murine vaginal candidiasis as assessed by a novel in vivo imaging technique
Pietrella, D., Rachini, A., Torosantucci, A., Chiani, P., Brown, A. J. P., Bistoni, F., Costantino, P., Mosci, P., d’Enfert, C., Rappuoli, R., et al. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.12.021 · Cited by 89
Negative regulation of NLRP3 inflammasome signaling
Chen, S., & Sun, B. (2013) · Protein & Cell · doi:10.1007/s13238-013-2128-8 · Cited by 84
Lipoteichoic Acid-Induced Lung Inflammation Depends on TLR2 and the Concerted Action of TLR4 and the Platelet-Activating Factor Receptor
Knapp, S., von Aulock, S., Leendertse, M., Haslinger, I., Draing, C., Golenbock, D. T., & van der Poll, T. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.5.3478 · Cited by 83
Role of N -Acetylglucosamine within Core Lipopolysaccharide of Several Species of Gram-Negative Bacteria in Targeting the DC-SIGN (CD209)
Zhang, P., Snyder, S., Feng, P., Azadi, P., Zhang, S., Bulgheresi, S., Sanderson, K. E., He, J. J., Klena, J. D., & Chen, T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.6.4002 · Cited by 83
Necessity of Oligonucleotide Aggregation for Toll-like Receptor 9 Activation
Wu, C. C. N., Lee, J., Raz, E., Corr, M., & Carson, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311662200 · Cited by 83
Analysis of Antiviral Response in Human Epithelial Cells Infected with Hepatitis E Virus
Devhare, P. B., Chatterjee, S. N., Arankalle, V. A., & Lole, K. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063793 · Cited by 81
Comparison of antibodies and carbohydrates to target vaccines to human dendritic cells via DC-SIGN
Cruz, L. J., Tacken, P. J., Pots, J. M., Torensma, R., Buschow, S. I., & Figdor, C. G. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.02.036 · Cited by 76
NLRP3 activation induces ASC-dependent programmed necrotic cell death, which leads to neutrophilic inflammation
Satoh, T. K., Kambe, N., & Matsue, H. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.169 · Cited by 75
Enhanced Immunogenicity of a Tricomponent Mannan Tetanus Toxoid Conjugate Vaccine Targeted to Dendritic Cells via Dectin-1 by Incorporating β-Glucan
Lipiński, T., Fitieh, A. M., St‐Pierre, J., Ostergaard, H. L., Bundle, D. R., & Touret, N. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202937 · Cited by 75
The mycobacterial cord factor adjuvant analogue trehalose-6,6′-dibehenate (TDB) activates the Nlrp3 inflammasome
Schweneker, K., Gorka, O., Schweneker, M., Poeck, H., Tschopp, J., Peschel, C., Ruland, J., & Groß, O. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.07.029 · Cited by 70
Superior Activity of the Type C Class of ISS In Vitro and In Vivo Across Multiple Species
Marshall, J. D., Fearon, K. L., Higgins, D., Hessel, E. M., Kanzler, H., Abbate, C., Yee, P., Gregorio, J. D., Cruz, T. D., Lizcano, J. O., et al. (2005) · DNA and Cell Biology · doi:10.1089/dna.2005.24.63 · Cited by 68
Characterization of a Nontoxic Monophosphoryl Lipid A
Johnson, A. G., Tomai, M. A., Solem, L. E., Beck, L., & Ribi, E. E. (1987) · Clinical Infectious Diseases · doi:10.1093/clinids/9.supplement_5.s512 · Cited by 67
An Adenovirus-Based Vaccine with a Double-Stranded RNA Adjuvant Protects Mice and Ferrets against H5N1 Avian Influenza in Oral Delivery Models
Scallan, C. D., Tingley, D. W., Lindbloom, J. D., Toomey, J. S., & Tucker, S. N. (2012) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00552-12 · Cited by 67
Therapeutic potential of various β-glucan sources in conjunction with anti-tumor monoclonal antibody in cancer therapy
Driscoll, M. F., Hansen, R., Ding, C., Cramer, D. E., & Yan, J. (2009) · Cancer Biology & Therapy · doi:10.4161/cbt.8.3.7337 · Cited by 66
Parasitic Infections: A Role for C-Type Lectins Receptors
Vázquez-Mendoza, A., Carrero, J. C., & Rodríguez‐Sosa, M. (2013) · BioMed Research International · doi:10.1155/2013/456352 · Cited by 64
Inhibitory C-type lectin receptors in myeloid cells
Redelinghuys, P., & Brown, G. D. (2010) · Immunology Letters · doi:10.1016/j.imlet.2010.10.005 · Cited by 62
Prophylactic and therapeutic efficacies of poly(IC.LC) against respiratory influenza A virus infection in mice
Wong, J. P., Saravolac, E. G., Sabuda, D., Levy, H. B., & Kende, M. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.11.2574 · Cited by 55
Collectins and fungal pathogens: roles of surfactant proteins and mannose binding lectin in host resistance
Brummer, E., & Stevens, D. A. (2010) · Medical Mycology · doi:10.3109/13693780903117473 · Cited by 53
Role of sugars in surface microbe–host interactions and immune reaction modulation
Lloyd, D. H., Viac, J., Werling, D., Rème, C. A., & Gatto, H. (2007) · Veterinary Dermatology · doi:10.1111/j.1365-3164.2007.00594.x · Cited by 53
Epigenetic Regulation of Tumor Necrosis Factor α (TNFα) Release in Human Macrophages by HIV-1 Single-stranded RNA (ssRNA) Is Dependent on TLR8 Signaling
Han, X., Li, X., Yue, S. C., Anandaiah, A. M., Hashem, F., Reinach, P. S., Koziel, H., & Tachado, S. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342683 · Cited by 47
Immunoprotective activity of a Salmonid Alphavirus Vaccine: Comparison of the immune responses induced by inactivated whole virus antigen formulations based on CpG class B oligonucleotides and poly I:C alone or combined with an oil adjuvant
Thim, H. L., Iliev, D. B., Christie, K. E., Villoing, S., McLoughlin, M. F., Strandskog, G., & Jørgensen, J. B. (2012) · Vaccine · doi:10.1016/j.vaccine.2012.05.010 · Cited by 47
Pathogen sensors and chemokine receptors in dendritic cell subsets
Kaisho, T. (2012) · Vaccine · doi:10.1016/j.vaccine.2012.10.043 · Cited by 46
Glycan-based DC-SIGN targeting to enhance antigen cross-presentation in anticancer vaccines
García-Vallejo, J. J., Unger, W. W. J., Kalay, H., & van Kooyk, Y. (2013) · OncoImmunology · doi:10.4161/onci.23040 · Cited by 44
Induction of intestinal pro-inflammatory immune responses by lipoteichoic acid
Zadeh, M., Khan, M. W., Goh, Y. J., Selle, K., Owen, J. L., Klaenhammer, T. R., & Mohamadzadeh, M. (2012) · Journal of Inflammation · doi:10.1186/1476-9255-9-7 · Cited by 43
Poly(I:C)/Alum Mixed Adjuvant Priming Enhances HBV Subunit Vaccine-Induced Immunity in Mice When Combined with Recombinant Adenoviral-Based HBV Vaccine Boosting
Chuai, X., Chen, H., Wang, W., Deng, Y. L., Wen, B., Ruan, L., & Tan, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054126 · Cited by 42
Enhancement of anti-cancer immunity by a lipoteichoic-acid-related molecule isolated from a penicillin-killed group A Streptococcus
Okamoto, M., Ohe, G., Oshikawa, T., Furuichi, S., Nishikawa, H., Tano, T., Ahmed, S. U., Yoshida, H., Moriya, Y., Saito, M., et al. (2001) · Cancer Immunology Immunotherapy · doi:10.1007/s002620100207 · Cited by 34
Activated Human CD4+CD45RO+ Memory T-Cells Indirectly Inhibit NLRP3 Inflammasome Activation through Downregulation of P2X7R Signalling
Beynon, V., Quintana, F. J., & Weiner, H. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039576 · Cited by 34
Monophosphoryl lipid A plus IFNγ maturation of dendritic cells induces antigen-specific CD8+ cytotoxic T cells with high cytolytic potential
ten Brinke, A., van Schijndel, G. M. W., Visser, R., de Gruijl, T. D., Zwaginga, J. J., & van Ham, S. M. (2010) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-010-0843-z · Cited by 33
The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity
Galandrini, R., Tassi, I., Morrone, S., Lanfrancone, L., Pelicci, P. G., Piccoli, M., Frati, L., & Santoni, A. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200107)31:7 · Cited by 32
CpG DNA-mediated Induction of Acute Liver Injury in d-Galactosamine-sensitized Mice
Yi, A., Yoon, H., Park, J. J., Kim, B., Kim, H. J., & Martínez‐Hernández, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601337200 · Cited by 32
Effect of Liposomal Formulations and Immunostimulating Peptidoglycan Monomer (PGM) on the Immune Reaction to Ovalbumin in Mice
Habjanec, L., Frkanec, R., Halassy, B., & Tomašić, J. (2006) · Journal of Liposome Research · doi:10.1080/08982100500528537 · Cited by 32
CpG increases vaccine antigen-specific cell-mediated immunity when administered with hepatitis B vaccine in HIV infection
Angel, J. B., Cooper, C., Clinch, J., Young, C. D., Chenier, A., Parato, K., Lautru, M., Davis, H. L., & Cameron, D. W. (2008) · Journal of Immune Based Therapies and Vaccines · doi:10.1186/1476-8518-6-4 · Cited by 30
Adjuvant activity of peptidoglycan monomer and its metabolic products
Halassy, B., Krstanović, M., Frkanec, R., & Tomašić, J. (2003) · Vaccine · doi:10.1016/s0264-410x(02)00547-9 · Cited by 30
Anticancer and Immunostimulatory Activity by Conjugate of Paclitaxel and Non-toxic Derivative of LPS for Combined Chemo-immunotherapy
Roy, A., Chandra, S., Mamilapally, S., Upadhyay, P. K., & Bhaskar, S. (2012) · Pharmaceutical Research · doi:10.1007/s11095-012-0756-y · Cited by 30
Vaccination with mannan protects mice against systemic aspergillosis
Liu, M., Machová, E., Neščáková, Z., Medovarská, I., Clemons, K. V., Martinez, M., Chen, V., Bystrický, S., & Stevens, D. A. (2012) · Medical Mycology · doi:10.3109/13693786.2012.683539 · Cited by 30
A novel liposomal vaccine improves humoral immunity and prevents tumor pulmonary metastasis in mice
Zhong, Z.-H., Wei, X., Qi, B., Xiao, W., Yang, L., Wei, Y., & Chen, L. (2010) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2010.07.053 · Cited by 28
HIV-1 Gp120 Protein Downregulates Nef Induced IL-6 Release in Immature Dentritic Cells through Interplay of DC-SIGN
Sarkar, R., Mitra, D., & Chakrabarti, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059073 · Cited by 28
Biological activities of lipoteichoic acid and peptidoglycan--teichoic acid of Bacillus subtilis 168 (Marburg)
Himanen, J. P., PYHÄLÄ, L., Ölander, R., Merimskaya, O., Tn, K., Lysyuk, O., Пронин, А. В., Av, S., Helander, I. M., & Sarvas, M. (1993) · Journal of General Microbiology · doi:10.1099/00221287-139-11-2659 · Cited by 27
Vaccination with Enzymatically Cleaved GPI-Anchored Proteins fromSchistosoma mansoniInduces Protection against Challenge Infection
Martins, V. D. P., Pinheiro, C. S., Figueiredo, B. C.-P., Assis, N. R. G., Morais, S. B., Caliari, M. V., Azevedo, V., Castro‐Borges, W., Wilson, R. A., & Oliveira, S. C. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/962538 · Cited by 27
The Staphylococcus aureus Peptidoglycan Protects Mice against the Pathogen and Eradicates Experimentally Induced Infection
Capparelli, R., Nocerino, N., Medaglia, C., Blaiotta, G., Bonelli, P., & Iannelli, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028377 · Cited by 26
Influenza A whole virion vaccine induces a rapid reduction of peripheral blood leukocytes via interferon-α-dependent apoptosis
Ato, M., Takahashi, Y., Fujii, H., Hashimoto, S., Kaji, T., Itamura, S., Horiuchi, Y., Arakawa, Y., Tashiro, M., & Takemori, T. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.02.016 · Cited by 23
Rat Macrophage C-Type Lectin Is an Activating Receptor Expressed by Phagocytic Cells
Lobato‐Pascual, A., Saether, P. C., Dahle, M. K., Gaustad, P., Dissen, E., Fossum, S., & Daws, M. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057406 · Cited by 22
Optimisation of Prime–Boost Immunization in Mice Using Novel Protein-Based and Recombinant Vaccinia (Tiantan)-Based HBV Vaccine
Chen, H., Chuai, X., Deng, Y. L., Wen, B., Wang, W., Xiong, S., Ruan, L., & Tan, W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043730 · Cited by 21
Adjuvant effects of trehalose dimycolate on the antibody response to type III pneumococcal polysaccharide
Baker, P. J., Fauntleroy, M. B., Stashak, P. W., Hiernaux, J. R., Cantrell, J. L., & Rudbach, J. A. (1989) · Infection and Immunity · doi:10.1128/iai.57.3.912-917.1989 · Cited by 20
Bacterial lipopolysaccharide induces long-lasting IgA deficiency concurrently with features of polyclonal B cell activation in normal and in lupus-prone mice
Cavallo, T., & Granholm, N. A. (1991) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.1991.tb08136.x · Cited by 12

Sorted by citations

Biological roles of glycans
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
An Update on the Genus Aeromonas: Taxonomy, Epidemiology, and Pathogenicity
Fernández-Bravo, A., & Figueras, M. J. (2020) · Microorganisms · doi:10.3390/microorganisms8010129 · Cited by 738
The NLRP3 Inflammasome Pathway: A Review of Mechanisms and Inhibitors for the Treatment of Inflammatory Diseases
Blevins, H. M., Xu, Y., Biby, S., & Zhang, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.879021 · Cited by 587
Toll-like receptors activation, signaling, and targeting: an overview
El-Zayat, S. R., Sibaii, H., & Mannaa, F. A. E. (2019) · Bulletin of the National Research Centre/Bulletin of the National Research Center · doi:10.1186/s42269-019-0227-2 · Cited by 603
Redefining Chronic Inflammation in Aging and Age-Related Diseases: Proposal of the Senoinflammation Concept
Chung, H. Y., Kim, D. H., Lee, E. K., Chung, K. W., Chung, S., Lee, B., Seo, A. Y., Chung, J. H., Jung, Y. S., Im, E., et al. (2018) · Aging and Disease · doi:10.14336/ad.2018.0324 · Cited by 512

See all 240

Authors: Mahla, R. S.
Affiliations: Indian Institute of Science Education and Research, Bhopal (IN)
Corresponding author: Mahla, Ranjeet Singh
ORCID: Mahla, Ranjeet Singh
Venue: Frontiers in Immunology
Publisher: Frontiers Media SA
Published: 2013
Volume: 4
Pages: 248-248
ISSN: 1664-3224 (ISSN-L)
DOI: 10.3389/fimmu.2013.00248
PMC: PMC3759294
OpenAlex: W2045475619
Cited by: 239
References: 205
Citations by year: 2026: 4 · 2025: 11 · 2024: 23 · 2023: 20 · 2022: 26 · 2021: 34 · 2020: 34 · 2019: 34 · 2018: 19 · 2017: 19 · 2016: 7 · 2015: 3 · 2014: 4 · 2013: 1
FWCI: 0.44
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Immunology (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Department of Biotechnology, Ministry of Science and Technology, India (SR/S2/RJN-55/2009, BT/PR6009/GBD/27/382/2012)
Department of Science and Technology, Ministry of Science and Technology, India
Topics: Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Life Sciences › Immunology and Microbiology › Immunology › Immune responses and vaccinations
Keywords: pathogen-associated molecular patterns, innate immunity, pattern recognition receptors, Toll-like receptors, RIG-I-like receptors, NOD-like receptors, C-type lectin-like receptors, DNA biosensor, β-glucan, lipopolysaccharide, vaccine adjuvants, vaccine development, interferon signaling, NF-κB, inflammatory cytokines

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology

Abstract

Overview

Integrity signals

Figures

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks