Cited by 274Inflammasome and immune disordersImmune Response and InflammationStreptococcal Infections and Treatments

The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.

Staphylococcus aureus Evades Lysozyme-Based Peptidoglycan Digestion that Links Phagocytosis, Inflammasome Activation, and IL-1β Secretion

Open access

Shimada, Takahiro, Park, Bong Goo, Wolf, Andrea J., Brikos, Constantinos, Goodridge, Helen S., Becker, Courtney A., Reyes, Christopher N., Miao, Edward A., Aderem, Alan, Götz, Friedrich, Liu, George Y., Underhill, David M.·2010·Cell Host & Microbe

DOI 10.1016/j.chom.2009.12.008PMC PMC2818986

Open this paper in CoChat — free account Open PDF

Abstract

IL-1beta produced by phagocytes is important for protection against the mucosal pathogen Staphylococcus aureus. Processing and maturation of this cytokine requires activation of the multiprotein inflammasome complex. We observed that the bacterial cell wall component peptidoglycan (PGN) must be particulate and internalized via phagocytosis to activate NLRP3 inflammasomes and IL-1beta secretion. In the context of S. aureus infection of macrophages, we find that phagocytosis and lysozyme-based bacterial cell wall degradation are necessary to induce IL-1beta secretion. Further, an S. aureus enzyme, PGN O-acetyltransferase A, previously demonstrated to make cell wall PGN resistant to lysozyme, strongly suppresses inflammasome activation and inflammation in vitro and in vivo. These observations demonstrate that phagocytosis and lysozyme-based cell wall degradation of S. aureus are functionally coupled to inflammasome activation and IL-1beta secretion and illustrate a case whereby a bacterium specifically subverts IL-1beta secretion through chemical modification of its cell wall PGN.

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 · 10.1016/j.chom.2009.12.008

Cites

66 of 66 references verified0 citation errors · 0 not checkable

Statistics

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.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

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

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

Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
Peptidoglycan structure and architecture
Vollmer, W., Blanot, D., & de Pedro, M. A. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00094.x · Cited by 2,355
Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S. L., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02664 · Cited by 1,864
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
Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2
Inohara, N., Ogura, Y., Fontalba, A., Gutierrez, O., Pons, F., Crespo, J., Fukase, K., Inamura, S., Kusumoto, S., Hashimoto, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200673200 · Cited by 1,694

Show all 65 references

Sorted by citations

Items 201–273 of 273

Phagocytosis: a process that shapes immune responses to engulfed meals
Li, K., & Underhill, D. M. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01231-9 · Cited by 16
Self-citation
The Influence of Antibiotic Resistance on Innate Immune Responses to Staphylococcus aureus Infection
Jahan, N., Patton, T., & O’Keeffe, M. A. (2022) · Antibiotics · doi:10.3390/antibiotics11050542 · Cited by 11
A Staphylococcal Glucosaminidase Drives Inflammatory Responses by Processing Peptidoglycan Chains to Physiological Lengths
Resko, Z. J., Anderson, C. M., Federle, M. J., & Alonzo, F. (2023) · Infection and Immunity · doi:10.1128/iai.00500-22 · Cited by 8
Measuring beta-lactam minimum inhibitory concentrations in Staphylococcus aureus in the clinical microbiology laboratory: pinning the tail on the donkey
Sakoulas, G., & Nizet, V. (2023) · Journal of Clinical Microbiology · doi:10.1128/jcm.00366-23 · Cited by 8
Haemophilus ducreyi Infection Induces Activation of the NLRP3 Inflammasome in Nonpolarized but Not in Polarized Human Macrophages
Li, W., Katz, B. P., Bauer, M. E., & Spinola, S. M. (2013) · Infection and Immunity · doi:10.1128/iai.00354-13 · Cited by 8
Streptococcus gordonii DL1 evades polymorphonuclear leukocyte-mediated killing via resistance to lysozyme
Urano-Tashiro, Y., Saiki, K., Yamanaka, Y., Ishikawa, Y., & Takahashi, Y. (2021) · PLoS ONE · doi:10.1371/journal.pone.0261568 · Cited by 8
Kakonein restores hyperglycemia-induced macrophage digestion dysfunction through regulation of cathepsin B-dependent NLRP3 inflammasome activation
Lian, D., Zhu, L., Yu, Y., Zhang, X., Lin, Y.-K., Liu, J., Han, R., Guo, Y., Cai, D., Xiao, W., et al. (2022) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ma0821-418r · Cited by 7
Chemical Barrier Proteins in Human Body Fluids
Kalló, G., Kumar, A., Tőzsér, J., & Csősz, É. (2022) · Biomedicines · doi:10.3390/biomedicines10071472 · Cited by 10
Inflammasome Activation: How Macrophages Watch What They Eat
Vance, R. E. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.011 · Cited by 7
The expression profiles of immune genes in Mus musculus macrophages during Staphylococcus aureus infection
Wang, Z., & Zhu, F. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190490 · Cited by 7
Activation of nucleotide‐binding domain‐like receptor containing protein 3 inflammasome in dendritic cells and macrophages by Streptococcus sanguinis
Saeki, A., Suzuki, T., Hasebe, A., Kamezaki, R., Fujita, M., Nakazawa, F., & Shibata, K. (2017) · Cellular Microbiology · doi:10.1111/cmi.12663 · Cited by 7
Strategy against super-resistant bacteria: Curdlan-induced trained immunity combined with multi-epitope subunit vaccine
Li, H., Niu, L., Wang, J., Chang, Q., Zhang, S., Wang, J., Zeng, J., Gao, M., & Ge, J. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135663 · Cited by 6
Bacterial Infection-Mimicking Three-Dimensional Phagocytosis and Chemotaxis in Electrospun Poly(ε-caprolactone) Nanofibrous Membrane
Lee, S., Maza, P. A. M., Sun, G.-M., Sláma, P., Lee, I.-J., & Kwak, J.-Y. (2021) · Membranes · doi:10.3390/membranes11080569 · Cited by 6
Effects of Small Intestinal Submucosa (SIS) on the Murine Innate Immune Microenvironment Induced by Heat-Killed Staphylococcus aureus
Chowdhury, R. R., Aachoui, Y., & Ghosh, S. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048724 · Cited by 6
Activation of the Inflammasome by Bacterial Pathogens
Ulland, T. K., & Sutterwala, F. S. (2011) · Springer eBooks · doi:10.1007/978-3-0348-0148-5_3 · Cited by 6
How Staphylococcus aureus Breaches Our Skin to Cause Infection
Otto, M. J. (2012) · The Journal of Infectious Diseases · doi:10.1093/infdis/jis248 · Cited by 6
Anti-Intracellular MRSA Activity of Antibiotic-Loaded Lipid-Polymer Hybrid Nanoparticles and Their Effectiveness in Murine Skin Wound Infection Models
Li, W., Tan, C. H., Baek, J.-S., Jiang, L., Ng, N. K. J., Chong, K. K. L., Wong, J. J., Gao, L., Kline, K. A., & Loo, S. C. J. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c01016 · Cited by 5
Neutrophil extracellular traps and interleukin-1β in cystic fibrosis lung disease
Fantone, K. M., Gokanapudi, N., & Rada, B. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1595994 · Cited by 9
Phagocytosis
Wolf, A. J., & Underhill, D. M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1311-4_5 · Cited by 5
Self-citation
Dietary turmeric presents mild immune suppressing and anti-inflammatory effects
Kim, Y., Lee, J.-A., Kim, T., Jung, B., & Lee, B. (2014) · Journal of Preventive Veterinary Medicine · doi:10.13041/jpvm.2014.38.1.7 · Cited by 5
Impact of neonatal malnutrition on expression TLR-9, NF-kB and cytokines of macrophages infected in vitro with methicillin resistant Staphylococcus aureus
de Morais, N. G., da Costa, T. B., de Lima, L. F. F., Basílio, D. D. S., de Morais, N. N. G., de Paiva-Cavalcanti, M., Pereira, V. R. A., & de Castro, C. M. M. B. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.05.009 · Cited by 5
From structure to function: Decoding peptidoglycan O-acetylation in pathogenic bacteria
Anderson, A. C., Malloch, T., & Clarke, A. J. (2025) · Carbohydrate Research · doi:10.1016/j.carres.2025.109517 · Cited by 4
Compositional analysis of bacterial peptidoglycan: insights from peptidoglycomics into structure and function
Anderson, E. M., Brewer, D., Sorbara, M. T., & Khursigara, C. M. (2025) · Journal of Bacteriology · doi:10.1128/jb.00359-25 · Cited by 4
Establishing a macrophage model with relevance for oral methacrylate monomer exposures: Attenuated Staphylococcus aureus-induced cytokine release from human macrophages.
Bølling, A., Olderbø, B. P., Samuelsen, J. T., & Rukke, H. V. (2019) · Dental Materials · doi:10.1016/j.dental.2019.07.005 · Cited by 4
Antibiotic Targets in Gonococcal Cell Wall Metabolism
Medina, K. M. P., & Dillard, J. P. (2018) · Antibiotics · doi:10.3390/antibiotics7030064 · Cited by 4
Lysozyme Gene Expression in 3T3-L1 Cells Sustains Expression of Adipogenic Genes and Adipocyte Differentiation
Lluch, A., Latorre, J., Fernández‐Real, J. M., & Moreno‐Navarrete, J. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.914788 · Cited by 4
Pattern recognition receptors and the innate immune network
van Hensbergen, V. P., & Hu, X. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00131-3 · Cited by 4
Staphylococcal infections
Liu, G. Y., & Bradley, J. S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-79525-8.00024-x · Cited by 3
Self-citation
Divulging the Complexities of Deep Partial- and Full-Thickness Burn Wounds Afflicted by Staphylococcus Aureus Biofilms in a Rat Burn Model
Weaver, A. J., Brandenburg, K. S., Karna, S. L. R., Olverson, C., & Leung, K. P. (2021) · European Burn Journal · doi:10.3390/ebj2030009 · Cited by 3
Biting the hand that feeds: Metabolic determinants of cell fate during infection
Fraschilla, I. R., & Evavold, C. L. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.923024 · Cited by 4
Staphylococcus aureus and Related Staphylococci
Missiakas, D. M., & Schneewind, O. (2015) · CRC Press eBooks · doi:10.1201/b17871-28 · Cited by 3
[Progress on mechanisms for pathogensto evade NOD-like receptor and Toll-like receptor signaling pathways].
Yujie, H. E., & Jianping, P. (2017) · PubMed Central · doi:10.3785/j.issn.1008-9292.2017.04.16 · Cited by 3
Typhoid toxin of Salmonella Typhi elicits host antimicrobial response during acute typhoid fever
Srour, S., Brown, F., Sheffield, J. W., ElGhazaly, M., O’Connor, D., Gibani, M. M., Darton, T. C., Pollard, A. J., Collins, M. O., & Humphreys, D. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00347-8 · Cited by 4
Resident microbes shape host immunity and protect against pathogen infection and inflammatory disease
Mori, D., & Goto, Y. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06219-9 · Cited by 3
A pretreatment scheme for plasmid extraction contained sugar, high concentration lysozyme and mild lysozyme removal
Zhang, Y. M., Jiao, Q., Xie, J., Liu, F., & Pan, Q. (2023) · Analytical Biochemistry · doi:10.1016/j.ab.2023.115242 · Cited by 2
The Antimicrobial Functions of Macrophages
Flannagan, R. S. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1311-4_6 · Cited by 2
NAGging Hexokinase PEPs up NLRP3
Hampton, H. R., Hutcheon, C. J., & Subramanian, N. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.07.017 · Cited by 2
Neutrophils
Jain, R., Mitchell, A. J., Tay, S. S., Roediger, B., & Weninger, W. (2016) · Springer eBooks · doi:10.1007/978-4-431-55855-2_9 · Cited by 2
The Staphylococcal Cell Wall
Sobral, R. G., & Tomasz, A. (2019) · ASM Press eBooks · doi:10.1128/9781683670131.ch36 · Cited by 2
Host Inflammatory Pathways in Malaria Infection: Potential Therapeutic Targets and Biomarkers of Disease Severity
Erdman, L. K. (2012) · TSpace (University of Toronto) · Cited by 2
Targeted p38 mitogen-activated protein kinase inhibition potently augment inflammatory responses of human macrophages toward Staphylococcus aureus
Lund, A., Moffat, D., Jepsen, S. D., Desler, C., Andresen, L. O., Bregenholt, S., Reddy, V., & Skov, S. (2025) · Molecular Immunology · doi:10.1016/j.molimm.2025.05.010 · Cited by 1
Staphylococcal lipoproteins and peptidoglycans synergize to drive skin abscess formation
Mohammad, M., Hu, Z., Scheffler, J. M., Nega, M., Luqman, A., Krzyżowska, M., Sundqvist, M., Kopparapu, P. K., Pullerits, R., Ali, A., et al. (2026) · mBio · doi:10.1128/mbio.00840-26 · Cited by 1
Self-citation
Staphylococcus aureus inhibits the NLRP3 inflammasome in macrophages to varying degrees during early and late stages of infection
Bhagat, S., Kaur, K., Petronglo, J. R., O'Connor, L. D., Wang, C., Li, Y., Swarnkar, G., Khanna, K., Cassat, J. E., Novack, D. V., et al. (2026) · Infection and Immunity · doi:10.1128/iai.00200-26 · Cited by 1
Assessment of antimicrobial activity of c-type lysozyme from Indian shrimp Fenneropenaeus indicus
(2014) · Journal of Coastal Life Medicine · doi:10.12980/jclm.2.2014jclm-2014-0013 · Cited by 1
Arthritis und Osteomyelitis im Kindes- und Jugendalter – bakteriell und nichtbakteriell
Hospach, T., Kallinich, T., Martin, L., Kalle, T. V., Reichert, F., Girschick, H. J., & Hedrich, C. M. (2024) · Zeitschrift für Rheumatologie · doi:10.1007/s00393-024-01504-z · Cited by 1
Disparate Activation of the Inflammasome by Chitin and Chitosan: A Dissertation
Bueter, C. L. (2013) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2w02z · Cited by 1
Antibiotic Education: Not Just Another Brick in the Cell Wall
Sastalla, I., & Datta, S. K. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.10.019 · Cited by 1
RESEARCH OF CERTAIN PATHOGENIC CHARACTERISTICS OF CLINICAL ISOLATES OF STAPHYLOCOCCI OF SKIN BIOME
Kutasevych, Y., Dzhoraeva, S., Goncharenko, V. V., Shcherbakova, Y. V., Мангушева, В. Ю., Sobol, N., & Shchegoleva, H. (2018) · EUREKA Health Sciences · doi:10.21303/2504-5679.2018.00585 · Cited by 1
Bacterial Infections
Miller, L. S. (2017) · Springer eBooks · doi:10.1007/978-3-319-29785-9_16 · Cited by 2
Ctrl-atl-delete: Re-thinking the mechanisms of biofilm formation by staphylococci
McCarthy, H. (2015) · Arrow@dit (Dublin Institute of Technology) · doi:10.13025/16886 · Cited by 1
Involvement of the Iron-Regulated Loci hts and fhuC in Biofilm Formation and Survival of Staphylococcus epidermidis within the Host
Oliveira, F., Lima, T., Correia, A., Silva, A. M., Soares, C., Morais, S., Weißelberg, S., Vilanova, M., Rohde, H., & Cerca, N. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02168-21 · Cited by 12
Etude du rôle de la phospholipase A2 sécrétée de type IIA dans la mucoviscidose : modulation de son expression par Pseudomonas aeruginosa
Pernet, E. (2014) · theses.fr (ABES) · doi:10.70675/0c2d3004z2b72z451dza874z4b00604dc4b8
Mvin mediates Francisella Tularensis virulence through evasion of AIM2 inflammasome activation
Ulland, T. K. (2010) · doi:10.17077/etd.c04zmq85
Dual Protective Functions of Helicobacter pylori Peptidoglycan Modifications Impact Early and Late Survival in the Host
Wang, G. (2013) · JSM Microbiology · doi:10.47739/jsmm-1001
hBD-2 and hBD-3 are induced in S. pneumoniae infected human macrophages via distinct signaling pathways but exhibit similar immune modulatory functions
Wittig, M. M. E. (2016) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-8304
Investigation of Protein and Inhibitor Binding to O-Acetylpeptidoglycan Esterase 1 from Neisseria gonorrhoeae
Ecclestone, M. (2015) · The Atrium (University of Guelph)
The role of lytic transglycosylases LtgA and LtgD in innate immune recognition and pathogenesis of Neisseria gonorrhoeae
Knilans, K. J. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/zz8r-fb35
The Comparative Studies of the Immune Response to Biofilm and Planktonic Forms of Staphylococci
LAVRYK, H., Kornіychuk, O., & Fedechko, J. M. (2018) · Experimental and Clinical Physiology and Biochemistry · doi:10.25040/ecpb2018.04.054
Disease in a Changing Ocean: Ecoimmunological Approaches to Coral Reef Ecology
Fuess, L. E. (2018) · UTA ResearchCommons (University of Texas Arlington)
Intracellular Bacteriolysis Triggering Aim2-Mediated Inflammasome Activation and Necroptosis Contributes to Pathogenicity of Staphylococcus AureusPreprint
Feng, S., Yang, Y., Liu, Z., Chen, W., Du, C., Hu, G., Yu, S.-X., Song, P., & Jinfeng, M. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4105355
Differential survival of Staphylococcal species in macrophagesPreprint
Wolz, C., Bayer, J., Becker, J., Liu, X., Gritsch, L., Daiber, E., Korn, N., Oesterhelt, F., Fraunholz, M. J., & Weber, A. (2023) · doi:10.22541/au.168278380.07406530/v1
Immune Response to Staphylococcus aureus
Nakane, A., & Subsomwong, P. (2024) · Springer eBooks · doi:10.1007/978-981-99-9428-1_5
Wall teichoic acid is required for DNA-triggered innate immune receptor activation by Staphylococcus aureusPreprint
Jastrab, J. B., Tseng, A., Fisch, D., Ragland, S. A., & Kagan, J. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.25.678139
Beyond bacterial defences: the role of lysozyme in cancer
Wang, L., Dong, Q., He, F., Gu, Z., & Sun, A. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70575 · Cited by 1
Modulation par l'interleukin (IL) -17 de la réponse immunitaire innée des cellules épithéliales mammaires bovines à des composants de Staphylococcus aureus
Bougarn, S. (2011) · theses.fr (ABES) · doi:10.70675/bd79dccbz426fz4eb7z976dz42817aba83b2
Étude de la régulation de l'inflammasome AIM2 dans des macrophages infectés par Francisella tularensis
Juruj, C. (2013) · theses.fr (ABES) · doi:10.70675/8f8f5168z111az4a9bzb0d4z0ed113ba0f1a
Le rôle des Guanylate Binding Proteins dans l’immunité cytosolique du macrophage : bactériolyse et morts cellulaires inflammasome-dépendant et indépendant
Wallet, P. (2017) · theses.fr (ABES) · doi:10.70675/81efce18ze9faz40cfzab53z6bfc2b336690
Peptidoglycan : a key elicitor of the gut- brain axis
Fioriti, F. (2023) · theses.fr (ABES) · doi:10.70675/9e7ce0aaz9b66z467bzbc3fz6fa3bf65d9a6
Mechanism-driven nanostrategies against intracellular infections: Leveraging the host-pathogen interplay
Zhu, J., Wu, B., Luo, M., Peng, Y., Yang, F., Liu, L., Wang, Z., & Huang, D. (2026) · Chemical Engineering Journal · doi:10.1016/j.cej.2026.178732
“Just the Best Ones” combination: a new strategy for multi-epitope vaccine candidate based on immunoinformatics analysis to induce protective immunity against MRSA infection
Chang, Q., Niu, L., Zhang, C., Xue, K., Yao, X., Li, H., Jia, Z., Wang, F., & Ge, J. (2026) · Microbiology Spectrum · doi:10.1128/spectrum.03085-25
Cell-autonomous immunity as an integrated immune network against bacterial and viral pathogens
Martín-González, L., Ramos, B., Huang, Y., Thurston, T. L. M., Towers, G. J., & Lobato‐Márquez, D. (2026) · Nature Microbiology · doi:10.1038/s41564-026-02428-x
Innate host defense lysozyme may help control Staphylococcus aureus in atopic dermatitis
Schlievert, P. M., Kilgore, S. H., Berdyshev, E. V., Nodzenski, M., David, G., Yoshida, T., Beck, L. A., & Leung, D. Y. M. (2026) · Microbiology Spectrum · doi:10.1128/spectrum.01585-26
Intracellular Staphylococcus aureus triggers isolate-specific host transcriptional responses alongside TNF-R1 regulated cell fate decisions
Walter, A., Bischler, T., Jungblut, M., Breitsprecher, L. F., Vilotic, F., Beck, J., Hofmann, L., Schäfer, N., Ziesmann, T., Franzkoch, R., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03246-8 · Cited by 2

Authors: Shimada, T., Park, B. G., Wolf, A. J., Brikos, C., Goodridge, H. S., Becker, C. A., Reyes, C. N., Miao, E. A., Aderem, A., Götz, F., Liu, G. Y., & Underhill, D. M.
Affiliations: Cedars-Sinai Medical Center (US)
Institute for Systems Biology (US)
University of Tübingen (DE)
Corresponding author: Underhill, David M.
ORCID: Wolf, Andrea J.
Goodridge, Helen S.
Becker, Courtney A.
Miao, Edward A.
Aderem, Alan
Götz, Friedrich
Liu, George Y.
Underhill, David M.
Venue: Cell Host & Microbe
Publisher: Elsevier BV
Published: 2010-01
Volume: 7
Issue: 1
Pages: 38-49
ISSN: 1931-3128 (ISSN-L)
DOI: 10.1016/j.chom.2009.12.008
PMC: PMC2818986
OpenAlex: W2064358027
Cited by: 274
References: 65
Citations by year: 2026: 9 · 2025: 12 · 2024: 13 · 2023: 12 · 2022: 17 · 2021: 17 · 2020: 11 · 2019: 18 · 2018: 21 · 2017: 13 · 2016: 20 · 2015: 20 · 2014: 13 · 2013: 17 · 2012: 26
FWCI: 10.16
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1293 d)
Locations: Cell Host & Microbe (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Genentech
National Institute of General Medical Sciences (GM-085796, R01GM085796)
National Institute of Allergy and Infectious Diseases (R01AI025032)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Health Sciences › Medicine › Infectious Diseases › Streptococcal Infections and Treatments
Keywords: Staphylococcus aureus, peptidoglycan, lysozyme, phagocytosis, NLRP3 inflammasome, IL-1β secretion, macrophages, inflammation, bacterial evasion of host defense
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Bacterial Proteins, Carrier Proteins, Macrophages, Models, Biological, Muramidase, Peptidoglycan, Phagosomes, Staphylococcus aureus, Interleukin-1beta

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

Staphylococcus aureus Evades Lysozyme-Based Peptidoglycan Digestion that Links Phagocytosis, Inflammasome Activation, and IL-1β Secretion

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks