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

Flagged first, then by citations

Show all 65 references

Sorted by citations

Items 101–200 of 273

NLRP3 inflammasomes that induce antitumor immunity
Zhivaki, D., & Kagan, J. C. (2021) · Trends in Immunology · doi:10.1016/j.it.2021.05.001 · Cited by 61
Peptidoglycan O-Acetylation as a Virulence Factor: Its Effect on Lysozyme in the Innate Immune System
Brott, A. S., & Clarke, A. J. (2019) · Antibiotics · doi:10.3390/antibiotics8030094 · Cited by 60
Two lytic transglycosylases inNeisseria gonorrhoeaeimpart resistance to killing by lysozyme and human neutrophils
Ragland, S. A., Schaub, R. E., Hackett, K. T., Dillard, J. P., & Criss, A. K. (2016) · Cellular Microbiology · doi:10.1111/cmi.12662 · Cited by 56
Nonpathogenic Lactobacillus rhamnosus activates the inflammasome and antiviral responses in human macrophages
Miettinen, M., Pietilä, T. E., Kekkonen, R. A., Kankainen, M., Latvala, S., Pirhonen, J., Österlund, P., Korpela, R., & Julkunen, I. (2012) · Gut Microbes · doi:10.4161/gmic.21736 · Cited by 56
The endolysosomal cysteine cathepsins L and K are involved in macrophage‐mediated clearance of Staphylococcus aureus and the concomitant cytokine induction
Müller, S., Faulhaber, A. K., Sieber, C., Pfeifer, D., Hochberg, T., Gansz, M., Deshmukh, S. D., Dauth, S., Brix, K., Säftig, P., et al. (2013) · The FASEB Journal · doi:10.1096/fj.13-232272 · Cited by 56
Characterisation of Innate Fungal Recognition in the Lung
Faro-Trindade, I., Willment, J. A., Kerrigan, A. M., Redelinghuys, P., Hadebe, S., Reid, D. M., Srinivasan, N., Wainwright, H., Lang, D. M., Steele, C., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035675 · Cited by 55
Mechanistic Pathways for Peptidoglycan O-Acetylation and De-O-Acetylation
Sychantha, D., Brott, A. S., Jones, C. S., & Clarke, A. J. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02332 · Cited by 56
Immune and Inflammatory Reponses to Staphylococcus aureus Skin Infections
Liu, Q., Mazhar, M., & Miller, L. S. (2018) · Current Dermatology Reports · doi:10.1007/s13671-018-0235-8 · Cited by 58
Antimicrobial Effects of Camel Milk against Some Bacterial Pathogens
Yassin, M. H., Soliman, M. M., Mostafa, S. A.-E., & Ali, H. A. (2015) · Journal of Food and Nutrition Research · doi:10.12691/jfnr-3-3-6 · Cited by 52
Consequences of Metabolic Interactions during Staphylococcus aureus Infection
Lung, T. W. F., & Prince, A. S. (2020) · Toxins · doi:10.3390/toxins12090581 · Cited by 57
Staphylococcus aureus in Substrates for Black Soldier Fly Larvae (Hermetia illucens) and Its Dynamics during Rearing
Gorrens, E., Looveren, N. V., Moll, L. V., Vandeweyer, D., Lachi, D., Smet, J. D., & Campenhout, L. V. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.02183-21 · Cited by 54
Cutting Edge: Primary Innate Immune Cells Respond Efficiently to Polymeric Peptidoglycan, but Not to Peptidoglycan Monomers
Iyer, J. K., & Coggeshall, K. M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1004058 · Cited by 48
O-Acetylation of Peptidoglycan Limits Helper T Cell Priming and Permits Staphylococcus aureus Reinfection
Sanchez, M., Kolar, S. L., Müller, S., Reyes, C. N., Wolf, A. J., Ogawa, C., Singhania, R., Carvalho, D. D. D., Arditi, M., Underhill, D. M., et al. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.08.008 · Cited by 52
Self-citation
Gasdermin D Flashes an Exit Signal for IL-1
Kuriakose, T., & Kanneganti, T. (2018) · Immunity · doi:10.1016/j.immuni.2018.01.003 · Cited by 45
New insights in the coordinated amidase and glucosaminidase activity of the major autolysin (Atl) in Staphylococcus aureus
Nega, M., Tribelli, P. M., Hipp, K., Stahl, M., & Götz, F. (2020) · Communications Biology · doi:10.1038/s42003-020-01405-2 · Cited by 42
Self-citation
Malassezia spp. induce inflammatory cytokines and activate NLRP3 inflammasomes in phagocytes
Wolf, A. J., Limon, J. J., Nguyen, C., Prince, A., Castro, A., & Underhill, D. M. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.2ma0820-259r · Cited by 47
Self-citation
Inhibitory Receptor Paired Ig-like Receptor B Is Exploited by Staphylococcus aureus for Virulence
NAKAYAMA, M., Kurokawa, K., Nakamura, K., Lee, B. L., Sekimizu, K., Kubagawa, H., Hiramatsu, K., Yagita∥, H., Okumura, K., Takai, T., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201940 · Cited by 47
Self-citation
Inflammasome/IL-1β Responses to Streptococcal Pathogens
LaRock, C. N., & Nizet, V. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00518 · Cited by 50
Structure of the pneumococcal l , d ‐carboxypeptidase DacB and pathophysiological effects of disabled cell wall hydrolases DacA and DacB
Abdullah, M. R., Gutiérrez‐Fernández, J., Pribyl, T. M., Gisch, N., Saleh, M., Rohde, M., Petruschka, L., Burchhardt, G., Schwudke, D., Hermoso, J. A., et al. (2014) · Molecular Microbiology · doi:10.1111/mmi.12729 · Cited by 54
Identification of Drosophila Yin and PEPT2 as Evolutionarily Conserved Phagosome-associated Muramyl Dipeptide Transporters
Charrière, G. M., Ip, W. E., Déjardin, S., Boyer, L., Sokolovska, A., Cappillino, M. P., Cherayil, B. J., Podolsky, D. K., Kobayashi, K. S., Silverman, N. S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.115584 · Cited by 46
Failure To Induce IFN-β Production during Staphylococcus aureus Infection Contributes to Pathogenicity
Kaplan, A. T., Ma, J., Kyme, P. A., Wolf, A. J., Becker, C. A., Tseng, C. W., Liu, G. Y., & Underhill, D. M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201111 · Cited by 46
Self-citation
A bacterial regulatory RNA attenuates virulence, spread and human host cell phagocytosis
Pabic, H. L., Germain‐Amiot, N., Bordeau, V., & Felden, B. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv783 · Cited by 45
The Staphylococcal Cell Wall
Sobral, R. G., & Tomasz, A. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0068-2019 · Cited by 45
NOD2 Stimulation by Staphylococcus aureus-Derived Peptidoglycan Is Boosted by Toll-Like Receptor 2 Costimulation with Lipoproteins in Dendritic Cells
Schäffler, H., Demircioğlu, D. D., Kühner, D., Menz, S., Bender, A., Autenrieth, I. B., Bodammer, P., Lamprecht, G., Götz, F., & Frick, J.-S. (2014) · Infection and Immunity · doi:10.1128/iai.02043-14 · Cited by 45
Self-citation
Disease reduction in aquaculture with genetic and genomic technology: current and future approaches
Elaswad, A., & Dunham, R. A. (2017) · Reviews in Aquaculture · doi:10.1111/raq.12205 · Cited by 44
The role of inflammasome modulation in virulence
Lupfer, C. R., & Kanneganti, T. (2012) · Virulence · doi:10.4161/viru.20266 · Cited by 43
Immunomodulation and Disease Tolerance to Staphylococcus aureus
Li, Z., Peres, A. G., Damian, A. C., & Madrenas, J. (2015) · Pathogens · doi:10.3390/pathogens4040793 · Cited by 44
Rhodomyrtone Modulates Innate Immune Responses of THP-1 Monocytes to Assist in Clearing Methicillin-Resistant Staphylococcus aureus
Srisuwan, S., Tongtawe, P., Srimanote, P., & Voravuthikunchai, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110321 · Cited by 41
Inflammasome Activation Can Mediate Tissue-Specific Pathogenesis or Protection in Staphylococcus aureus Infection
Melehani, J. H., & Duncan, J. A. (2016) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-41171-2_13 · Cited by 41
Balancing Act of the Intestinal Antimicrobial Proteins on Gut Microbiota and Health
Ra, Y. E., & Bang, Y. (2024) · The Journal of Microbiology · doi:10.1007/s12275-024-00122-3 · Cited by 51
Neisseria gonorrhoeae Lytic Transglycosylases LtgA and LtgD Reduce Host Innate Immune Signaling through TLR2 and NOD2
Knilans, K. J., Hackett, K. T., Anderson, J. E., Weng, C., Dillard, J. P., & Duncan, J. A. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00088 · Cited by 39
Is a Reported Penicillin Allergy Sufficient Grounds to Forgo the Multidimensional Antimicrobial Benefits of β-Lactam Antibiotics?
Sakoulas, G., Geriak, M., & Nizet, V. (2018) · Clinical Infectious Diseases · doi:10.1093/cid/ciy557 · Cited by 39
The complement system, toll-like receptors and inflammasomes in host defense: three musketeers’ one target
Kumar, V. (2019) · International Reviews of Immunology · doi:10.1080/08830185.2019.1609962 · Cited by 39
Interleukin (IL)-1β and IL-10 Host Responses in Patients With Staphylococcus aureus Bacteremia Determined by Antimicrobial Therapy
Volk, C. F., Burgdorf, S., Edwardson, G., Nizet, V., Sakoulas, G., & Rose, W. E. (2019) · Clinical Infectious Diseases · doi:10.1093/cid/ciz686 · Cited by 39
De‐ O ‐acetylation of peptidoglycan regulates glycan chain extension and affects in vivo survival of N eisseria meningitidis
Veyrier, F. J., Williams, A. H., Mesnage, S., Schmitt, C., Taha, M., & Boneca, I. G. (2013) · Molecular Microbiology · doi:10.1111/mmi.12153 · Cited by 37
Inhibitory Role for d -Alanylation of Wall Teichoic Acid in Activation of Insect Toll Pathway by Peptidoglycan of Staphylococcus aureus
Tabuchi, Y., Shiratsuchi, A., Kurokawa, K., Gong, J. H., Sekimizu, K., Lee, B. L., & Nakanishi, Y. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000625 · Cited by 37
Immunomodulatory effects of pCramoll and rCramoll on peritoneal exudate cells (PECs) infected and non-infected with Staphylococcus aureus
da Silva, L. C. N., Alves, N. M. P., de Castro, M. C. A. B., Pereira, V. R. A., Varejão, N., Coelho, L. C. B. B., de Figueiredo, R. C. B. Q., & Correia, M. T. D. S. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.09.045 · Cited by 35
Fosfomycin Protects Mice From Staphylococcus aureus Pneumonia Caused by α-Hemolysin in Extracellular Vesicles by Inhibiting MAPK-Regulated NLRP3 Inflammasomes
An, Y., Wang, Y., Zhan, J., Tang, X., Shen, K., Shen, F., Wang, C., Luan, W., Wang, X., Wang, X., et al. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00253 · Cited by 35
Staphylococcus aureus in Inflammation and Pain: Update on Pathologic Mechanisms
Rasquel-Oliveira, F. S., Ribeiro, J. M., Martelossi-Cebinelli, G., Costa, F., Nakazato, G., Casagrande, R., & Verri, W. A., Jr. (2025) · Pathogens · doi:10.3390/pathogens14020185 · Cited by 41
The Innate Immune Response Against Staphylococcus aureus
Bekeredjian‐Ding, I., Stein, C., & Uebele, J. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_5004 · Cited by 38
Inflammatory properties of antibiotic-treated bacteria
Wolf, A. J., Liu, G. Y., & Underhill, D. M. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.4mr0316-153rr · Cited by 33
Self-citation
Transcriptional analyses provide new insight into the late-stage immune response of a diseased Caribbean coral
Fuess, L. E., Mann, W. T., Jinks, L. R., Brinkhuis, V., & Mydlarz, L. D. (2018) · Royal Society Open Science · doi:10.1098/rsos.172062 · Cited by 34
Cloning and immune characterization of the c-type lysozyme gene in red-spotted grouper, Epinephelus akaara
Mai, W., Liu, P., Chen, H., & Zhou, Y. (2013) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2013.11.002 · Cited by 34
Inflammasome activation by Gram-positive bacteria: Mechanisms of activation and regulation
Keestra-Gounder, A. M., & Nagao, P. E. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1075834 · Cited by 33
The inflammasome regulatory pathway and infections: Role in pathophysiology and clinical implications
Osawa, R., Williams, K. L., & Singh, N. (2010) · Journal of Infection · doi:10.1016/j.jinf.2010.10.002 · Cited by 34
Processed human amniotic fluid retains its antibacterial activity
Mao, Y., Pierce, J., Singh‐Varma, A., Boyer, M. J., Kohn, J., & Reems, J.-A. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1812-8 · Cited by 32
Frontline Science: Staphylococcus aureus promotes receptor-interacting protein kinase 3- and protease-dependent production of IL-1β in human neutrophils
Kremserová, S., & Nauseef, W. M. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.4hi0918-346r · Cited by 30
An In Vitro Mixed Infection Model With Commensal and Pathogenic Staphylococci for the Exploration of Interspecific Interactions and Their Impacts on Skin Physiology
Kohda, K., Li, X., Soga, N., Nagura, R., Tie, D., Nakajima, S., Nakagawa, I., Ito, M., & Ikeuchi, A. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.712360 · Cited by 32
TLR2 and caspase-1 signaling are critical for bacterial containment but not clearance during craniotomy-associated biofilm infection
Aldrich, A. L., Heim, C. E., Shi, W., Fallet, R. W., Duan, B., & Kielian, T. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01793-6 · Cited by 29
Bacterial infection reinforces host metabolic flux from arginine to spermine for NLRP3 inflammasome evasion
Jiang, J., Wang, W., Sun, F., Zhang, Y., Liu, Q., & Yang, D. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108832 · Cited by 29
Diverse Control Mechanisms of the Interleukin-1 Cytokine Family
Evavold, C. L., & Kagan, J. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.910983 · Cited by 34
Impact of cell wall peptidoglycan O- acetylation on the pathogenesis of Staphylococcus aureus in septic arthritis
Baranwal, G., Mohammad, M., Jarneborn, A., Reddy, B. R., Golla, A., Chakravarty, S., Biswas, L., Götz, F., Shankarappa, S. A., Jin, T., et al. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.08.002 · Cited by 28
Self-citation
Adipose tissue knockdown of lysozyme reduces local inflammation and improves adipogenesis in high-fat diet-fed mice
Latorre, J., Lluch, A., Ortega, F. J., Gavaldà‐Navarro, A., Comas, F., Morón‐Ros, S., Rodrı́guez, A., Becerril, S., Villarroya, F., Frühbeck, G., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105486 · Cited by 30
Targeting fundamental pathways to disrupt Staphylococcus aureus survival: clinical implications of recent discoveries
Thomsen, I. P., & Liu, G. Y. (2018) · JCI Insight · doi:10.1172/jci.insight.98216 · Cited by 27
Self-citation
NOD1 and NOD2: Essential Monitoring Partners in the Innate Immune System
Li, Z., & Shang, D. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46090561 · Cited by 29
Staphylococcus aureus Adenosine Inhibits sPLA2-IIA–Mediated Host Killing in the Airways
Pernet, E., Brunet, J., Guillemot, L., Chignard, M., Touqui, L., & Wu, Y. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402665 · Cited by 25
Targeting the host–pathogen interface for treatment of Staphylococcus aureus infection
Park, B., & Liu, G. Y. (2011) · Seminars in Immunopathology · doi:10.1007/s00281-011-0297-1 · Cited by 25
Self-citation
Future Perspective on Host–Pathogen Interactions During Bacterial Biofilm Formation within the Nasopharynx
Blanchette, K. A., & Orihuela, C. J. (2012) · Future Microbiology · doi:10.2217/fmb.11.160 · Cited by 24
Adenosine synthase A contributes to recurrent Staphylococcus aureus infection by dampening protective immunity
Deng, J. P., Zhang, B., Chu, H., Wang, X., Wang, Y., Gong, H., Li, R., Yang, D., Li, C., Dou, Y., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103505 · Cited by 24
The Inflammasome and the Epidermal Growth Factor Receptor (EGFR) Are Involved in the Staphylococcus aureus-Mediated Induction of IL-1alpha and IL-1beta in Human Keratinocytes
Simanski, M., Rademacher, F., Schröder, L. C., Gläser, R., & Harder, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147118 · Cited by 24
Osteopontin is essential for IL‐1β production and apoptosis in peri‐implantitis
Che, C., Liu, J., Yang, J., Ma, L., Bai, N., & Zhang, Q. (2018) · Clinical Implant Dentistry and Related Research · doi:10.1111/cid.12592 · Cited by 24
Lose the battle to win the war: bacterial strategies for evading host inflammasome activation
Higa, N., Toma, C., Nohara, T., Nakasone, N., Takaesu, G., & Suzuki, T. (2013) · Trends in Microbiology · doi:10.1016/j.tim.2013.04.005 · Cited by 23
PINK1/parkin-mediated mitophagy alleviates Staphylococcus aureus-induced NLRP3 inflammasome and NF-κB pathway activation in bovine mammary epithelial cells
Liu, K., Zhou, X., Fang, L., Dong, J., Cui, L., Li, J., Meng, X., Zhu, G., Li, J., & Wang, H. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109200 · Cited by 24
Intracellular bacteriolysis contributes to pathogenicity of Staphylococcus aureus by exacerbating AIM2-mediated inflammation and necroptosis
Feng, S., Yang, Y., Liu, Z., Chen, W., Du, C., Hu, G., Yu, S.-X., Song, P., & Miao, J. (2022) · Virulence · doi:10.1080/21505594.2022.2127209 · Cited by 23
PINK1/Parkin‐mediated mitophagy enhances the survival of Staphylococcus aureus in bovine macrophages
Zhou, X., Liu, K., Li, J., Cui, L., Dong, J., Li, J., Meng, X., Zhu, G., & Wang, H. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17664 · Cited by 22
Peptidoglycan-induced modulation of metabolic and inflammatory responses
Wolf, A. J. (2023) · Immunometabolism · doi:10.1097/in9.0000000000000024 · Cited by 22
Self-citation
Cloning and expression analysis of c-type lysozyme gene in golden pompano, Trachinotus ovatus
Zhou, C., Lin, H., Huang, Z., Wang, J., Wang, Y., & Yu, W. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.04.137 · Cited by 22
Role of JAK-STAT signaling in maturation of phagosomes containing Staphylococcus aureus
Zhu, F., Zhou, Y., Jiang, C., & Zhang, X. (2015) · Scientific Reports · doi:10.1038/srep14854 · Cited by 22
The impact of α-toxin on host cell plasma membrane permeability and cytokine expression during human blood infection by CA-MRSA USA300
Nygaard, T. K., Pallister, K. B., Zurek, O. W., & Voyich, J. M. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0213080 · Cited by 21
LOX-1 is involved in IL-1β production and extracellular matrix breakdown in dental peri-implantitis
Che, C., Liu, J., Ma, L., Xu, H., Bai, N., & Zhang, Q. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.09.003 · Cited by 21
Inactivation of inflammasomes by pathogens regulates inflammation
Garib, F. Y., Ризопулу, А. П., Kuchmiy, A. A., & Garib, V. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916110109 · Cited by 22
Biomimetic-gasdermin-protein-expressing nanoplatform mediates tumor-specific pyroptosis for cancer immunotherapy
Wang, X., Wang, Y., Zhang, W., Zhu, X., Liu, Z., Liu, M., Liu, S., Li, B., Chen, Y., Wang, Z., et al. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.01.021 · Cited by 20
Peptidoglycan Acetylation of Campylobacter jejuni Is Essential for Maintaining Cell Wall Integrity and Colonization in Chicken Intestines
Iwata, T., Watanabe, A., Kusumoto, M., & Akiba, M. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02068-16 · Cited by 20
Staphylococcus aureus induces cell-surface expression of immune stimulatory NKG2D ligands on human monocytes
Mellergaard, M., Høgh, R. I., Lund, A., Aldana, B. I., Guérillot, R., Møller, S. H., Hayes, A. S., Panagiotopoulou, N., Frimand, Z., Jepsen, S. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012673 · Cited by 18
Plasmacytoid Dendritic Cells: Neglected Regulators of the Immune Response to Staphylococcus aureus
Bekeredjian‐Ding, I., Greil, J., Ammann, S., & Parčina, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00238 · Cited by 21
VraSR has an important role in immune evasion of Staphylococcus aureus with low level vancomycin resistance
Gao, C., Dai, Y., Chang, W., Fang, C., Wang, Z., & Ma, X. (2019) · Microbes and Infection · doi:10.1016/j.micinf.2019.04.003 · Cited by 19
Synergistic Effects of Influenza and Staphylococcus aureus Toxins on Inflammation Activation and Cytotoxicity in Human Monocytic Cell Lines
Jeannoël, M., Casalegno, J., Ottmann, M., Badiou, C., Dumitrescu, O., Lina, B., & Lina, G. (2018) · Toxins · doi:10.3390/toxins10070286 · Cited by 17
Host-directed therapy against tuberculosis: Concept and recent developments
Udinia, S., Suar, M., & Kumar, D. (2023) · Journal of Biosciences · doi:10.1007/s12038-023-00374-y · Cited by 15
TLR4 (not TLR2) dominate cognate TLR activity associated with CoCrMo implant particles
Samelko, L., Landgraeber, S., McAllister, K., Jacobs, J. J., & Hallab, N. J. (2016) · Journal of Orthopaedic Research® · doi:10.1002/jor.23368 · Cited by 16
Bacterial subversion of NLR-mediated immune responses
Kienes, I., Johnston, E. L., Bitto, N. J., Kaparakis‐Liaskos, M., & Kufer, T. A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.930882 · Cited by 16
Intracellular Staphylococcus aureus-induced NF-κB activation and proinflammatory responses of P815 cells are mediated by NOD2
Xie, X., Wang, L., 龚凤云, Xia, C., Chen, J., Song, Y., Shen, A., & Song, J. (2012) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-012-0055-1 · Cited by 15
Staphylococcus aureus : a model for bacterial cell biology and pathogenesis
Pinho, M. G., Götz, F., & Peschel, A. (2025) · Journal of Bacteriology · doi:10.1128/jb.00106-25 · Cited by 16
Self-citation
The hidden base of the iceberg: gut peptidoglycome dynamics is foundational to its influence on the host
Wheeler, R., & Boneca, I. G. (2024) · Gut Microbes · doi:10.1080/19490976.2024.2395099 · Cited by 16
Francisella tularensis Live Vaccine Strain Folate Metabolism and Pseudouridine Synthase Gene Mutants Modulate Macrophage Caspase-1 Activation
Ulland, T. K., Janowski, A. M., Buchan, B. W., Faron, M. L., Cassel, S. L., Jones, B. D., & Sutterwala, F. S. (2012) · Infection and Immunity · doi:10.1128/iai.00991-12 · Cited by 14
Development of a High Throughput Screen for the Identification of Inhibitors of Peptidoglycan O-Acetyltransferases, New Potential Antibacterial Targets
Brott, A. S., Jones, C. S., & Clarke, A. J. (2019) · Antibiotics · doi:10.3390/antibiotics8020065 · Cited by 14
The Relevance of IL-1-Signaling in the Protection against Gram-Positive Bacteria
Midiri, A., Mancuso, G., Beninati, C., Gerace, E., & Biondo, C. (2021) · Pathogens · doi:10.3390/pathogens10020132 · Cited by 14
Infectious (Non)tolerance--Frustrated Commensalism Gone Awry?Preprint
Nussbaum, J. C., & Locksley, R. M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007328 · Cited by 14
In vitro PCR verification that lysozyme inhibits nucleic acid replication and transcription
Liu, L., Jia, X., Zhao, X., Li, T., Luo, Z., Deng, R., Peng, B., Mao, D., Liu, H., & Zheng, Q. (2023) · Scientific Reports · doi:10.1038/s41598-023-33228-6 · Cited by 12
Differential survival of Staphylococcal species in macrophages
Bayer, J., Becker, J., Liu, X., Gritsch, L., Daiber, E., Korn, N., Oesterhelt, F., Fraunholz, M. J., Weber, A. N. R., & Wolz, C. (2023) · Molecular Microbiology · doi:10.1111/mmi.15184 · Cited by 13
Lysozyme: an endogenous antimicrobial protein with potent activity against extracellular, but not intracellular Mycobacterium tuberculosis
Maier, F. I., Klinger, D., Grieshober, M., Noschka, R., Rodríguez, A., Wiese, S., Forssmann, W., Ständker, L., & Stenger, S. (2024) · Medical Microbiology and Immunology · doi:10.1007/s00430-024-00793-0 · Cited by 13
The Pneumococcal Cell Wall
Gisch, N., Peters, K., Zähringer, U., & Vollmer, W. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-410530-0.00008-9 · Cited by 13
Involvement of caspase‐1 in inflammasomes activation and bacterial clearance in S. aureus ‐infected osteoblast‐like MG ‐63 cells
Leite, E. L., Gautron, A., Deplanche, M., Nicolas, A., Ossemond, J., Nguyen, M., Carmo, F. L. R. D., Gilot, D., Azevedo, V., Götz, F., et al. (2020) · Cellular Microbiology · doi:10.1111/cmi.13204 · Cited by 13
Self-citation
Strategies of bacterial detection by inflammasomes
Jastrab, J. B., & Kagan, J. C. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.03.009 · Cited by 14
N-acetylmuramic acid triggers anti-inflammatory capacity in LPS-induced RAW 264.7 cells and mice
Wu, Z. F., Pan, D., Guo, Y., & Zeng, X. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2014.12.048 · Cited by 12
TLR and NLRP3 inflammasome expression deregulation in macrophages of adult rats subjected to neonatal malnutrition and infected with methicillin-resistant Staphylococcus aureus
de Morais, N. G., da Costa, T. B., de Lira, J. M. B., de Albuquerque, S. D. C. G., Pereira, V. R. A., de Paiva-Cavalcanti, M., & de Castro, C. M. M. B. (2016) · Nutrition · doi:10.1016/j.nut.2016.06.005 · Cited by 12
The CD36 and SR-A/CD204 scavenger receptors fine-tune Staphylococcus aureus-stimulated cytokine production in mouse macrophages
Peruń, A., Gębicka, M., Biedroń, R., Skalska, P., & Józefowski, S. (2022) · Cellular Immunology · doi:10.1016/j.cellimm.2022.104483 · Cited by 11
Arterial Catheterization and Infection: Toll‐like Receptors in Defense against Microorganisms and Therapeutic Implications
Hambsch, Z. J., Kerfeld, M. J., Kirkpatrick, D. R., McEntire, D., Reisbig, M. D., Youngblood, C. F., & Agrawal, D. K. (2015) · Clinical and Translational Science · doi:10.1111/cts.12320 · Cited by 11
Antimicrobial activity of Pityrocarpa monilifomis leaves and its capacity to enhance the activity of four antibiotics against Staphylococcus aureus strains
Juliette, F. V. D. S., s, C. U. N. D. S. L., Isabel, R. D. S. A., Alex, re, G. D. S., Alex, re, J. M., Janete, M. D. A., Maria, T. D. S. C., & rcia, V. D. S. M. A. (2013) · Journal of Medicinal Plants Research · doi:10.5897/jmpr2013.2591 · Cited by 11
Genetic Determinants Enabling Medium-Dependent Adaptation to Nafcillin in Methicillin-Resistant Staphylococcus aureus
Salazar, M. J., Machado, H., Dillon, N. A., Tsunemoto, H., Szubin, R., Dahesh, S., Pogliano, J., Sakoulas, G., Palsson, B. Ø., Nizet, V., et al. (2020) · mSystems · doi:10.1128/msystems.00828-19 · Cited by 13
Staphylococcus aureus manipulates osteocytes to cause persistent chronic osteomyelitis and antibiotic resistance via pyroptosis pathway suppression
Cai, Y., Hu, H., Chen, Y., Li, J., Zhang, C., Yuan, X., Li, W., Huang, C., Lin, Y., Zhang, Z., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101295 · Cited by 9

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