ArticleThe Journal of biological chemistry2012
Neisseria gonorrhoeae virulence factor NG1686 is a bifunctional M23B family metallopeptidase that influences resistance to hydrogen peroxide and colony morphology.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- The Neisseria gonorrhoeae type IV pilus promotes resistance to hydrogen peroxide- and LL-37-mediated killing by modulating the availability of intracellular, labile iron.PLoS pathogens · 2022Article
- BB0761, a MepM homolog, contributes to Borrelia burgdorferi cell division and mammalian infectivity.Molecular microbiology · 2022Article
- Comparative Genomics ofmSystems · 2021Article
- Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.PloS one · 2021Article
- Bacterial Infections Affect Male Fertility: A Focus on the Oxidative Stress-Autophagy Axis.Frontiers in cell and developmental biology · 2021Review
- Diversification of LytM Protein Functions in Polar Elongation and Cell Division ofFrontiers in microbiology · 2021Article
- Article
- Transcriptional regulation of a gonococcal gene encoding a virulence factor (L-lactate permease).PLoS pathogens · 2019Article
- The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment Release.Frontiers in microbiology · 2019Review
- The lytic transglycosylase MltB connects membrane homeostasis and in vivo fitness of Acinetobacter baumannii.Molecular microbiology · 2018Article
- Pathogenesis of Neisseria gonorrhoeae in the female reproductive tract: neutrophilic host response, sustained infection, and clinical sequelae.Current opinion in hematology · 2018Review
- Two lytic transglycosylases in Neisseria gonorrhoeae impart resistance to killing by lysozyme and human neutrophils.Cellular microbiology · 2017Article
- Analyzing Neisseria gonorrhoeae Pilin Antigenic Variation Using 454 Sequencing Technology.Journal of bacteriology · 2016Article
- Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae.The Journal of biological chemistry · 2016Article
- The Gonococcal NlpD Protein Facilitates Cell Separation by Activating Peptidoglycan Cleavage by AmiC.Journal of bacteriology · 2015Article
- Article
- Quantitative proteomics of the Neisseria gonorrhoeae cell envelope and membrane vesicles for the discovery of potential therapeutic targets.Molecular & cellular proteomics : MCP · 2014Article
- Article
- Peptidoglycan at its peaks: how chromatographic analyses can reveal bacterial cell wall structure and assembly.Molecular microbiology · 2013Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Symptomatic gonococcal infection, caused exclusively by the human-specific pathogen Neisseria gonorrhoeae (the gonococcus), is characterized by the influx of polymorphonuclear leukocytes (PMNs) to the site of infection. Although PMNs possess a potent antimicrobial arsenal comprising both oxidative and non-oxidative killing mechanisms, gonococci survive this interaction, suggesting that the gonococcus has evolved many defenses against PMN killing. We previously identified the NG1686 protein as a gonococcal virulence factor that protects against both non-oxidative PMN-mediated killing and oxidative killing by hydrogen peroxide. In this work, we show that deletion of ng1686 affects gonococcal colony morphology but not cell morphology and that overexpression of ng1686 does not confer enhanced survival to hydrogen peroxide on gonococci. NG1686 contains M23B endopeptidase active sites found in proteins that cleave bacterial cell wall peptidoglycan. Strains of N. gonorrhoeae expressing mutant NG1686 proteins with substitutions in many, but not all, conserved metallopeptidase active sites recapitulated the hydrogen peroxide sensitivity and altered colony morphology of the Δng1686 mutant strain. We showed that purified NG1686 protein degrades peptidoglycan in vitro and that mutations in many conserved active site residues abolished its degradative activity. Finally, we demonstrated that NG1686 possesses both dd-carboxypeptidase and endopeptidase activities. We conclude that the NG1686 protein is a M23B peptidase with dual activities that targets the cell wall to affect colony morphology and resistance to hydrogen peroxide and PMN-mediated killing.
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