Neisseria gonorrhoeae virulence factor NG1686 is a bifunctional M23B family metallopeptidase that influences resistance to hydrogen peroxide and colony morphology.

The Journal of Biological Chemistry
Elizabeth A StohlH Steven Seifert

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 de...Continue Reading

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Citations

May 18, 2013·Molecular Microbiology·Samantha M DesmaraisKerwyn Casey Huang
Jul 7, 2016·Journal of Bacteriology·Ella RotmanH Steven Seifert
Nov 18, 2015·Journal of Bacteriology·Elizabeth A StohlH Steven Seifert
Jul 22, 2020·Andrologia·Ralf HenkelDavid Fisher
Sep 8, 2021·Frontiers in Microbiology·Wanda M Figueroa-CuilanPamela J B Brown
Nov 17, 2021·PloS One·Andrea Olga PapadopoulosBavesh Davandra Kana

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