Structure-function studies of the Neisseria gonorrhoeae major outer membrane porin

Adrienne Chen, H. Steven Seifert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The major outer membrane porin (PorB) expressed by Neisseria gonorrhoeae plays multiple roles during infection, in addition to its function as an outer membrane pore. We have generated a panel of mutants of N. gonorrhoeae strain FA1090 expressing a variety of mutant porB genes that all function as porins. We identified multiple regions of porin that are involved in its binding to the complement regulatory factors C4b-binding protein and factor H and confirmed that the ability to bind at least one factor is required for FA1090 to survive the bactericidal effects of human serum. We tested the ability of these mutants to inhibit both apoptosis and the oxidative burst in polymorphonuclear leukocytes but were unable to identify the porin domains required for either function. This study has identified nonessential porin domains and some potentially essential portions of the protein and has further expanded our understanding of the contribution of the porin domains required for complement regulation.

Original languageEnglish (US)
Pages (from-to)4383-4391
Number of pages9
JournalInfection and immunity
Volume81
Issue number12
DOIs
StatePublished - Dec 2013

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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