The Neisseria type 2 IgA1 protease cleaves LAMP1 and promotes survival of bacteria within epithelial cells

Lan Lin, Patricia Ayala, Jason Larson, Martha Mulks, Minoru Fukuda, Sven R. Carlsson, Caroline Enns, Magdalene So

Research output: Contribution to journalArticle

113 Scopus citations

Abstract

Infection of human epithelial cells by Neisseria meningitidis (MC) and Neisseria gonorrhoeae (GC) increases the rate of degradation of LAMP1, a major integral membrane glycoprotein of late endosomes and lysosomes. Several lines of evidence indicate that the neisserial IgA1 protease is directly responsible for this LAMP1 degradation. LAMP1 contains an IgA1-like hinge region with potential cleavage sites for the neisserial type 1 and type 2 IgA1 proteases. Neisserial type 2 IgA1 protease cleaves purified LAMP1 in vitro. Unlike its wild-type isogenic parent, an Iga- mutant of N. gonorrhoeae cannot effect LAMP1 turnover and its growth in epithelial cells is dramatically reduced. Thus, IgA1 protease cleavage of LAMP1 promotes intracellular survival of pathogenic Neisseria spp.

Original languageEnglish (US)
Pages (from-to)1083-1094
Number of pages12
JournalMolecular Microbiology
Volume24
Issue number5
DOIs
StatePublished - Jan 1 1997

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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