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The Neisseria type 2 IgA1 protease cleaves LAMP1 and promotes survival of bacteria within epithelial cells
Author(s) -
Lin Lan,
Ayala Patricia,
Larson Jason,
Mulks Martha,
Fukuda Minoru,
Carlsson Sven R.,
Enns Caroline,
So Magdalene
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.4191776.x
Subject(s) - biology , proteases , protease , microbiology and biotechnology , neisseria , neisseria gonorrhoeae , glycoprotein , endosome , virology , bacteria , intracellular , biochemistry , enzyme , genetics
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 affect LAMP1 turnover and its growth in epithelial cells is dramatically reduced. Thus, IgA1 protease cleavage of LAMP1 promotes intracellular survival of pathogenic Neisseria spp.