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Identification of a new OmpA‐like protein in Neisseria gonorrhoeae involved in the binding to human epithelial cells and in vivo colonization
Author(s) -
Serino Laura,
Nesta Barbara,
Leuzzi Rosanna,
Fontana Maria Rita,
Monaci Elisabetta,
Mocca Brian T.,
Cartocci Elena,
Masignani Vega,
Jerse Ann E.,
Rappuoli Rino,
Pizza Mariagrazia
Publication year - 2007
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 - 10.1111/j.1365-2958.2007.05745.x
Subject(s) - biology , neisseria gonorrhoeae , bacterial outer membrane , virulence , microbiology and biotechnology , virulence factor , escherichia coli , neisseria , enterobacteriaceae , mutant , secretion , membrane protein , bacteria , gene , biochemistry , genetics , membrane
Summary Outer membrane protein As (OmpAs) are highly conserved proteins within the Enterobacteriaceae family. OmpA contributes to the maintenance of structural membrane integrity and invasion into mammalian cells. In Escherichia coli K1 OmpA also contributes to serum resistance and is involved in the virulence of the bacterium. Here we describe the identification of an OmpA‐like protein in Neisseria gonorrhoeae (Ng‐OmpA). We show that the gonococcal OmpA‐like protein, similarly to E. coli OmpA, plays a significant role in the adhesion and invasion into human cervical carcinoma and endometrial cells and is required for entry into macrophages and intracellular survival. Furthermore, the isogenic knockout ompA mutant demonstrates reduced recovery in a mouse model of infection when compared with the wild‐type strain, suggesting that Ng‐OmpA plays an important role in the in vivo colonization. All together, these data suggest that the newly identified surface exposed protein Ng‐OmpA represents a novel virulence factor of gonococcus.