TY - JOUR
T1 - Identification of a new OmpA-like protein in Neisseria gonorrhoeae involved in the binding to human epithelial cells and in vivo colonization
AU - Serino, Laura
AU - Nesta, Barbara
AU - Leuzzi, Rosanna
AU - Fontana, Maria Rita
AU - Monaci, Elisabetta
AU - Mocca, Brian T.
AU - Cartocci, Elena
AU - Masignani, Vega
AU - Jerse, Ann E.
AU - Rappuoli, Rino
AU - Pizza, Mariagrazia
PY - 2007/6
Y1 - 2007/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34249801803&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2958.2007.05745.x
DO - 10.1111/j.1365-2958.2007.05745.x
M3 - Article
C2 - 17542928
AN - SCOPUS:34249801803
SN - 0950-382X
VL - 64
SP - 1391
EP - 1403
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 5
ER -