Identification of a 43-kDa outer-membrane protein as an adhesin in Aeromonas caviae.

Aeromonas spp. are associated with intestinal and extra-intestinal infections. However, the virulence factors of A. caviae remain, for the most part, poorly known. This study examined the interactions involved in the adherence of A. caviae isolates Ae56, Ae391 and Ae398 to HEp-2 cells. All strains expressed high levels of aggregative adherence. Maximum adhesion occurred with bacteria grown at 22 degrees C, but transmission electron microscopy did not reveal the presence of fimbrial structures on the bacterial cell surface. Outer-membrane proteins (OMPs) extracted from isolate Ae398, grown at 22 degrees C and 37 degrees C, showed similar SDS-PAGE protein profiles. Most proteins were < 60 kDa. A major 43-kDa protein was seen only in the boiled OMP extract. The biotinylated 43-kDa protein bound specifically to HEp-2 cells. Microbeads coated with the 43-kDa protein were also adherent to HEp-2 cells, and anti-43-kDa protein antibody blocked adherence of 43-kDa protein-coated latex beads. These data suggest that the 43-kDa OMP functions as an adhesin in A. caviae.