Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis

Abstract

The direct binding of bacteria to platelets is a central interaction in the pathogenesis of infective endocarditis. GspB is a serine-rich, cell wall glycoprotein of Streptococcus gordonii that mediates the binding of this organism to human platelets in vitro. To assess the contribution of this adhesin to the pathogenesis of endocarditis, we compared the virulence of S. gordonii M99 (which expresses GspB) with an isogenic, gspB mutant (PS846) in two rat models of endovascular infection. In the first group of experiments, animals were infected intravenously with M99 or PS846, and sacrificed 72 h later, to assess levels of bacteria within cardiac vegetations, kidneys, and spleens. When inoculated with 10(5)CFU, rats infected with PS846 had significantly lower densities of organisms within vegetations (mean: 3.84 log(10)CFU/g) as compared with M99-infected rats (6.67 log(10)CFU/g; P<0.001). Marked differences were also seen in rats co-infected with M99 and PS846, at a 1:1 ratio. While M99 was found at high levels within vegetations, kidneys and spleens (mean log(10)CFU/g: 6.62, 5.07 and 4.18, respectively) PS846 was not detected within these tissues. Thus, platelet binding by GspB appears to be a major interaction in the pathogenesis of endocarditis due to S. gordonii.

Fig. 1

Effect of GspB expression on virulence. Levels of bacteria (mean ± SD) in vegetations, kidneys, and spleens recovered from rats infected with either M99 or PS846. *P≤0.05.

Fig. 2

Effect of GspB expression on rats co-infected with M99 and PS846. PS846 could not be detected in any tissues harvested. See text for lower limits of detection. *P < 0.0001.