Unknown

Dataset Information

0

Host cell invasion and virulence mediated by Candida albicans Ssa1.


ABSTRACT: Candida albicans Ssa1 and Ssa2 are members of the HSP70 family of heat shock proteins that are expressed on the cell surface and function as receptors for antimicrobial peptides such as histatins. We investigated the role of Ssa1 and Ssa2 in mediating pathogenic host cell interactions and virulence. A C. albicans ssa1?/? mutant had attenuated virulence in murine models of disseminated and oropharyngeal candidiasis, whereas an ssa2?/? mutant did not. In vitro studies revealed that the ssa1?/? mutant caused markedly less damage to endothelial cells and oral epithelial cell lines. Also, the ssa1?/? mutant had defective binding to endothelial cell N-cadherin and epithelial cell E-cadherin, receptors that mediate host cell endocytosis of C. albicans. As a result, this mutant had impaired capacity to induce its own endocytosis by endothelial cells and oral epithelial cells. Latex beads coated with recombinant Ssa1 were avidly endocytosed by both endothelial cells and oral epithelial cells, demonstrating that Ssa1 is sufficient to induce host cell endocytosis. These results indicate that Ssa1 is a novel invasin that binds to host cell cadherins, induces host cell endocytosis, and is critical for C. albicans to cause maximal damage to host cells and induce disseminated and oropharyngeal disease.

SUBMITTER: Sun JN 

PROVIDER: S-EPMC2978716 | BioStudies | 2010-01-01T00:00:00Z

REPOSITORIES: biostudies

Similar Datasets

1000-01-01 | S-EPMC3435201 | BioStudies
2007-01-01 | S-EPMC1802757 | BioStudies
1000-01-01 | S-EPMC3870263 | BioStudies
2017-01-01 | S-EPMC5362030 | BioStudies
2009-01-01 | S-EPMC4098847 | BioStudies
1000-01-01 | S-EPMC1395393 | BioStudies
2011-01-01 | S-EPMC3188548 | BioStudies
2009-01-01 | S-EPMC2738641 | BioStudies
2009-01-01 | S-EPMC2756863 | BioStudies
1000-01-01 | S-EPMC1326393 | BioStudies