1887

Abstract

The opportunistic pathogen colonizes the oral cavity and gastrointestinal tract. Adherence to host cells, extracellular matrix and salivary glycoproteins that coat oral surfaces, including prostheses, is an important prerequisite for colonization. In addition, interactions of with commensal oral streptococci are suggested to promote retention and persistence of fungal cells in mixed-species communities. The hyphal filament specific cell wall protein Als3, a member of the Als protein family, is a major determinant in adherence. Here, we utilized site-specific in-frame deletions within Als3 expressed on the surface of heterologous to determine regions involved in interactions of Als3 with . N-terminal region amino acid residue deletions Δ166–225, Δ218–285, Δ270–305 and Δ277–286 were each effective in inhibiting binding of to Als3. In addition, these deletions differentially affected biofilm formation, hydrophobicity, and adherence to silicone and human tissue proteins. Deletion of the central repeat domain (Δ434–830) did not significantly affect interaction of Als3 with SspB protein, but affected other adherence properties and biofilm formation. Deletion of the amyloid-forming region (Δ325–331) did not affect interaction of Als3 with SspB adhesin, suggesting this interaction was amyloid-independent. These findings highlighted the essential function of the N-terminal domain of Als3 in mediating the interaction of with , and suggested that amyloid formation is not essential for the inter-kingdom interaction.

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2015-01-01
2024-04-24
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