ArticleFrontiers in microbiology2014
A proposed mechanism for the interaction between the Candida albicans Als3 adhesin and streptococcal cell wall proteins.
Article in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
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- Adhesion ofFrontiers in cellular and infection microbiology · 2020Article
- Fungal-Bacterial Interactions in Health and Disease.Pathogens (Basel, Switzerland) · 2019Review
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- Tipping the Balance:Journal of fungi (Basel, Switzerland) · 2018Review
- Antigen I/II mediates interactions between Streptococcus mutans and Candida albicans.Molecular oral microbiology · 2018Article
- Coassociation between Group B Streptococcus and Candida albicans Promotes Interactions with Vaginal Epithelium.Infection and immunity · 2018Article
- Development and regulation of single- and multi-species Candida albicans biofilms.Nature reviews. Microbiology · 2018Review
- S. oralis activates the Efg1 filamentation pathway in C. albicans to promote cross-kingdom interactions and mucosal biofilms.Virulence · 2017Article
- Article
- Candida albicans Agglutinin-Like Sequence (Als) Family Vignettes: A Review of Als Protein Structure and Function.Frontiers in microbiology · 2016Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
C. albicans binds various bacteria, including the oral commensal Streptococcus gordonii. Published reports documented the role of C. albicans Als3 and S. gordonii SspB in this interaction, and the importance of the Als N-terminal domain (NT-Als) in C. albicans adhesion. Here, we demonstrate that Als1 also binds S. gordonii. We also describe use of the NT-Als crystal structure to design mutations that precisely disrupt peptide-binding cavity (PBC) or amyloid-forming region (AFR) function in Als3. C. albicans displaying Als3 PBC mutant proteins showed significantly reduced binding to S. gordonii; mutation of the AFR did not affect the interaction. These observations present an enigma: the Als PBC binds free C termini of ligands, but the SspB C terminus is covalently linked to peptidoglycan and thus unavailable as a ligand. These observations and the predicted SspB elongated structure suggest that partial proteolysis of streptococcal cell wall proteins is necessary for recognition by Als adhesins.
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