Journal
FRONTIERS IN MICROBIOLOGY
Volume 5, Issue -, Pages -Publisher
FRONTIERS RESEARCH FOUNDATION
DOI: 10.3389/fmicb.2014.00564
Keywords
interkingdom interactions; streptococcal adhesin; SspB; Als3 adhesin; peptide-binding cavity; adhesion tethers; isopeptide bond
Categories
Funding
- Public Health Service grant from the National Institute of Dental and Craniofacial Research [DE14158]
- Biotechnology and Biological Sciences Research Council, UK [BB/K003887/1]
- Public Health Service Research Facilities Improvement Program grant [C06 RR16515-01]
- Biotechnology and Biological Sciences Research Council [BB/K003887/1, 983152] Funding Source: researchfish
- BBSRC [BB/K003887/1] Funding Source: UKRI
Ask authors/readers for more resources
C. albicans binds various bacteria, including the oral commensal Streptococcus gordonh. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available