Journal
FUTURE MICROBIOLOGY
Volume 10, Issue 10, Pages 1635-1648Publisher
FUTURE MEDICINE LTD
DOI: 10.2217/fmb.15.79
Keywords
adhesion; candidiasis; cell-surface glycoprotein; commensalism; host-fungus interaction; NMR; structural biology; x-ray crystallography
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Funding
- BBSRC UK [BB/K003887/1]
- Public Health Service Grant from the National Institute for Dental and Craniofacial Research, NIH [R01 DE14158]
- BBSRC [BB/K003887/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K003887/1] Funding Source: researchfish
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Candida albicans colonizes many host sites suggesting its interaction with diverse ligands. Candida albicans adhesion is mediated by a number of proteins including those in the Als (agglutinin-like sequence) family, which have been studied intensively. The recent solution of the Als binding domain structure ended years of speculation regarding the molecular mechanism for Als adhesive function. Als adhesins bind flexible C termini from a broad collection of proteins, providing the basis for adhesion to various cell types and perhaps for C. albicans broad tissue tropism. Understanding adhesive functions at the molecular level will reveal the sequence of events in C. albicans pathogenesis, from host recognition to complex interactions such as development of polymicrobial biofilms or disseminated disease.
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