Journal NLM ID:9706653 WWW link:http://mmbr.asm.org/content/62/1/130.long Publisher: Washington, DC: American Society for Microbiology Correspondence: micwlcttuhsc.edu Institutions: Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock, USA, Department of Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA, Departamento de Microbiologı́a y Ecologı́a, Facultad de Farmacia, Universitat de Valencia, Valencia, Spain
The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was initially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis
Comments, role: review; backbone chains; mannose polymers are linked to the protein moiety through asparagine by N-glycosidic bonds through two GlcNAc (ID 40761)
Related record ID(s): 40527, 40759, 40760, 40761 NCBI Taxonomy refs (TaxIDs):5476 Reference(s) to other database(s): GTC:G63401UQ Show glycosyltransferases
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