Linked Life Data

11800271

Source:http://linkedlifedata.com/resource/pubmed/id/11800271

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-1-21
pubmed:abstractText
Fungal cell wall N-linked glycans have been studied most extensively in Saccharomyces cerevisiae and in Candida albicans. The glycans are located on the fungal cell surface in the form of phosphomannoprotein complexes and the amount of glycosylation is influenced both by genetics and environmental factors. The glycans, which are comprised mostly of mannan, are important in fungal-host interactions, as they make first contact with the immune system. Initial N-linked glycosylation events take place in the endoplasmic reticulum and are conserved throughout all eukaryotes, but yeasts are capable of additional glycosylation that may result in a glycan comprised of more than 200 mannose units. In C. albicans, the glycan can be delineated into an inner mannan core, which is similar to mammalian glycoproteins, an alpha-linked mannan backbone with alpha-oligomannosyl side chains, and beta(1,2)-oligomannosides which are phosphodiester linked to the alpha-mannan. Both the beta-oligomannosides, which make up the acid-labile part of the phosphomannan complex, and alpha-oligomannosides, which make up the acid-stable part of the complex, serve as adhesins in the attachment of C. albicans yeast cells to host splenic and lymph node macrophages. The beta-oligomannosides can induce release of tumour necrosis factor (TNF)-alpha, and antibodies specific to certain beta-oligomannosides enhance host resistance to various forms of candidiasis. The importance of the N-linked glycans in fungal-host interactions provides rationale for further studies, which may well lead to effective immunotherapeutic strategies for prevention and, possibly, treatment of disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1369-3786
pubmed:author
pubmed:issnType
Print
pubmed:volume
39 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-86
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
N-glycosylation of yeast, with emphasis on Candida albicans.
pubmed:affiliation
Department of Microbiology, Montana State University, Bozeman 59717, USA. jcutler@montana.edu
pubmed:publicationType
Journal Article, Review