Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-5-24
pubmed:abstractText
Clearance of Candida albicans from the oral cavity is thought to be mediated via specific receptor-ligand interactions between salivary constituents and the fungus. Since surfaces in the oral cavity are normally coated with a saliva-derived pellicle, specific interactions between salivary constituents and C. albicans may also contribute to adhesion of C. albicans to the oral mucosa and dental prostheses. Therefore, the purpose of this study was to identify salivary constituents to which C. albicans is capable of binding. A solid-phase overlay assay was used in which electrophoretically separated rat and human salivary constituents bound to membrane filters were incubated with radiolabelled C. albicans cells. C. albicans adhered to a single salivary component from each host. Correlation of cell-binding activity with specific monoclonal antibody (MAb)-binding activity indicated that the constituent bound by C. albicans in human saliva was low-molecular-weight mucin (MG2) and that in rat saliva was rat submandibular gland (RSMG) mucin. Further studies showed an identical cell hybridization signal and MAb colocalization by using RSMG ductal saliva and an aqueous RSMG extract in the solid-phase overlay assay. Analysis of cell binding to the aqueous extract of RSMG fractionated by anion-exchange chromatography demonstrated that C. albicans binding was restricted to an acidic subfraction of the RSMG extract, which also bound the RSMG mucin-specific MAb. The Candida-binding fraction contained predominantly RSMG mucin glycoprotein and also a noncovalently associated, chloroform-extractable material. Furthermore, we identified two strains of C. albicans which differed severalfold in the ability to bind RSMG mucin in the overlay assay. These results suggest that C. albicans binds to only a specific subfraction of RSMG mucin and that the two C. albicans strains tested differ in the ability to bind RSMG mucin subfractions.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-13233235, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1514934, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1692672, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1729194, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1747107, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1900531, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-1910004, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2019432, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2030668, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2152886, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2194958, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2194965, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2222261, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2654229, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2698728, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2926128, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-2992430, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3081183, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3288364, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3298951, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3301884, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3305626, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3497964, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3518803, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3674885, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3843705, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3944083, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-3993927, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-4062287, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-6165346, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-6373615, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-6724692, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-6801238, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-6948857, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-7104000, http://linkedlifedata.com/resource/pubmed/commentcorrection/8478083-7139659
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1940-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Analysis of Candida albicans adhesion to salivary mucin.
pubmed:affiliation
Department of Microbiology, University of Rochester School of Medicine and Dentistry, New York 14642.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't