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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2000-5-18
pubmed:abstractText
Mannose-binding lectin (MBL) is present in human serum and plays an important role in innate immunity by binding to carbohydrate on micro-organisms. Whereas the gp120/gp41 of human immunodeficiency virus type 1 (HIV-1) contains numerous N-linked glycosylation sites and many of these sites contain high-mannose glycans which could interact with MBL, the interaction between MBL and primary isolates (PI) of HIV-1 has not been studied. To determine if PI of HIV bind to MBL, a virus capture assay was developed in which virus was incubated in MBL-coated microtitre wells followed by detection of bound virus with an ELISA for p24 antigen. The X4 HIV-1(MN) T cell line-adapted strain and PI of HIV (R5 and X4) bound to MBL. Binding of virus to MBL was via the carbohydrate-recognition domain of MBL since binding did not occur in the absence of Ca(2+) and was blocked by preincubation of MBL-coated wells with soluble mannan. The interaction of virus with MBL-coated wells was also inhibited by preincubation of virus with soluble MBL, indicating that both immobilized and soluble forms of MBL bound to HIV. Although host cell glycoproteins are incorporated into the membrane of HIV, binding of virus to immobilized MBL required expression of gp120/gp41 on virus particles, suggesting the presence of either an unusually high carbohydrate density and/or a unique carbohydrate structure on gp120/gp41 that is the target of MBL. This study shows that PI of HIV bind to MBL and suggests that MBL can selectively interact with HIV in vivo via carbohydrate structures on gp120/gp41.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
949-55
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1.
pubmed:affiliation
Department of Immunology/Microbiology, Rush University, 1653 West Congress Parkway, Chicago, IL 60612, USA. msaifudd@rush.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.