Linked Life Data

15242536

Source:http://linkedlifedata.com/resource/pubmed/id/15242536

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-7-9
pubmed:abstractText
Human saliva contains multiple components that inhibit HIV-1 infection in vitro, which may contribute to low oral HIV-1 transmission. Salivary agglutinin (SAG) is a high-molecular-weight glycoprotein encoded by DMBT-1 and identical to gp340, a member of the lung scavange receptor, cysteine-rich receptor family. gp340 binds to surfactants A and D, which is believed to function in the clearance of microorganisms from the lung, as part of the innate immune response. Previously we reported that SAG (gp340) specifically inhibits HIV-1 infection with broad activity against diverse HIV-1 isolates. This gp340 inhibitory activity is mediated by binding to viral gp120 and involves a region different from the CD4-binding site on gp120. Here, we report that the gp340-binding region is localized to a linear, highly conserved sequence near the stem of the V3 loop that is critical for chemokine receptor interaction during viral binding and infection. The interaction of gp340 with gp120 is enhanced by prebinding of sCD4 to gp120, suggesting that gp340 inhibitory activity is mediated by blocking access of the gp120 to the chemokine receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0889-2229
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
600-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
gp340 (SAG) binds to the V3 sequence of gp120 important for chemokine receptor interaction.
pubmed:affiliation
Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia, 19104-6030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.