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rdf:type |
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lifeskim:mentions |
umls-concept:C0019134,
umls-concept:C0019691,
umls-concept:C0019704,
umls-concept:C0021311,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0178539,
umls-concept:C0205349,
umls-concept:C0220806,
umls-concept:C0441655,
umls-concept:C1167622,
umls-concept:C1519878,
umls-concept:C1533691,
umls-concept:C1707520
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|
pubmed:issue |
22
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|
pubmed:dateCreated |
1994-7-8
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|
pubmed:abstractText |
Chemically modified heparins were tested for their activities in (i) inhibiting HIV-1 replication in vitro and (ii) inhibiting the binding to recombinant HIV-1 gp120 of monoclonal antibodies specific for the V3 loop. The results reveal that N-desulfation reduces activity, although this is largely restored on N-acetylation. Selective O-desulfation also markedly reduces activity, whereas carboxyl reduction has little effect. Overall these results show that the anti-HIV-1 activity of heparin does not depend simply on negative density, and indicate instead that particular structures, notably O-sulfates, are involved. Our studies reveal that for chemically modified heparins and heparin-derived fragments there is a striking correlation between anti-HIV-1 activity in vitro and binding to the V3 loop of gp120 in solid phase ELISA. This strongly suggests that the heparin exerts its anti-HIV-1 activity by binding to the V3 loop of gp120.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6974-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7911328-Acetylation,
pubmed-meshheading:7911328-Amino Acid Sequence,
pubmed-meshheading:7911328-Animals,
pubmed-meshheading:7911328-Antiviral Agents,
pubmed-meshheading:7911328-CD4-Positive T-Lymphocytes,
pubmed-meshheading:7911328-Cattle,
pubmed-meshheading:7911328-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:7911328-HIV Envelope Protein gp120,
pubmed-meshheading:7911328-HIV-1,
pubmed-meshheading:7911328-Heparin,
pubmed-meshheading:7911328-Humans,
pubmed-meshheading:7911328-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7911328-Molecular Sequence Data,
pubmed-meshheading:7911328-Peptide Fragments,
pubmed-meshheading:7911328-Protein Binding,
pubmed-meshheading:7911328-Structure-Activity Relationship,
pubmed-meshheading:7911328-Sulfates,
pubmed-meshheading:7911328-Swine
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pubmed:year |
1994
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pubmed:articleTitle |
Anti-HIV-1 activity of chemically modified heparins: correlation between binding to the V3 loop of gp120 and inhibition of cellular HIV-1 infection in vitro.
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pubmed:affiliation |
Department of Biochemistry, Royal Holloway and Bedford New College, Egham, Surrey, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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