Methods and Compositions for Inhibiting HIV Infectivity
- Others
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- Crombie et al (1998) Identification of a CD36-related thrombospondin 1-binding domain in HIV-1 envelope glycoprotein gp120: relationship to HIV-1-specific inhibitory factors in human saliva. J Exp Med. 187(1):25-35
- Crombie et al (2001) Peptides derived from salivary thrombospondin-1 replicate its anti-HIV effect: potential role in microbicide development. J Acquir Immune Defic Syndr. 27(1):91-3.
- Issued US Patent 6,964,763.
- *Abstract
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It has long been known that some substance in saliva is capable of inhibiting HIV infection. A team of Cornell investigators has identified that substance as thrombospondin (TSP) and has identified the mechanism by which it works.
A six amino acid motif (CSVTCG) in TSP was found to bind to a conserved region of the HIV-1 envelope glycoprotein gp120. This HIV binding domain is structurally similar to the CLESH-1 domains in CD36 and LIMPII which bind to TSP. When TSP, CSVTCG peptides or other TSP analogs bind with gp120, the virion can no longer bind to cellular CD4 receptors or to the co-receptors (e.g., CCR5) through which HIV gains entry into cells.
These TSP binding studies also showed that TSP and its analogs bind to several pro-inflammatory chemokines in a concentration dependent, saturatable manner.
TSP, CSVTCG peptides and other TSP analogs have potential use as microbicides, inhibiting systemic or local HIV infection and transmission. They may also have use as therapeutics to treat inflammation.
The protein or peptide may be co-delivered with a contraceptive, carried by a non-contraceptive prophylactic device such as a surgical glove or oral dam, included in consumer products such as toothpaste, or formulated for more standard forms of pharmaceutical delivery.
- *Licensing
- Dan-Oscar Antsonda429@cornell.edu212-746-1297
- Country/Region
- USA
