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  • Interaction of the HIV-1 GP120 V3 loop with bacterial lipopolysaccharide [Elektronski vir] : a pattern recognition inhibition
    Majerle, Andreja ...
    HIV-1 represents an elusive target for therapeutic compounds due to its high rate of mutation. Targeting structural patterns instead of a constantly changing specific 3D structure may represent an ... approach that is less sensitive to viral mutations. The V3 loop of gp120 of HIV-1, which is responsible for binding of viral gp120 to CCR5 or CXCR4 coreceptors, has already been identified as an effective target for the inhibition of viral entry. The peptide derived from the V3 loop of gp120 specifically interacts with the lipid A moiety of LPS, as does the full gp120 protein. NMR analysis of V3 in complex with LPS shows formation of an amphipathic turn. The interaction between LPS and V3 relies on the structural pattern, comprising a combination of hydrophobic and charge interactions, similar to the interactionbetween antimicrobial peptides and LPS. LPS inhibited binding of gp120 to the surface of target T cells. Nonendotoxic LPS antagonists inhibitedviral infection, demonstrating the possibility for the development ofan inhibitor of HIV-1 attachment to T cells based on the recognition of a conserved structural pattern.
    Source: Journal of biological chemistry [Elektronski vir]. - ISSN 1083-351X (Vol. 286, iss. 29, 22 Jul. 2011, str. 26228-26237)
    Type of material - e-article
    Publish date - 2011
    Language - english
    COBISS.SI-ID - 4677402
    DOI

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