Abstract
The formation of a complex among gp120, CD4, and CCR5/CXCR4 represents a key step in human immunodeficiency virus (HIV) infection. The use of synthetic peptides reproducing sequences of these surface proteins has increased knowledge about the interactions that determine the penetration of HIV viruses into target cells. The final aim of such investigations is the design of molecules able to inhibit the initial step of infection and the development of high-sensitivity in vitro assays for detection of HIV. In particular, the studies presented herein concern the role of the gp120 V3 loop in the CD4 binding, the importance of the N-terminal sequence of HIV-coreceptor CCR5, the sequences patterned on CXCR4 natural ligand (stromal-derived factor 1 [SDF-1]) as inhibitory peptides, and the importance of substrate secondary structure in determining the enzymatic processing of gp120 precursor (gp160).
MeSH terms
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Amino Acid Sequence
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CD4 Antigens / metabolism
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Chemokine CXCL12
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Chemokines, CXC / chemistry
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Chemokines, CXC / genetics
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Chemokines, CXC / metabolism*
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Cytokines / chemistry
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Cytokines / genetics
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Cytokines / metabolism*
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Drug Design
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HIV Envelope Protein gp120 / chemistry
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HIV Envelope Protein gp120 / genetics
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HIV Envelope Protein gp120 / metabolism*
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HIV Infections / metabolism
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HIV Infections / virology*
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HIV-1 / genetics
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HIV-1 / metabolism
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Humans
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Molecular Sequence Data
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Peptide Fragments / metabolism*
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Point Mutation
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Receptors, CCR5 / chemistry
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Receptors, CCR5 / genetics
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Receptors, CCR5 / metabolism*
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Receptors, CXCR4 / chemistry
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Receptors, CXCR4 / genetics
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Receptors, CXCR4 / metabolism*
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Recombinant Proteins / metabolism
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Tumor Cells, Cultured
Substances
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CD4 Antigens
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CXCL12 protein, human
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Chemokine CXCL12
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Chemokines, CXC
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Cytokines
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HIV Envelope Protein gp120
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Peptide Fragments
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Receptors, CCR5
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Receptors, CXCR4
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Recombinant Proteins