translation agency

NLM AIDSLINE
The C domain of HIV-1 gp41 binds the putative cellular receptor protein P62.
Chen YH; Xiao Y; Wu W; Yang J; Sui S; Dierich MP; School of Life
November 30, 1999
AIDS. 1999 Jun 18;13(9):1021-4. Unique Identifier : AIDSLINE

OBJECTIVE: To characterize the binding of gp41 with the putative receptor protein P62. DESIGN: HIV-1 gp41 binds several cellular proteins by two binding sites, one of which has been shown to bind to a putative receptor protein P45 (45 kDa). Based on this, an attempt was made to determine the relationship between the two binding sites and P62 (62 kDa). METHODS: Using surface plasmon resonance (SPR) measurement, the interaction was measured between recombinant soluble gp41 (rsgp41, Env aa539-684) and protein P62. Inhibition of this interaction was attempted by the use of synthetic peptides (P1, aa583-599; P2, aa646-674) corresponding to the two binding sites in gp41. In addition, the direct binding of P62 to peptide P2 was examined in an enzyme-linked immunosorbent assay. RESULTS: Using SPR measurement, the interaction between P62 and rsgp41 was confirmed, and the interaction was found to be inhibited by only the synthetic peptide P2 sequence that corresponds to the C domain of gp41; neither P1 nor a control peptide inhibited the interaction. Moreover, like rsgp41, P2 was able to bind P62 whereas P1 and another recombinant gp41 (aa567-648 that does not include the C domain) were not. CONCLUSIONS: P62 bound rsgp41 and the synthetic peptide P2. This interaction could be inhibited only by P2. These results indicate that the C domain of HIV-1 gp41 binds P62.

JOURNAL ARTICLE Animal Binding Sites Enzyme-Linked Immunosorbent Assay HIV Antibodies/IMMUNOLOGY/METABOLISM HIV Envelope Protein gp41/*METABOLISM HIV-1/*METABOLISM Membrane Proteins/METABOLISM Mice Molecular Sequence Data Peptides/CHEMISTRY/CHEMICAL SYNTHESIS/METABOLISM Protein Binding Rabbits Receptors, HIV/*METABOLISM Recombinant Proteins/METABOLISM RNA-Binding Proteins/*METABOLISM Support, Non-U.S. Gov't Surface Plasmon Resonance

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