Is the V3 loop involved in HIV binding to CD4?
The entry of the human immunodeficiency virus into cells requires the interaction of the viral envelope glycoprotein gp120 with CD4 and a chemokine receptor. The gp120 binding site has been previously mapped to the Ig-CDR2-like region of CD4 first domain. A second area of this domain (Ig-CDR3-like region) is involved in gp120-CD4 interactions, but its gp120 counterpart remained so far unknown. Using a photoaffinity labeling experiment, we demonstrate that a peptide, mapping the (307-330)m region of HIV-MN-gp120 V3 loop, binds a sequence including a part of the Ig-CDR3-like region. These results may contribute to explain the complex mechanism of human immunodeficiency virus penetration, helping the development of new therapeutic agents.
Dettin
Monica
M
Department of Chemical Process Engineering, University of Padova, 35131-Padova, Italy. monica.dettin@unipd.it
Ferranti
Pasquale
P
Scarinci
Claudia
C
Picariello
Gianluca
G
Di Bello
Carlo
C
D000595:Amino Acid Sequence; D001665:Binding Sites; D015704:CD4 Antigens / Q000737:chemistry* / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D015699:HIV Envelope Protein gp120 / Q000737:chemistry* / Q000378:metabolism*; D015497:HIV-1 / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D019920:Photoaffinity Labels / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D019920:Photoaffinity Labels