A biochemical approach for detecting interactions between peptides from the HIV gp120 glycoprotein and a CD4 sequence.
Peptides selected from the HIV viral protein gp120 bind to a synthetic peptide mimicking sequence 78-89 of the human lymphocyte CD4 molecule, linked to activated Sepharose. The binding of viral fragments to the CD4 peptide-Sepharose beads was ascertained either by aid of a ninhydrin reagent or by fluorescence microscopy. A suitable alignment of these HIV peptides with the CD4 fragment showed that multiple interactions might occur between hydrophobic or charged groups of the two molecules. Although this experiment does not demonstrate that these two amino acid stretches are involved in the primary binding of gp120 to CD4 receptors, the present data suggest that the two sequences might have some kind of interaction during subsequent steps of viral infection.
Chersi
Alberto
A
Regina Elena Institute for Cancer Research, Lab of Biochemistry, Via delle Messi d'oro 156, 00158 Rome, Italy. biochimica@ifo.it
Falasca
Giuliana
G
Malorni
Walter
W
D000595:Amino Acid Sequence; D001665:Binding Sites; D015704:CD4 Antigens / Q000737:chemistry*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D010446:Peptide Fragments; D010455:Peptides