Antigenicity of three synthetic peptides from the C-terminus of HIV-1 gp 120 correlates with the fragmentation pattern obtained in FAB mass spectrometry.
The proteolytic cleavage site of HIV-1 envelope glycoprotein precursor gp160 is sensitive to mutations. In this study we observed that the antigenicity of synthetic peptides from the C-terminus of gp120 is dependent on the length of the peptide, suggesting a conformational restriction. The physical properties of the peptides evaluated by FAB mass spectrometry correlated with the serological data, but differed from predictions based on the linear sequence. From our results we conclude that the C-terminus of HIV-1 gp120 is conformationally restricted. Furthermore FAB mass spectrometry seems to possess the ability to provide information concerning the conformation of synthetic peptides.
Streckert
H J
HJ
Department of Medical Microbiology and Virology, Ruhr-University Bochum, FRG.
Weber
C
C
Müller
D
D
D000939:Epitopes / Q000737:chemistry; D015686:Gene Products, env / Q000737:chemistry / Q000276:immunology; D015483:HIV Antibodies / Q000097:blood; D015488:HIV Antigens / Q000737:chemistry; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000276:immunology*; D019302:HIV Envelope Protein gp160; D015497:HIV-1 / Q000737:chemistry / Q000276:immunology*; D006801:Humans; D066298:In Vitro Techniques; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology*; D011498:Protein Precursors / Q000737:chemistry / Q000276:immunology; D016339:Spectrometry, Mass, Fast Atom Bombardment
D000939:Epitopes; D015686:Gene Products, env; D015483:HIV Antibodies; D015488:HIV Antigens; D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D010446:Peptide Fragments; D011498:Protein Precursors