Nuclear magnetic resonance analysis of solution conformations in C4-V3 hybrid peptides derived from human immunodeficiency virus (HIV) type 1 gp120: relation to specificity of peptide-induced anti-HIV neutralizing antibodies.
Immunogenic peptides containing epitopes of the gp120 C4 and V3 regions from human immunodeficiency virus strains MN and EV91 have been studied by nuclear magnetic resonance and molecular modeling and used as immunogens in rhesus monkeys. The results, combined with those for other peptides, suggest a correlation between solution conformation and immunologic cross-reactivity.
Vu
H M
HM
Departments of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Myers
D
D
de Lorimier
R
R
Matthews
T J
TJ
Moody
M A
MA
Heinly
C
C
Torres
J V
JV
Haynes
B F
BF
Spicer
L
L
D000595:Amino Acid Sequence; D000818:Animals; D003429:Cross Reactions; D015483:HIV Antibodies / Q000096:biosynthesis*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry* / Q000276:immunology*; D008253:Macaca mulatta; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120