作者: S Modrow , B H Hahn , G M Shaw , R C Gallo , F Wong-Staal
DOI: 10.1128/JVI.61.2.570-578.1987
关键词:
摘要: Independent isolates of human immunodeficiency virus (HIV) exhibit a striking genomic diversity, most which is located in the viral envelope gene. Since this property HIV group viruses may play an important role pathobiology virus, we analyzed predicted amino acid sequences proteins seven different strains, three represent sequential from single patient. By using computer program that predicts secondary protein structure and superimposes values for hydrophilicity, surface probability, flexibility, identified several potential antigenic epitopes viruses. Interestingly, majority exterior (gp120) were found regions high sequence variability are interspersed with highly conserved among independent isolates. A comparison revealed changes concerning occurred only to be antigenic, predominantly variable regions. The membrane-associated gp41 contains no regions; about 80% acids conserved, one hydrophilic area was as likely accessible antibody recognition. These findings give insight into possible tertiary variant should facilitate experimental approaches directed toward identification fine mapping proteins.