Joos B Fischer M Schweizer A Kuster H Böni J Wong JK Weber R Trkola A Günthard HF 2007 The rapid evolution of human immunodeficiency virus (HIV) envelope represents a major challenge to vaccine and drug development, particularly because the underlying mechanisms are not completely understood. To explore whether distinct patterns of positive selection within the envelope glycoprotein (gp) 120 exist and are associated with functionally relevant domains, we conducted a long-term survey of sequence evolution in 20 HIV-1-infected persons who interrupted antiretroviral therapy. In total, 1753 clonal sequences encompassing the C2-V3-C3 region of gp120 were derived. Strikingly, positively selected amino acids mapped almost exclusively (P=.0003) to externally accessible residues on the gp120 crystal structure. The current understanding of envelope structure and function associates the main determinants of viral entry and the targets for neutralizing antibodies with these exterior regions of gp120, strongly suggesting that the observed adaptive evolution of these sites occurs in response to respective selective forces. application/pdf https://sonar.ch/global/documents/146588 eng info:eu-repo/semantics/altIdentifier/doi/10.1086/518935 info:eu-repo/semantics/altIdentifier/pmid/17570120 info:eu-repo/semantics/openAccess The Journal of infectious diseases. - 2007 Anti-Retroviral Agents Drug Administration Schedule Evolution, Molecular HIV Envelope Protein gp120 HIV Infections HIV-1 Humans Longitudinal Studies Molecular Sequence Data Phylogeny Protein Structure, Tertiary Sequence Analysis, Protein Positive in vivo selection of the HIV-1 envelope protein gp120 occurs at surface-exposed regions. http://purl.org/coar/resource_type/c_6501