title: Sequence similarity between the envelope surface unit (SU) glycoproteins of primate and small ruminant lentiviruses.
abstract: Sequence similarity has been previously described in the transmembrane domain unit of envelope glycoproteins of primate and non-primate lentiviruses but similarity between the surface unit (SU) glycoprotein of these viruses is less clear or absent. Here we describe a consistent and significant sequence-similarity between the ovine/caprine lentivirus surface glycoprotein gp135 and the primate lentivirus gp120 in the region between variable loops V2 and V3. The biological relevance of this sequence similarity was indicated by clustering of conserved motifs in regions of structural importance in the human immunodeficiency virus type 1 gp120, conservation of cysteine residue pairs forming disulfide bonds and similar patterns of sequence variation in gp135 and gp120 between strains. The results indicate that SU glycoproteins from primate and small ruminant lentiviruses have structurally related domains.
authors.affiliation: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164-7040, USA. ihe@vetmed.wsu.edu
authors.forename: I
authors.initials: I
authors.lastname: Hötzel
authors.forename: W P
authors.initials: WP
authors.lastname: Cheevers
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016088:Arthritis-Encephalitis Virus, Caprine / Q000235:genetics; D017124:Conserved Sequence; D015699:HIV Envelope Protein gp120 / Q000235:genetics; D015497:HIV-1 / Q000235:genetics; D015498:HIV-2 / Q000235:genetics; D006801:Humans; D016086:Lentivirus / Q000235:genetics*; D008969:Molecular Sequence Data; D011323:Primates; D012418:Ruminants; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000235:genetics*; D014790:Visna-maedi virus / Q000235:genetics
chemical_list: D015699:HIV Envelope Protein gp120; D014759:Viral Envelope Proteins; C089034:glycoprotein 135, Maedi visna virus