[Structural organization and intravirion interactions of proteins of the bovine leukemia virus].
Data on structural organization and interactions inside the virion of bovine leukemia virus (BLV) proteins are presented. Uniqueness of the structural organization of BLV proteins having no antigenic relationship between the corresponding animal retrovirus proteins is emphasized. Certain connection is also observed in the structural organization of surface glycoprotein gp69, major internal protein p24 and internal protein p12 with the corresponding polypeptides of human T-cell leukemia virus (HTLV). It is shown that BLV proteins form various complexes inside the virion which are not found in other known retroviruses. A structural model of BLV is presented.
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D000595:Amino Acid Sequence; D005814:Genes, Viral; D006031:Glycosylation; D001909:Leukemia Virus, Bovine / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D012194:RNA-Directed DNA Polymerase / Q000235:genetics / Q000378:metabolism; D012190:Retroviridae / Q000648:ultrastructure*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D014771:Virion / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*
D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase; D010447:Peptide Hydrolases
Strukturnaia organizatsiia i vnutrivirionnye vzaimodeĭstviia belkov virusa leĭkoza krupnogo rogatogo skota.