Agnoprotein of mammalian polyomaviruses.
Polyomaviruses are naked viruses with an icosahedral capsid that surrounds a circular double-stranded DNA molecule of about 5000 base-pairs. Their genome encodes at least five proteins: large and small tumor antigens and the capsid proteins VP1, VP2 and VP3. The tumor antigens are expressed during early stages of the viral life cycle and are implicated in the regulation of viral transcription and DNA replication, while the capsid proteins are produced later during infection. Members of the Polyomaviridae family have been isolated in birds (Avipolyomavirus) and mammals (Orthopolyomavirus and Wukipolyomavirus). Some mammalian polyomaviruses encode an additional protein, referred to as agnoprotein, which is a relatively small polypeptide that exerts multiple functions. This review discusses the structure, post-translational modifications, and functions of agnoprotein, and speculates why not all polyomaviruses express this protein.
Department of Medical Biology, University of Tromsø, NO-9037 Tromsø, Norway.
Nancy
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Gerits
Ugo
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Moens
D000595:Amino Acid Sequence; D000818:Animals; D002335:Carnivora / Q000821:virology*; D006801:Humans; D008969:Molecular Sequence Data; D027382:Polyomaviridae / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011323:Primates / Q000821:virology*; D011499:Protein Processing, Post-Translational; D012377:Rodentia / Q000821:virology*; D013347:Subcellular Fractions / Q000378:metabolism; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000086082:Viroporin Proteins
D054334:Viral Regulatory and Accessory Proteins; C042559:agnoprotein, polyomavirus; D000086082:Viroporin Proteins