Potyvirus serology, sequences and biology.
Amino acid sequences of the cytoplasmic cylindrical inclusion protein (CIP), large nuclear inclusion protein (NIb), and coat protein (CP) of potyviruses were re-examined in light of reported serological relationships, and correlated with known and deduced biological functions. No obvious correlations were observed between either amino acid sequences or epitopes recognized by monoclonal antibodies and the natural host ranges of the potyviruses examined. Whereas the identified sequence motifs of the RNA helicase (CIP) and replicase (NIb) are predicted to be antigenic, most of the conserved sequences and epitopes in the CIP, NIb and CP were presumed to be maintained for structural rather than functional reasons. Three possible potyvirus clusters are proposed on the basis of the length and composition of the virion surface-exposed amino terminal extension of the CP; these clusters do not correlate with overall CP sequence homology, host range, or vectors, but are of potential evolutionary significance and hence of possible taxonomic value.
Hammond
J
J
United States Department of Agriculture, Beltsville Agricultural Research Center, Maryland.
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010942:Plant Viruses / Q000145:classification / Q000276:immunology; D012328:RNA Viruses / Q000145:classification / Q000276:immunology; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry / Q000276:immunology
D014764:Viral Proteins