title: Arginine-glycine-aspartic acid motif is critical for human parechovirus 1 entry.
abstract: The human parechovirus 1 RGD motif in VP1 was studied by mutagenesis. An RGD-to-RGE change gave only revertant viruses with a restored RGD, while deletion of GD was lethal and nonrevertable. Mutations at the +1 and +2 positions had some effect on growth properties and a +1 M-to-P change was lethal. These studies indicate that the RGD motif plays a critical role in infectivity, presumably by interacting with integrins, and that downstream amino acids can have an influence on function.
authors.affiliation: Department of Biological Sciences, John Tabor Laboratories, University of Essex, Colchester CO4 3SQ, United Kingdom.
authors.forename: Y
authors.initials: Y
authors.lastname: Boonyakiat
authors.forename: P J
authors.initials: PJ
authors.lastname: Hughes
authors.forename: F
authors.initials: F
authors.lastname: Ghazi
authors.forename: G
authors.initials: G
authors.lastname: Stanway
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine; D001224:Aspartic Acid; D005998:Glycine; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D009842:Oligopeptides; D010849:Picornaviridae / Q000235:genetics / Q000502:physiology*; D016415:Sequence Alignment; D014764:Viral Proteins / Q000235:genetics*; D014779:Virus Replication
chemical_list: D009842:Oligopeptides; D014764:Viral Proteins; D001224:Aspartic Acid; C047981:arginyl-glycyl-aspartic acid; D001120:Arginine; D005998:Glycine