Arginine-Glycine-Aspartic Acid Motif Is Critical for Human Parechovirus 1 Entry
Open Access
- 15 October 2001
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 75 (20) , 10000-10004
- https://doi.org/10.1128/jvi.75.20.10000-10004.2001
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.Keywords
This publication has 47 references indexed in Scilit:
- Human Parechovirus 1 Utilizes Integrins αvβ3 and αvβ1 as ReceptorsJournal of Virology, 2000
- Cell receptors for picornaviruses as determinants of cell tropism and pathogenesisTrends in Microbiology, 1998
- Cell Attachment and Mouse Virulence of Echovirus 9 Correlate with an RGD Motif in the Capsid Protein VP1Virology, 1997
- Systematic Replacement of Amino Acid Residues within an Arg-Gly-Asp-containing Loop of Foot-and-Mouth Disease Virus and Effect on Cell RecognitionJournal of Biological Chemistry, 1996
- Complete nucleotide sequence and biological properties of an infectious clone of prototype echovirus 9Virus Research, 1995
- Nucleotide sequence of the P1 region of serotype Asia1 foot-and-mouth disease virusVirus Genes, 1994
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- The nucleotide sequences of wild-type coxsackievirus A9 strains imply that an RGD motif in VP1 is functionally significantJournal of General Virology, 1992
- The Nucleotide Sequence of Coxsackievirus A9; Implications for Receptor Binding and Enterovirus ClassificationJournal of General Virology, 1989
- New Perspectives in Cell Adhesion: RGD and IntegrinsScience, 1987