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Foot-and-mouth disease virus appears to initiateinfection by binding to cells at an Arg-Gly-Asp (RGD) sequence found in theflexible beta G-beta H loop of the viral capsid protein VP1. The role of the RGDsequence in attachment of virus to cells was tested by using syntheticfull-length viral RNAs mutated within or near the RGD sequence. Baby hamsterkidney (BHK) cells transfected with three different RNAs carrying mutationsbordering the RGD sequence produced infectious viruses with wild-type plaquemorphology; however, one of these mutant viruses bound to cells less efficientlythan wild type. BHK cells transfected with RNAs containing changes within theRGD sequence produced noninfectious particles indistinguishable from wild-typevirus in terms of sedimentation coefficient, binding to monoclonal antibodies,and protein composition. These virus-like particles are defined as ads- viruses,since they were unable to adsorb to and infect BHK cells. These mutants weredefective only in cell binding, since antibody-complexed ads- viruses were ableto infect Chinese hamster ovary cells expressing an immunoglobulin Fc receptor.These results confirm the essential role of the RGD sequence in binding offoot-and-mouth disease virus to susceptible cells and demonstrate that thenatural cellular receptor for the virus serves only to bind virus to thecell.

proceedings of the national academy of sciences of the united states of america

RGD sequence of foot-and-mouth disease virus isessential for infecting cells via the natural receptor but can be bypassed by anantibody-dependent enhancement pathway.