Cell Recognition by Foot-and-Mouth Disease Virus That Lacks the RGD Integrin-Binding Motif: Flexibility in Aphthovirus Receptor Usage

• DOI: 10.1128/jvi.74.4.1641-1647.2000
• Publication Date: 2002-07-27T09:55:53Z
• Authors: Eric Baranowski; Carmen M. Ruiz-Ja...; Noemi Sevilla; David Andreu; Ewald Beck; Esteban Domingo
• Keywords: RGD motif; Motif (music); Aphthovirus

ABSTRACT Cell surface molecules that can act as virus receptors may exert an important selective pressure on RNA viral quasispecies. Large population passages of foot-and-mouth disease (FMDV) in cell culture select for mutant viruses render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible integrin receptor recognition. Here, we provide evidence viability recombinant FMDVs including Asp-143→Gly change at the RGD was conditioned by number capsid substitutions selected upon FMDV evolution culture. Multiply passaged acquired ability to infect human K-562 cells, which do not express α v β 3 . In contrast previously described culture-adapted FMDVs, RGD-independent infection did require binding glycosaminoglycan heparan sulfate (HS). Viruses bind HS and lack integrin-binding replicate efficiently BHK-21 cells. Interestingly, mutants from quasispecies inability heparin regained sensitivity inhibition synthetic peptide represents G-H loop VP1. Thus, single amino acid replacement leading loss recognition shift preferential usage integrin. These results indicate least three different mechanisms suggest potential this use multiple, alternative entry even into same type.