Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/8549
Share/Export:
logo share SHARE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: blexibility in aphthovirus receptor usage

AuthorsBaranowski, Eric; Ruiz-Jarabo, Carmen M.; Sevilla, Noemí CSIC ORCID; Andreu, David; Beck, Ewald; Domingo, Esteban CSIC ORCID
KeywordsFoot-and-mouth disease virus
Issue Date2000
PublisherAmerican Society for Microbiology
CitationJournal of Virology, 2000, p. 1641-1647, Vol. 74, No. 4
AbstractCell 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 virus (FMDV) in cell culture select for mutant viruses that render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible for integrin receptor recognition. Here, we provide evidence that viability of recombinant FMDVs including a Asp-143Gly change at the RGD motif was conditioned by a number of capsid substitutions selected upon FMDV evolution in cell culture. Multiply passaged FMDVs acquired the ability to infect human K-562 cells, which do not express integrin alpha-v-beta-3. In contrast to previously described cell culture-adapted FMDVs, the RGD-independent infection did not require binding to the surface glycosaminoglycan heparan sulfate (HS). Viruses which do not bind HS and lack the RGD integrin-binding motif replicate efficiently in BHK-21 cells. Interestingly, FMDV mutants selected from the quasispecies for the inability to bind heparin regained sensitivity to inhibition by a synthetic peptide that represents the G-H loop of VP1. Thus, a single amino acid replacement leading to loss of HS recognition can shift preferential receptor usage of FMDV from HS to integrin. These results indicate at least three different mechanisms for cell recognition by FMDV and suggest a potential for this virus to use multiple, alternative receptors for entry even into the same cell type
Publisher version (URL)http://jvi.asm.org/cgi/content/full/74/4/1641
URIhttp://hdl.handle.net/10261/8549
ISSN0022-538X
E-ISSN1098-5514
Appears in Collections:(CBM) Artículos




Files in This Item:
File Description SizeFormat
EBaranowski_JVirol_1641.pdf118,7 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work

Page view(s)

380
checked on May 26, 2022

Download(s)

272
checked on May 26, 2022

Google ScholarTM

Check


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.