Biochemical evidence of recombination within the unsegmented RNA genome of aphthovirus [PDF]
Journal of Virology, 1982 Four different pairs of temperature-sensitive mutants, derived from the same strain of aphthovirus, were crossed by using an infectious center recombination test. Each parental mutant carried an unselected marker affecting the isoelectric point of a virus-coded polypeptide; progeny of the crosses, able to grow at the nonpermissive temperature, were ...
Andrew M. Q. King +3 more
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Evolution of a persistent aphthovirus in cytolytic infections: partial reversion of phenotypic traits accompanied by genetic diversification [PDF]
Journal of Virology, 1996 Foot-and-mouth disease virus (FMDV) shows a dual potential to be cytolytic or to establish persistent infections in cell culture. FMDV R100, a virus rescued after 100 passages of carrier BHK-21 cells persistently infected with FMDV clone C-S8c1, showed multiple genetic and phenotypic alterations relative to the parental clone C-S8c1.
Noemı́ Sevilla, Esteban Domingo
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Foot-and-mouth disease virus 3C protease as virulence determinant plays multiple roles in cleaving viral polyprotein and host factors [PDF]
VirulenceFoot-and-mouth disease virus (FMDV) can cause a severe infectious disease that primarily affects even-toed ungulates. FMDV is classified into the genus of Aphthovirus in the family Picornaviridae.
Houcheng Zhou +6 more
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Identification of an essential region for internal initiation of translation in the aphthovirus internal ribosome entry site and implications for viral evolution [PDF]
Journal of Virology, 1996 Translation of aphthovirus RNA is initiated at an internal ribosome entry site (IRES) element, preceding the first functional AUG initiation codon. The effect of mutations at the base of domain 3 of the aphthovirus IRES on translation activity has been analyzed by site-directed mutagenesis and expression of bicistronic RNAs in transfected cells.
Encarnación Martı́nez-Salas +2 more
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RNA, 1999 Internal initiation of translation is promoted by internal ribosome entry site (IRES) cis-acting elements. Using transcripts that correspond to the structural domains of the foot-and-mouth disease virus (FMDV) IRES, we have identified RNA-RNA interactions between separated domains (1-2, 3, 4-5, or HH) of the IRES structure. All the assayed domains were
Ricardo Ramos +1 more
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Guanidine-resistant mutants of aphthovirus induce the synthesis of an altered nonstructural polypeptide, P34 [PDF]
Journal of Virology, 1982 Extracts of cells infected with guanidine-resistant mutants of aphthovirus were examined for differences in virus-induced polypeptides by using electrofocusing. Four of 1 independent spontaneous mutants induced the synthesis of an altered nonstructural polypeptide, P34.
Keith Saunders, Andrew M. Q. King
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Nucleic Acids Research, 1993 Statistical analyses of RNA folding in 5' nontranslated regions (5'NTR) of encephalomyocarditis virus, Theiler's murine encephalomyelitis virus, foot-and-mouth disease virus, and hepatitis A virus indicate that two highly significant folding regions occur in the 5' and 3' portions of the 5'NTR.
Shu‐Yun Le +3 more
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Conserved structural motifs located in distal loops of aphthovirus internal ribosome entry site domain 3 are required for internal initiation of translation [PDF]
Journal of Virology, 1997 A comparison of picornavirus internal ribosome entry site (IRES) secondary structures revealed the existence of conserved motifs located on loops. We have carried out a mutational analysis to test their requirement for IRES-driven translation. The GUAA sequence, located in the aphthovirus 3A loop, did not tolerate substitutions that disrupt the GNRA ...
Sonia López de Quinto +1 more
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Cell Recognition by Foot-and-Mouth Disease Virus That Lacks the RGD Integrin-Binding Motif: Flexibility in Aphthovirus Receptor Usage [PDF]
Journal of Virology, 2000 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 virus (FMDV) in cell culture select for mutant viruses that render dispensable a highly conserved Arg-Gly-Asp (RGD) motif responsible for integrin
Éric Baranowski +5 more
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