Results 11 to 20 of about 1,890 (161)
Equine rhinitis A virus and its low pH empty particle: clues towards an aphthovirus entry mechanism?
PLoS Pathogens, 2009 Equine rhinitis A virus (ERAV) is closely related to foot-and-mouth disease virus (FMDV), belonging to the genus Aphthovirus of the Picornaviridae. How picornaviruses introduce their RNA genome into the cytoplasm of the host cell to initiate replication ...
Tobias J Tuthill +7 more
doaj +6 more sources
Isolation and characterization of recombinants between attenuated and virulent aphthovirus strains [PDF]
Journal of Virology, 1987 A guanidine-resistant mutant of the attenuated strain of aphthovirus type 01 strain Campos and the original wild-type strain were crossed to generate recombinant viruses. Two independently derived recombinant viruses were isolated. One isolate (RI) contained the P1 (structural proteins) gene region of attenuated strain and P3 (polymerase precursor ...
Ana T. Giraudo +4 more
semanticscholar +4 more sources
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
semanticscholar +4 more sources
Cell Entry of the Aphthovirus Equine Rhinitis A Virus Is Dependent on Endosome Acidification [PDF]
Journal of Virology, 2010 ABSTRACT Equine rhinitis A virus (ERAV) is genetically closely related to foot-and-mouth disease virus (FMDV), and both are now classified within the genus Aphthovirus of the family Picornaviridae .
Elisabetta Groppelli +2 more
semanticscholar +4 more sources
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
semanticscholar +4 more sources
The structural polypeptides of aphthovirus are phosphoproteins. [PDF]
Proceedings of the National Academy of Sciences, 1980 Analysis of aphthovirus A12, strain 119ab, grown in the presence of inorganic 32P revealed that two of the major viral polypeptides, VP4 and trypsin-sensitive protein VP3, were highly phosphorylated. The other major polypeptides, VP1 and VP2, were also phosphorylated but to a much lesser extent.
J.L. La Torre +3 more
semanticscholar +5 more sources
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
semanticscholar +4 more sources
Nucleic Acids Research, 1989 An analysis of published nucleotide sequences of the 5'-untranslated region (5'-UTR) of 7 cardioviruses and 3 aphthoviruses has allowed us to derive a consensus secondary structure model that differs from that previously proposed for the 5'-UTR of entero- and rhinoviruses, though all these viruses belong to the same family, Picornaviridae.
Evgeny V. Pilipenko +4 more
semanticscholar +6 more sources
RNA, 2000 The strategies developed by internal ribosome entry site (IRES) elements to recruit the translational machinery are poorly understood. In this study we show that protein-RNA interaction of the eIF4G translation initiation factor with sequences of the foot-and-mouth disease virus (FMDV) IRES is a key determinant of internal translation initiation in ...
Sonia López de Quinto +1 more
semanticscholar +5 more sources
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
semanticscholar +5 more sources