Isolation and characterization of recombinants between attenuated and virulent aphthovirus strains [PDF]
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
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Behavior of intertypic recombinants between virulent and attenuated aphthovirus strains in tissue culture and cattle [PDF]
Two aphthovirus intertypic recombinants between the virulent strain A Venceslau and guanidine-resistant attenuated mutants of either strain C3 Resende or O1 Campos were obtained in an attempt to establish the region(s) of the viral genome responsible for attenuation in cattle. Recombinants that inherited the 3' half of the genome from either attenuated
Ana T. Giraudo +6 more
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Biochemical evidence of recombination within the unsegmented RNA genome of aphthovirus [PDF]
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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Guanidine-resistant mutants of aphthovirus induce the synthesis of an altered nonstructural polypeptide, P34 [PDF]
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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Immunogenicity of an aphthovirus chimera of the glycoprotein of vesicular stomatitis virus [PDF]
An oligodeoxynucleotide coding for amino acids 139 through 149 of antigenic site A (ASA) of the VP1 capsid protein of the foot-and-mouth disease virus C3 serotype (FMDV C3) was inserted into three different in-frame sites of the vesicular stomatitis virus New Jersey serotype (VSV-NJ) glycoprotein (G) gene cDNA present in plasmid pKG97 under control of ...
Pablo R. Grigera +4 more
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The structural polypeptides of aphthovirus are phosphoproteins. [PDF]
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
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Evolution of a persistent aphthovirus in cytolytic infections: partial reversion of phenotypic traits accompanied by genetic diversification [PDF]
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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Assessment of Foot-and-Mouth Disease Trends in Türkiye Between 2005 and 2025. [PDF]
Foot‐and‐mouth disease (FMD) is a highly contagious viral illness that continues to threaten livestock health, productivity, and trade, particularly in countries like Türkiye where multiple FMD serotypes cocirculate. This study aimed to analyze the temporal and spatial distributions, serotype dynamics, and seasonal patterns of FMD in Türkiye between ...
Pedro Mil-Homens M +5 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]
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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