Disease relevance of Aphthovirus

• Sixteen substitution mutations of the conserved DvExNPGP sequence, implicated in cardiovirus and aphthovirus primary polyprotein cleavage, were created in encephalomyocarditis virus cDNA, expressed, and characterized for processing activity [1].
• Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: flexibility in aphthovirus receptor usage [2].
• Specific proteolysis of protein synthesis initiation factor eIF-4 gamma occurs during infection with rhinoviruses, enteroviruses, and aphthoviruses, apparently leading to an inability of the ribosomes to bind capped mRNAs [3].
• Another more distantly related picornavirus, equine rhinitis B virus (ERBV), which is not classified as an aphthovirus, also encodes an L protein [4].
• One peptide copied the sequence of amino acids 141 to 160 from the capsid VP1 of the aphthovirus strains O1 BFS 1860 and O1 Kaufbeuren (O peptide), the other copied the equivalent sequence from aphthovirus strain A24 Cruzeiro (A peptide) [5].

High impact information on Aphthovirus

• The results have shown that the enhanced IRES activity associated with a single pyrimidine transition fixed in a persistent aphthovirus variant (E. Martínez-Salas, J. C. Sáiz, M. Dávila, G. J. Belsham, and E. Domingo, J. Virol. 67:3748-3755, 1993) is base specific [6].
• The aphthovirus leader is a protease involved in viral polyprotein processing and host cell translation shutoff [7].
• 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 [8].
• Heterogeneity of the polyribocytidylic acid tract in aphthovirus: biochemical and biological studies of viruses carrying polyribocytidylic acid tracts of different lengths [9].
• Sialic acid acts as a receptor for equine rhinitis A virus binding and infection [10].

Chemical compound and disease context of Aphthovirus

• Guanidine-resistant mutants of aphthovirus induce the synthesis of an altered nonstructural polypeptide, P34 [11].
• The only other member of the Aphthovirus genus, equine rhinitis A virus (ERAV), also encodes an L protein, but this shares only 32% amino acid identity with its FMDV counterpart [4].
• The aphthovirus polypeptide was designed to contain only a single additional amino acid, the N-terminal methionine [12].

Biological context of Aphthovirus

• SV2 contained an amino-terminal extension of the reading frame, which was analogous to the leader protein of members of the Aphthovirus, Cardiovirus, Erbovirus, Kobuvirus, and Teschovirus genera, but there was no significant amino acid homology with any of these known leader proteins [13].

Gene context of Aphthovirus

• These results place ERV-1 alongside FMDV in the aphthovirus genus of the picornavirus family and indicate that this virus may serve as a model system for examining the biology of FMDV [14].
• Measurement of an antigenic response to the aphthovirus infection-associated antigen (VIA), the viral RNA polymerase 3D(pol), is frequently used as a discriminating assay for the extent of viral replication in animals [15].
• One peptide copied the sequence of amino acids 141 to 160 from the VP1 of aphthovirus strains O1BFS 1860 and O1 Kaufbeuren (O peptide), the other copied the equivalent sequence from aphthovirus strain A24 Cruzeiro (A peptide) [16].
• The IRES elements of cardio-, entero- and aphthoviruses bind a cellular protein, p57 [17].

Analytical, diagnostic and therapeutic context of Aphthovirus

• Extracts of cells infected with guanidine-resistant mutants of aphthovirus were examined for differences in virus-induced polypeptides by using electrofocusing [11].

References