Monoclonal antibodies, against O1 serotype foot-and-mouth disease virus, from a natural bovine host, recognize similar antigenic features to those defined by the mouse.

Barnett, P.V.; Samuel, A. R.; Püllen, Lukas; Ansell, D M; Butcher, R.N.; Parkhouse, R. M. E.

doi:10.1099/0022-1317-79-7-1687

Cited by 41 publications

(42 citation statements)

References 45 publications

(43 reference statements)

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“… a The hypervariable regions were derived from the alignment of serotype A and O capsid sequences b The antigenic sites are a summary of those described by Thomas et al [80]; Baxt et al [11]; Bolwell et al [16]; Saiz et al [72] (type A); Kitson et al [43]; Crowther et al [21]; Barnett et al [5]; Barnett et al [6] (type O) c The amino acid residues have been numbered independently for each FMDV protein. For each residue, the first digit indicates the protein (1D, 1B or 1C), and the last three digits indicate the amino acid position…”

Section: Resultsmentioning

confidence: 99%

Genetic heterogeneity in the leader and P1-coding regions of foot-and-mouth disease virus serotypes A and O in Africa

et al. 2013

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Genetic information regarding the leader (L) and complete capsid-coding (P1) region of FMD serotype A and O viruses prevalent on the African continent is lacking. Here, we present the complete L-P1 sequences for eight serotype A and nine serotype O viruses recovered from FMDV outbreaks in East and West Africa over the last 33 years. Phylogenetic analysis of the P1 and capsid-coding regions revealed that the African isolates grouped according to serotype, and certain clusters were indicative of transboundary as well as intra-regional spread of the virus. However, similar analysis of the L region revealed random groupings of isolates from serotypes O and A. Comparisons between the phylogenetic trees derived from the structural coding regions and the L region pointed to a possibility of genetic recombination. The intertypic nucleotide and amino acid variation of all the isolates in this study supported results from previous studies where the externally located 1D was the most variable whilst the internally located 1A was the most conserved, which likely reflects the selective pressures on these proteins. Amino acids identified previously as important for FMDV structure and functioning were found to be highly conserved. The information gained from this study will contribute to the construction of structurally designed FMDV vaccines in Africa.Electronic supplementary materialThe online version of this article (doi:10.1007/s00705-013-1838-9) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Genetic heterogeneity in the leader and P1-coding regions of foot-and-mouth disease virus serotypes A and O in Africa

et al. 2013

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“…The role of the IgG1 isotype in protection of cattle from disease has been reported [33] and a predominance of IgG1 over IgG2 antibodies in animals receiving infectious or inactivated virus [50]. T-cell responses were measured by IFN-c (cytokine) [34] which is mainly produced by activated cells [34] Clinical Score Viral RNA and Virus IsolaƟon in anamnestic responses.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of immune responses of stabilised SAT2 antigens of foot-and-mouth disease in cattle

Scott

Rathogwa

Capozzo³

et al. 2017

Vaccine

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“…In particular, the distinct amino acid residues at 2079 (Tyr) of VP2 lies adjacent to the RGD motif (Figure 5A), and (ii) Thr-1041 and Gln-1045 of VP1 are clustered around the fivefold axis (Figure 5B). The outcome of the substitution at residue 2079 of VP2 could potentially dislocate both antigenic sites 1 (1141–1160 residues of the VP1 G-H loop, [39]) and 2 (2070–2078 residues of the VP2 B-C loop, [40]), with a structural and/or functional change [33]. One of the amino acid mutations, Lys-1041 → Glu in VP1 was fixed in two heparin-binding derivatives of C-S8c1 (C-S8c1p100c10 and the MARLS mutant) [20,22].…”

Section: Discussionmentioning

confidence: 99%

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

Bai

Bao

et al. 2014

Virol J

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BackgroundSome cell-adapted strains of foot-and-mouth disease virus (FMDV) can utilize heparan sulfate (HS) as a receptor to facilitate viral infection in cultured cells. A number of independent sites on the capsid that might be involved in FMDV-HS interaction have been studied. However, the previously reported residues do not adequately explain HS-dependent infection of two cell-adapted PanAsia-1 strains (O/Tibet/CHA/6/99tc and O/Fujian/CHA/9/99tc) of FMDV serotype O.To identify the molecular determinant(s) for the interaction of O/Tibet/CHA/6/99tc and O/Fujian/CHA/9/99tc with HS receptor, several chimeric viruses and site-directed mutants were generated by using an infectious cDNA of a non-HS-utilizing rescued virus (Cathay topotype) as the genomic backbone. Phenotypic properties of these viruses were determined by plaque assays and virus adsorption and penetration assays in cultured cells.ResultsOnly two of the rescued viruses encoding VP0 of O/Tibet/CHA/6/99tc or VP1 of O/Fujian/CHA/9/99tc formed plaques on wild-type Chinese hamster ovary (WT-CHO; HS+) cells, but not on HS-negative pgsD-677 cells. The formation of plaques by these two chimeric viruses on WT-CHO cells could be abolished by the introduction of single amino acid mutations Gln-2080 → Leu in VP2 of O/Tibet/CHA/6/99tc and Lys-1083 → Glu in VP1 of O/Fujian/CHA/9/99tc, respectively. Nonetheless, the introduced mutation Leu-2080 → Gln in VP2 of O/Fujian/CHA/9/99tc for the construction of expectant recombinant plasmid led to non-infectious progeny virus in baby hamster kidney 21 (BHK-21) cells, and the site-directed mutant encoding Glu-1083 → Lys in VP1 of O/Tibet/CHA/6/99tc did not acquire the ability to produce plaques on WT-CHO cells.Significant differences in the inhibition of the infectivity of four HS-utilizing viruses by heparin and RGD-containing peptide were observed in BHK-21 cells.Interestingly, the chimeric virus encoding VP0 of O/Fujian/CHA/9/99tc, and the site-directed mutant encoding Gln-2080 → Leu in VP2 of O/Tibet/CHA/6/99tc could bind to HS, but there was no expression of the 3A protein of these two viruses in WT-CHO cells.ConclusionThe results suggest that the cooperation of certain specific amino acid residues in the capsid proteins of these two cell-adapted PanAsia-1 strains is essential for viral infectivity, the heparin affinity and the capability on FMDV-HS interaction.

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Monoclonal antibodies, against O1 serotype foot-and-mouth disease virus, from a natural bovine host, recognize similar antigenic features to those defined by the mouse.

Cited by 41 publications

References 45 publications

Genetic heterogeneity in the leader and P1-coding regions of foot-and-mouth disease virus serotypes A and O in Africa

Genetic heterogeneity in the leader and P1-coding regions of foot-and-mouth disease virus serotypes A and O in Africa

Evaluation of immune responses of stabilised SAT2 antigens of foot-and-mouth disease in cattle

Effects of two amino acid substitutions in the capsid proteins on the interaction of two cell-adapted PanAsia-1 strains of foot-and-mouth disease virus serotype O with heparan sulfate receptor

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