A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C

Mateu, M. G.; Martı́nez, Miguel Ángel; Capucci, Lorenzo; Andreu, David; Giralt, Ernest; Sánchez‐Madrid, Francisco; Brocchi, Emiliana; Domingo, Esteban

doi:10.1099/0022-1317-71-3-629

Cited by 182 publications

(179 citation statements)

References 44 publications

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“…Another relevant finding of the present work is that antigenic cross-reactivity may be strongly dependent on the assay format, as shown by the comparison of our results with earlier enzyme immuno-electrotransfer blot (EITB) (using capsid protein VP1 [3]) and enzyme immunodot (EID) (using a peptide-KLH conjugate [13]) data. Similar problems have been observed earlier and discussed on the basis that the microscopic environment supporting the peptide (e.g.…”

Section: Rele6ance Of Conformation In Linear Antigenic Sitessupporting

confidence: 58%

“…In serotype C, neutralizing antiAbbre6iations: 2D-1 H NMR, two-dimensional proton nuclear magnetic resonance; AA, amino acid residue; AAA, amino acid analysis; Ahx, 6-aminohexanoic acid; AM, 2-[4-aminomethyl-(2,4-dimethoxyphenyl)]phenoxyacetic acid (linker); C A , analyte concentration; DdHa, conformational chemical shift for proton a; DIEA, diisopropylethylamine; DMF, N,N%-dimethylformamide; EDC, N-ethyl-N%-dimethylaminopropylcarbodiimide; EID, enzyme immunodot; EITB, enzyme immuno-electrotransfer blot; ESIMS, electrospray ionization mass spectrometry; Et 3 Si, triethylsilane; Fab, fragment antigen binding; FMDV, foot-and-mouth disease virus; Fmoc, 9-fluorenylmethoxycarbonyl; HPLC, high performance liquid chromatography; IC 50 , 50% inhibition concentration; k a , association rate constant (M − 1 s − 1 ); K A , association thermodynamic constant (M − 1 ); k d , dissociation rate constant (s − 1 ); K D , dissociation thermodynamic constant (M); KLH, keyhole limpet hemocyanin; K i , solution affinity constant (M − 1 ); mAb, monoclonal antibody; MALDI-TOF MS, matrix-assisted laser desorption -time-of-flight mass spectrometry; MBHA, p-methylbenzhydrylamine resin; MeCN, acetonitrile; NHS, N-hydroxysuccinimide; NMM, N-methylmorpholine; NOE, nuclear Overhauser effect; PBS, phosphate buffer saline; R eq , equilibrium response; RI, bulk refractive index; R immob , immobilization response; R max , maximum response (RU); RPLC, reverse phase liquid chromatography; RU, resonance units; SPPS, solid phase peptide synthesis; SPR, surface plasmon resonance; t Bu, tert-butyl; TBTU, 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate; TFA, trifluoroacetic acid; TFE, 2,2,2-trifluoroethanol.…”

Section: Introductionmentioning

confidence: 99%

“…bodies recognize FMDV GH loop (residues 136-150 of capsid protein VP1 [2]), which includes several overlapping linear epitopes [3] and is also termed antigenic site A. Site A includes highly conserved residues, such as an Arg-Gly-Asp (RGD) motif, and two leucines ( 144 Leu, 147 Leu), which are deeply involved in cell and antibody recognition events [4].…”

Section: Introductionmentioning

confidence: 99%

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Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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Foot-and-mouth disease virus (FMDV) isolate C 1 -Barcelona (or C-S30) includes four replacements within its immunodominant site (GH loop, residues 136-150 of capsid protein VP1, YTTSTRGDLAHVTAT), relative to reference strain C-S8c1 (YTASAR-GDLAHLTTT). Although one of the mutations in C-S30 ( 147 Leu Val) is known to be detrimental for antibody recognition, reactivity of this isolate with the neutralizing monoclonal antibody (mAb) 4C4, raised against FMDV C 1 -Brescia (GH loop: YTASTRGDLAHLTAT), was indistinguishable from those of strains C-S8c1 or C 1 -Brescia. A structural interpretation for these somewhat striking findings is available, based on the observation that 15-residue peptides reproducing the C-S30 and C-S8c1 GH loops adopt very similar, quasi-circular, conformations in crystal complexes with 4C4. Nevertheless, surface plasmon resonance (SPR) kinetic analyses of the interactions between these peptides and three anti-GH loop mAbs have now revealed that the linear C-S30 peptides were less antigenic in solution than their C-S8c1 and C 1 -Brescia counterparts. We have, therefore, tried to modulate peptide antigenicity in solution by cyclization. Functional SPR and structural two dimensional proton nuclear magnetic resonance (2D-1 H NMR) studies of both linear and cyclic peptide antigens are discussed here. Conformation seems to have an important role in peptide antigenicity, even when continuous (i.e. linear) antigenic sites are involved.

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Section: Rele6ance Of Conformation In Linear Antigenic Sitessupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Gomes

Giralt

Andreu

2001

Vaccine

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“…1), previously proposed to be essential for the viability of FMDV. The 86 mutants isolated from FMDV C-S8c1 (Table 1), together with many field viruses and laboratory variants sequenced (29,36,(38)(39)(40)(41)(42) should be sufficient to consider FMDV of serotype C highly intolerant to amino acid substitutions at the RGD motif and several contiguous residues. Work with peptides indicates that, in addition to the RGD triplet, neighboring residues 144, 145, and 147 are also involved in receptor recognition of C-S8c1 (13), thus explaining their high degree of conservation.…”

Section: Discussionmentioning

confidence: 99%

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Martı́nez

Verdaguer

Mateu

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

119

117

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Aphthoviruses use a conserved Arg-Gly-Asp triplet for attachment to host cells and this motif is believed to be essential for virus viability. Here we report that this triplet-which is also a widespread motif involved in cell-tocell adhesion-can become dispensable upon short-term evolution of the virus harboring it. Foot-and-mouth disease virus (FMDV), which was multiply passaged in cell culture, showed an altered repertoire of antigenic variants resistant to a neutralizing monoclonal antibody. The altered repertoire includes variants with substitutions at the Arg-Gly-Asp motif. Mutants lacking this sequence replicated normally in cell culture and were indistinguishable from the parental virus. Studies with individual FMDV clones indicate that amino acid replacements on the capsid surface located around the loop harboring the Arg-Gly-Asp triplet may mediate in the dispensability of this motif. The results show that FMDV quasispecies evolving in a constant biological environment have the capability of rendering totally dispensable a receptor recognition motif previously invariant, and to ensure an alternative pathway for normal viral replication. Thus, variability of highly conserved motifs, even those that viruses have adapted from functional cellular motifs, can contribute to phenotypic f lexibility of RNA viruses in nature.

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“…Site C (about 15 residues) is located in the carboxy terminal of VP1. The third site, Site D, which is the major antigenic site of type C [38], includes the B-C loop of VP2 (residues 70-80) and the B-B knob of VP3 (residues 56-61) and part of carboxy-terminal (residue 193) of VP1.…”

Section: Fmdv Genomementioning

confidence: 99%

Foot-and-mouth Disease: Global Status and Future Road Map for Control and Prevention in India

et al. 2012

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Foot-and-mouth disease (FMD) is a transboundary, economically devastating and highly contagious viral disease of livestock, most importantly cattle, buffalo and pig. The disease also affects goats, sheep, wild ruminant species and elephants. The causative FMD virus is antigenically diverse having seven distinct serotypes and many variants within them. Being a single stranded RNA virus, it confirms the quasispecies nature with emergences and reemergences of different genetic lineages with altered antigenicity within the serotypes, making vaccination based control programme a high cost effective, time consuming and difficult to achieve. As per the OIE and FAO, the disease is a major threat to food security of the world, and particularly the countries having the disease are more prone to food insecurity. Further, FMD free status is an indicator of development, and all developed countries are free from it. The disease is endemic in India and three serotypes of the virus viz; O, A and Asia1 are circulating. Annual direct loss due to FMD in India has been estimated at Rs. 20,000 crores. Many countries in the world are now free from FMD with or without vaccination and presence of the disease in other neighboring countries is a major threat to them. Countries having FMD face trade barrier posed by FMD free countries, causing heavy economic loss to the livestock industry. Progressive control pathway has been developed by FAO for global eradication of FMD. Vaccination based FMD control programme is in operation in India which involves biannual vaccinations of all cattle and buffaloes in selected areas, regular active surveillance and antibody monitoring in vaccinated population with the objective of creating FMD free zones. At present, the disease occurrence, severity of the clinical disease and number of outbreaks have progressively and substantially declined in the control zones as a result of last 10 rounds of vaccination with an oil adjuvanted trivalent inactivated vaccine. In this review, FMD scenario in India and in the world is briefed. Besides, the measures taken for the control and eradication of this devastating disease is presented. Besides, the initial success achieved through the FMD control programme in India, a road map for the control and eradication of FMD at national level is discussed.

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A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C

Cited by 182 publications

References 44 publications

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Antigenicity modulation upon peptide cyclization: application to the GH loop of foot-and-mouth disease virus strain C1-Barcelona

Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus

Foot-and-mouth Disease: Global Status and Future Road Map for Control and Prevention in India

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