Identification of anigenic epitopes on the foot and mouth disease virus isolate O1/Manisa/Turkey/69 using monoclonal antibodies

A sparse hierarchical Bayesian model for detecting relevant antigenic sites in virus evolution

“…In the VP1 Cterminus we have identified VP1 207, VP1 208, VP1 209, VP1 210 and VP1 211 which are part of a region known to be antigenic in all FMDV serotypes except Asia1 (Aktas and Samuel 2000;Grazioli et al 2006;Lea et al 1994;Saiz et al 1991). With the conjugate SABRE method identifying all these neighbouring residues, it suggests that this section of the protein is a highly antigenic part of the SAT2 serotype.…”

“…The VP2 B-C loop is antigenic in all serotypes and contains the highly antigenic VP2 72 residue, which has been experimentally validated in all of the FMDV serotypes except SAT2 (Aktas and Samuel 2000;Crowther et al 1993a;Grazioli et al 2006Grazioli et al , 2013Kitson et al 1990;Lea et al 1994;Saiz et al 1991). The VP1 C-terminus has been proven to be antigenic in all but the Asia1 serotype, although it is almost certainly antigenic there also (Aktas and Samuel 2000;Baxt et al 1989;Grazioli et al 2006;Mateu 1995). Figure 8a shows the model predictions for the antigenically significant branches based on using just the branch variables from the original SAT1 dataset.…”

“…Firstly we include any residues which have been experimentally validated as important within the SAT1 serotype by monoclonal antibody escape mutant studies (MAbs) (Grazioli et al 2006). Secondly, we include those residues which are part of cords of connected experimentally validated antigenic residues for four or more different serotypes; VP1 140-169 (part of the VP1 G-H loop), VP1 200-224 (VP1 C terminus), VP2 70-82 (VP2 B-C loop) and VP3 56-61 (VP3 B-B knob) (Aktas and Samuel 2000;Barnett et al 1989;Crowther et al 1993a;Baxt et al 1989;Bolwell et al 1989;Grazioli et al 2006Grazioli et al , 2013Lea et al 1994;Kitson et al 1990;Mateu 1995;Saiz et al 1991;Thomas et al 1988a, b). As antigenic sites have been found in a large number of different individual locations, we include additional information from other serotypes when classifying whole loops due the similar structure of the different serotypes.…”

Novel antibody binding determinants on the capsid surface of serotype O foot-and-mouth disease virus

“…Several studies have been carried out in the past two decades to identify the targets on the virus surface for the binding of neutralizing antibodies, and monoclonal antibodies (mAbs) have been powerful tools for identifying the amino acid footprint of different antigenic sites, mainly by sequencing mAb-resistant (mar) mutants. This approach has been used successfully to delineate the neutralizing antigenic sites of viruses representing different serotypes (Aktas & Samuel, 2000; Baxt et al , 1989; Crowther et al , 1993; Kitson et al , 1990; Mahapatra et al , 2011; Maree et al , 2013; Mateu et al , 1990; Xie et al , 1987). FMDV serotype O has been studied most extensively, where five neutralizing antigenic sites (1–5) have been identified on its surface, involving three of the capsid proteins (VP1–3).…”

Engineering foot-and-mouth disease virus serotype O IND R2/1975 for one-step purification by immobilized metal affinity chromatography

“…Viral RNA was extracted from the infected BHK-21 cell lysates using the QIAmp Viral RNA mini Kit (Qiagen, Germany) and the capsid coding region of the viral genome was reverse transcribed and amplified using the SuperScript ® III one-step RT-PCR kit (Invitrogen, USA) and the primer set L463F and NK61R [23]. Sequencing reaction was performed using the purified PCR amplicon and the BIG Dye Terminator v.3.1 cycle sequencing kit (Applied Biosystems, USA).…”