2014
DOI: 10.1186/1743-422x-11-136
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Characterization of monoclonal antibodies against foot-and-mouth disease virus serotype O and application in identification of antigenic variation in relation to vaccine strain selection

Abstract: BackgroundFoot-and-mouth disease (FMD) has severe implications for animal farming which leads to considerable financial losses because of its rapid spread, high morbidity and loss of productivity. For these reasons, the use of vaccine is often favoured to prevent and control FMD. Selection of the proper vaccine is extremely difficult because of the antigenic variation within FMDV serotypes. The aim of the current study was to produce a panel of mAbs and use it for the characterization of new isolates of FMDV s… Show more

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Cited by 19 publications
(14 citation statements)
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“…A large polyprotein, encoded by the ORF, is subsequently cleaved by viral proteases (10) to produce four structural polypeptides (VP1-4), with VP1-3 being exposed on the surface of the virus, encapsulating the RNA genome. Of these, the VP1 protein (also referred to as 1D), encoded by, on average, 639 nt, contains several major antigenic determinants (11,12) in addition to playing a number of other critical roles, including viral attachment, cell entry and stimulation of immunity.…”
Section: Foot and Mouth Disease Virus: Genome Organisationmentioning
confidence: 99%
“…A large polyprotein, encoded by the ORF, is subsequently cleaved by viral proteases (10) to produce four structural polypeptides (VP1-4), with VP1-3 being exposed on the surface of the virus, encapsulating the RNA genome. Of these, the VP1 protein (also referred to as 1D), encoded by, on average, 639 nt, contains several major antigenic determinants (11,12) in addition to playing a number of other critical roles, including viral attachment, cell entry and stimulation of immunity.…”
Section: Foot and Mouth Disease Virus: Genome Organisationmentioning
confidence: 99%
“…In order to dissect the discrepancies of individual epitopes on the VLPs and unassembled proteins, a solution competitive ELISA was developed. Four neutralizing mAbs of FMDV, F21-48, F21-64, F21-58, and F21-41, used in the solution competitive ELISA were previously studied ( 17 ), which recognized antigenic site 1 on the G-H loop of VP1 at Amino Acid (aa) 148, and aa 136–151, antigenic site 2 in the region of VP2 at aa 77, and antigenic site 3 of VP1 at aa 43–44, respectively.…”
Section: Resultsmentioning
confidence: 99%
“…The binding abilities of the VLPs and the unassembled capsid proteins were analyzed by four neutralizing monoclonal antibodies (MAbs) of FMDV (F21-48, F21-64, F21-58, and F21-41) provided by Dr. Yang (National Centre for Foreign Animal Disease, Canada) ( 17 ).…”
Section: Methodsmentioning
confidence: 99%
“…Isolation of mAb‐resistant mutants was performed as previously described (Yang, Xu, Goolia, & Zhang, ). Briefly, SVDV (UK 27/72, tissue culture infective dose 10 7 /ml) was mixed with the purified mAb F44SVD–136 and incubated at 37°C for 30 min.…”
Section: Methodsmentioning
confidence: 99%