Source: http://www.gentaurpub.com/Mouse-Anti-Foot-and-Mouth-Disease-Virus-Serotype-O1/TW91c2UgQW50aS1Gb290LWFuZC1Nb3V0aCBEaXNlYXNlIFZpcnVzIFNlcm90eXBlIE8x.html
Timestamp: 2019-04-24 18:37:26+00:00

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Identification of antigenic epitopes on the foot and mouth disease virus isolate O1/Manisa/Turkey/69 using monoclonal antibodies.
A panel of mouse monoclonal antibodies (MAbs) was produced against a strain of type O foot and mouth disease virus (FMDV) from the Middle East, O1/Manisa/Turkey/69. Seven neutralising MAbs were fully characterised and all were found to react with conformational epitopes. Monoclonal antibody neutralisation-resistant mutants (MARMs) were generated from the parental virus stock and the complete capsid sequences of these MARMs were determined. Sequence analysis revealed that five of the MARMs had amino acid substitutions at either residue 72 or 73 of VP2 (beta B-beta C loop), indicating that five of the MAbs were directed against antigenic site 2. The sixth MARM contained a single amino acid substitution at position 198 of VP1 (carboxy-terminal region). The seventh MARM contained two amino acid substitutions, at position 72 of VP2 and position 149 of VP1 (beta G-beta H loop). These findings indicate that MAbs directed against a type O FMDV from the Middle East recognise residues in the same structural features to those raised against strains from Europe of the same serotype.
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Analysis of clinical and environmental strains of nontoxigenic Vibrio cholerae for susceptibility to CTXPhi: molecular basis for origination of new strains with epidemic potential.
Toxigenic Vibrio cholerae strains are lysogens of CTXPhi, a filamentous phage which encodes cholera toxin. The receptor for CTXPhi for invading V. cholerae cells is the toxin-coregulated pilus (TCP), the genes for which reside in a larger genetic element, the TCP pathogenicity island. We analyzed 146 CTX-negative strains of V. cholerae O1 or non-O1 isolated from patients or surface waters in five different countries for the presence of the TCP pathogenicity island, the regulatory gene toxR, and the CTXPhi attachment sequence attRS, as well as for susceptibility of the strains to CTXPhi, to investigate the molecular basis for the emergence of new clones of toxigenic V. cholerae. DNA probe or PCR assays for tcpA, tcpI, acfB, toxR, and attRS revealed that 6.85% of the strains, all of which belonged to the O1 serogroup, carried the TCP pathogenicity island, toxR, and multiple copies of attRS, whereas the remaining 93.15% of the strains were negative for TCP but positive for either one or both or neither of toxR and attRS. An analysis of the strains for susceptibility to CTXPhi, using a genetically marked derivative of the phage CTX-KmPhi, showed that all TCP-positive CTX-negative strains and 1 of 136 TCP-negative strains were infected by the phage either in vitro or in the intestines of infant mice. The phage genome integrated into the chromosome of infected V. cholerae O1 cells forming stable lysogens. Comparative analysis of rRNA gene restriction patterns revealed that the lysogens derived from nontoxigenic progenitors were either closely related to or distinctly different from previously described clones of toxigenic V. cholerae. To our knowledge, this is the first demonstration of lysogenic conversion of naturally occurring nontoxigenic V. cholerae strains by CTXPhi. The results of this study further indicated that strains belonging to the O1 serogroup of V. cholerae are more likely to possess the TCP pathogenicity island and hence to be infected by CTXPhi, leading to the origination of potential new epidemic clones.
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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.
Eight neutralizing and two non-neutralizing anti-foot-and-mouth disease virus (FMDV) bovine IgG1 and IgG2 monoclonal antibodies (BMAbs) recognize conformationally dependent epitopes. The majority of those shown to neutralize virus passively protected mice from virus challenge, regardless of isotype. Well-characterized anti-FMDV mouse MAbs, representing five independent neutralizing epitopes on O1 serotype virus, were examined with each of the ten BMAbs in a competition-based ELISA. Five of the neutralizing BMAbs (C48, C65, C74, C83 and MH6) were shown to be directed against epitopes on, or in close proximity to, that previously defined as neutralizing antigenic site 2. Another neutralizing BMAb, MH5, bound to an epitope on, or in close proximity to antigenic site 3. Two neutralizing BMAbs (C2 and C96) simultaneously abrogated the binding of mouse antibodies to sites 2 and 4, contesting the autonomous nature of these two regions. None of the BMAbs were shown to be directed towards the immunodominant antigenic site 1. Sequence analyses of neutralization escape mutants supported the competition ELISA results, and included changes at site 2 (VP2 aa C78Y), site 3 (VP1 N46S) and site 4 (VP3 E58K). Additionally, a substitution at a previously unrecorded location (VP2 aa T1881) prevented the binding of site 2 (C48) and sites 2 and 4 (C2) directed BMAbs. Although the bovine and murine anti-FMDV repertoires may not be identical these results support the recognition of similar antigenic features. This is the first report characterizing anti-FMDV MAbs produced from a natural target host, the cow.
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Antigenic relationships of foot-and-mouth disease virus serotype Asia-1 isolates demonstrated by monoclonal antibodies.
A panel (26) of monoclonal antibodies (MAbs) was elicited against three distinct isolates of foot-and-mouth disease virus (FMDV) serotype Asia-1. Each MAb was characterized according to the location of its epitope: Class I, restricted to the intact virion (140S); Class II, restricted to 140S and the virion protein subunit (12Sps); Class III, available on 140S, 12Sps and virus protein 1; Class IV, restricted to 12Sps. In addition, the MAbs were further categorized by isotype, neutralization of viral infectivity, capacity to bind in radioimmunoassay and precipitation in the Ouchterlony reaction. Neutralization of FMDV infectivity by a MAb of the IgA isotype is reported for the first time. A minimum of seven distinct neutralization epitopes were described on FMDV Asia-1. Some of the neutralizing MAbs bound FMDVs in addition to those that they neutralized. The MAbs defined epitopes common to FMDV serotypes Asia-1, A, O1 and C but neutralizing capacity was restricted to serotype Asia-1. Class IV MAbs defined epitopes highly conserved throughout the FMDV serotypes. Identification of FMDV neutralization epitopes makes possible the direct selection of optimal FMDV strains for vaccine fabrication. In addition, these data are crucial to the design of future synthetic vaccines.
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