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Publications (2)4.75 Total impact

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    ABSTRACT: Passively administered antibodies to conserved epitopes on the attachment (G) glycoprotein of human respiratory syncytial virus (hRSV) have potential in the immunoprophylaxis of human infections. This study set out to generate monoclonal antibodies (MAbs) recognizing all prevalent lineages of HRSV and capable of immunoprophylaxis in mice. Two murine MAbs of broad specificity for prevalent virus strains were generated by immunization of mice with hRSV of sub-group A followed by selection of hybridomas on recombinant G glycoprotein from a sub-group B virus. The anti-G hybridomas generated secreted antibody of high affinity but negligible neutralizing capacity one of which was tested in mice and found to be protective against live virus challenge. Western blotting and partial epitope mapping on transiently expressed G-glycoprotein fragments indicate that these antibodies recognize a complex epitope on the protein backbone of the molecule involving residues both C'- and N-terminal to the central conserved motif. J. Med. Virol. © 2014 Wiley Periodicals, Inc.
    Journal of Medical Virology 01/2014; · 2.37 Impact Factor
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    ABSTRACT: Little is known of the proteome of human metapneumovirus (HMPV). In this study a panel of monoclonal antibodies to the virus have been characterized and used to identify viral proteins present in infected cell lysates. Of thirteen anti-HMPV monoclonal antibodies four reacted with recombinant fusion glycoprotein and one with recombinant G glycoprotein by immunofuorescence but not in western blots suggesting that they recognize conformation dependent epitopes. The specificity of the remaining antibodies were determined by MALDI/TOF analysis of the proteins they immunoprecipitated from HMPV infected cell lysates and by western blotting. Five MAbs bound to the nucleoprotein and three to the phosphoprotein. In western blots of lysates of cells infected with low passage HMPV, the anti-nucleoprotein MAbs stained a single polypeptide corresponding in size to the full length nucleocapsid protein. On repeated passage of the virus in cell culture, however, a second, smaller band appeared which may result from internal initiation of translation within the nucleocapsid gene as described for avian metapneumovirus. Antibodies to the phosphoprotein, besides the full length form, also recognized multiple polypeptides in infected cell lysates, with patterns differing for the two subtypes A and B. The possibility that these too may derive by internal initiation of translation is discussed.
    Journal of Medical Virology 07/2012; 84(7):1061-70. · 2.37 Impact Factor