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• W2023368387 abstract "Forty-three hybridoma cell lines producing monoclonal antibody to diphtheria toxin were isolated. Based upon their reactivity with various fragments of the toxin and mutant toxin-related proteins, the monoclonal antibodies were subdivided into 10 groups which recognize at least 10 distinct epitopes on the toxin molecule. Specific antibodies directed against both fragments A and B were found to neutralize cytotoxicity, both in vitro and in vivo. Neutralization was found to correlate with antibody-mediated inhibition of toxin binding to its eukaryotic cell surface receptor. The results presented suggest that the Pro378 and/or Gly431 of mature toxin are part of, or close to, the toxin receptor-binding domain. In addition, antigenic determinants in the C-terminal portion of fragment A, as well as a portion of the toxin defined by the tox-3 and tox-45 nonsense mutations (i.e. ca 31,000-42,000 daltons) appear to be juxtaposed to the receptor-binding domain and may form a secondary binding region." @default.
• W2023368387 created "2016-06-24" @default.
• W2023368387 creator A5022651282 @default.
• W2023368387 creator A5036639335 @default.
• W2023368387 date "1984-09-01" @default.
• W2023368387 modified "2023-09-25" @default.
• W2023368387 title "Monoclonal antibody analysis of diphtheria toxin—I. Localization of epitopes and neutralization of cytotoxicity" @default.
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• W2023368387 doi "https://doi.org/10.1016/0161-5890(84)90165-2" @default.
• W2023368387 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6207425" @default.
• W2023368387 hasPublicationYear "1984" @default.
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