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Exceptionally potent cross-reactive neutralization of Nipah and Hendra viruses by a human monoclonal antibody

  1. Author:
    Zhu, Z.
    Bossart, K. N.
    Bishop, K. A.
    Crameri, G.
    Dimitrov, A. S.
    McEachern, J. A.
    Feng, Y.
    Middleton, D.
    Wang, L. F.
    Broder, C. C.
    Dimitrov, D. S.

  2. Author Address

    Zhu, Zhongyu, Feng, Yang, Dimitrov, Dimiter S.] NCI, CCRNP, Prot Interact Grp, Ctr Canc Res,NIH, Frederick, MD 21702 USA. [Zhu, Zhongyu] NCI, Sci Applicat Int Corp Frederick, Basic Res Program, Frederick, MD 21701 USA. [Bishop, Kimberly A.; Dimitrov, Antony S.; Broder, Christopher C.] Uniformed Serv Univ Hlth Sci, Dept Microbiol & Immunol, Bethesda, MD 20814 USA. [Bossart, Katharine N.; Crameri, Gary, McEachern, Jennifer A.; Middleton, Deborah, Wang, Lin-Fa] Commonwealth Sci & Ind Res Org Livestock Ind, Australian Anim Hlth Lab, Geelong, Vic, Australia. [Bossart, Katharine N.; Crameri, Gary, McEachern, Jennifer A.; Middleton, Deborah, Wang, Lin-Fa] Australian Biosecur Cooperat Res Ctr Emerging Inf, Geelong, Vic, Australia.
    1. Year: 2008
  2. Journal: Journal of Infectious Diseases
    1. 197
    2. 6
    3. Pages: 846-853
  4. Type of Article: Article
  1. Abstract:

    We have previously identified neutralizing human monoclonal antibodies against Nipah virus (NiV) and Hendra virus (HeV) by panning a large nonimmune antibody library against a soluble form of the HeV attachment-envelope glycoprotein G (sG(HeV)). One of these antibodies, m102, which exhibited the highest level of crossreactive neutralization of both NiV and HeVG, was affinity maturated by light-chain shuffling combined with random mutagenesis of its heavy-chain variable domain and panning against sGHeV. One of the selected antibody Fab clones, m102.4, had affinity of binding to sGHeV that was equal to or higher than that of the other Fabs, it was converted to IgG1 and tested against infectious NiV and HeV. It exhibited exceptionally potent and crossreactive inhibitory activity with 50% inhibitory concentrations below 0.04 and 0.6 mu g/ mL, respectively. The virus-neutralizing activity correlated with the binding affinity of the antibody to sG(HeV) and sG(NiV). m102.4 bound a soluble form of NiV G (sG(NiV)) better than it bound sG(HeV), and it neutralized NiV better than HeV, despite being originally selected against sGHeV. These results suggest that m102.4 has potential as a therapeutic agent for the treatment of diseases caused by henipaviruses. It could be also used for prophylaxis and diagnosis, and as a research reagent.

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External Sources

  1. PMID: 18271743

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