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Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies

  1. Author:
    Zhu, Z. Y.
    Chakraborti, S.
    He, Y.
    Roberts, A.
    Sheahan, T.
    Xiao, X. D.
    Hensley, L. E.
    Prabakaran, P.
    Rockx, B.
    Sidorov, I. A.
    Corti, D.
    Vogel, L.
    Feng, Y.
    Kim, J. O.
    Wang, L. F.
    Baric, R.
    Lanzavecchia, A.
    Curtis, K. M.
    Nabel, G. J.
    Subbarao, K.
    Jiang, S.
    Dimitrov, D. S.

  2. Author Address

    NIH, Natl Canc Inst, Ctr Canc Res Nanobiol Program, Ft Detrick, MD 21702 USA. NIH, Ctr Canc Res Nanobiol Program, Protein Interact Grp, Ft Detrick, MD 21702 USA. NIH, NCI, SAIC Frederick Inc, Basic Res Program, Ft Detrick, MD 21702 USA. New York Blood Ctr, Lindsley F Kimball Res Inst, Lab Viral Immunol, New York, NY 10021 USA. NIH, NIAID, Lab Infect Dis, Bethesda, MD 20892 USA. NIH, NIAID, Vaccine Res Ctr, Bethesda, MD 20892 USA. Univ N Carolina, Dept Epidemiol, Chapel Hill, NC 27599 USA. United States Army Med Res Inst Infect Dis, Div Virol, Ft Detrick, MD 21702 USA. Inst Res Biomed, CH-6500 Bellinzona, Switzerland. CSIRO, Livestock Ind, Australian Biosecur Cooperat Res Ctr Emerging Inf, Australian Anim Hlth Lab, Geelong, Vic 3220, Australia.;Dimitrov, DS, NIH, Natl Canc Inst, Ctr Canc Res Nanobiol Program, PO Box B,Bldg 469,Room 150B, Ft Detrick, MD 21702 USA.;dimitrov@ncifcrf.gov
    1. Year: 2007
    2. Date: Jul
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 104
    2. 29
    3. Pages: 12123-12128
  4. Type of Article: Article
  5. ISSN: 0027-8424
  1. Abstract:

    The severe acute respiratory syndrome coronavirus (SARS-CoV) caused a worldwide epidemic in late 2002/early 2003 and a second outbreak in the winter of 2003/2004 by an independent animal-to-human transmission. The GD03 strain, which was isolated from an index patient of the second outbreak, was reported to resist neutralization by the human monoclonal antibodies (hmAbs) 80R and S3.1, which can potently neutralize isolates from the first outbreak. Here we report that two hmAbs, m396 and S230.15, potently neutralized GD03 and representative isolates from the first SARS outbreak (Urbani, Tor2) and from palm civets (SZ3, SZ16). These antibodies also protected mice challenged with the Urbani or recombinant viruses bearing the GD03 and SZ16 spike (S) glycoproteins. Both antibodies competed with the SARS-CoV receptor, ACE2, for binding to the receptor-binding domain (RBD), suggesting a mechanism of neutralization that involves interference with the SARS-CoV-ACE2 interaction. Two putative hot-spot residues in the RBD (Ile-489 and Tyr-491) were identified within the SARS-CoV spike that likely contribute to most of the m396-binding energy. Residues Ile-489 and Tyr-491 are highly conserved within the SARS-CoV spike, indicating a possible mechanism of the m396 cross-reactivity. Sequence analysis and mutagenesis data show that m396 might neutralize all zoonotic and epidemic SARS-CoV isolates with known sequences, except strains derived from bats. These antibodies exhibit cross-reactivity against isolates from the two SARS outbreaks and palm civets and could have potential applications for diagnosis, prophylaxis, and treatment of SARSCoV infections.

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External Sources

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  2. DOI: 10.1073/pnas.0701000104
  3. View record in Web of Science®
  4. WOS: 000248199200047

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