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Cross-Neutralization of Human and Palm Civet Severe Acute Respiratory Syndrome Coronaviruses by Antibodies Targeting the Receptor-Binding Domain of Spike Protein

Yuxian He, Jingjing Li, Wenhui Li, Sara Lustigman, Michael Farzan and Shibo Jiang
J Immunol May 15, 2006, 176 (10) 6085-6092; DOI: https://doi.org/10.4049/jimmunol.176.10.6085
Yuxian He
*Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021; and
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Jingjing Li
*Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021; and
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Wenhui Li
† Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, MA 01772
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Sara Lustigman
*Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021; and
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Michael Farzan
† Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, MA 01772
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Shibo Jiang
*Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021; and
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Abstract

The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is considered as a protective Ag for vaccine design. We previously demonstrated that the receptor-binding domain (RBD) of S protein contains multiple conformational epitopes (Conf I-VI) that confer the major target of neutralizing Abs. Here we show that the recombinant RBDs derived from the S protein sequences of Tor2, GD03, and SZ3, the representative strains of human 2002–2003 and 2003–2004 SARS-CoV and palm civet SARS-CoV, respectively, induce in the immunized mice and rabbits high titers of cross-neutralizing Abs against pseudoviruses expressing S proteins of Tor2, GD03, and SZ3. We also demonstrate that the Tor2-RBD induced-Conf I-VI mAbs can potently neutralize both human SARS-CoV strains, Tor2 and GD03. However, only the Conf IV-VI, but not Conf I-III mAbs, neutralize civet SARS-CoV strain SZ3. All these mAbs reacted significantly with each of the three RBD variants (Tor2-RBD, GD03-RBD, and SZ3-RBD) that differ at several amino acids. Regardless, the Conf I-IV and VI epitopes were completely disrupted by single-point mutation of the conserved residues in the RBD (e.g., D429A, R441A, or D454A) and the Conf III epitope was significantly affected by E452A or D463A substitution. Interestingly, the Conf V epitope, which may overlap the receptor-binding motif and induce most potent neutralizing Abs, was conserved in these mutants. These data suggest that the major neutralizing epitopes of SARS-CoV have been apparently maintained during cross-species transmission, and that RBD-based vaccines may induce broad protection against both human and animal SARS-CoV variants.

  • Received January 11, 2006.
  • Accepted February 23, 2006.
  • Copyright © 2006 by The American Association of Immunologists
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The Journal of Immunology: 176 (10)
The Journal of Immunology
Vol. 176, Issue 10
15 May 2006
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Cross-Neutralization of Human and Palm Civet Severe Acute Respiratory Syndrome Coronaviruses by Antibodies Targeting the Receptor-Binding Domain of Spike Protein
Yuxian He, Jingjing Li, Wenhui Li, Sara Lustigman, Michael Farzan, Shibo Jiang
The Journal of Immunology May 15, 2006, 176 (10) 6085-6092; DOI: 10.4049/jimmunol.176.10.6085

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Cross-Neutralization of Human and Palm Civet Severe Acute Respiratory Syndrome Coronaviruses by Antibodies Targeting the Receptor-Binding Domain of Spike Protein
Yuxian He, Jingjing Li, Wenhui Li, Sara Lustigman, Michael Farzan, Shibo Jiang
The Journal of Immunology May 15, 2006, 176 (10) 6085-6092; DOI: 10.4049/jimmunol.176.10.6085
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