JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhou, T.
Right arrow Articles by Luo, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhou, T.
Right arrow Articles by Luo, M.

 Previous Article  |  Next Article 

Journal of Virology, July 2004, p. 7217-7226, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.7217-7226.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

An Exposed Domain in the Severe Acute Respiratory Syndrome Coronavirus Spike Protein Induces Neutralizing Antibodies

Tong Zhou,1 Hong Wang,1 Danlin Luo,2 Thomas Rowe,3 Zheng Wang,1 Robert J. Hogan,3 Shihong Qiu,2 Robert J. Bunzel,2 Guoqiang Huang,4 Vinod Mishra,4 Thomas G. Voss,3 Robert Kimberly,1 and Ming Luo2*

Division of Clinical Immunology and Rheumatology, Department of Medicine,1 Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294,2 Division of Homeland Security and Emerging Infectious Diseases Research, Southern Research Institute, Birmingham, Alabama 35205-5305 ,3 Southern Biotechnology Associates, Birmingham, Alabama 352094

Received 12 November 2003/ Accepted 19 February 2004

Exposed epitopes of the spike protein may be recognized by neutralizing antibodies against severe acute respiratory syndrome (SARS) coronavirus (CoV). A protein fragment (S-II) containing predicted epitopes of the spike protein was expressed in Escherichia coli. The properly refolded protein fragment specifically bound to the surface of Vero cells. Monoclonal antibodies raised against this fragment recognized the native spike protein of SARS CoV in both monomeric and trimeric forms. These monoclonal antibodies were capable of blocking S-II attachment to Vero cells and exhibited in vitro antiviral activity. These neutralizing antibodies mapped to epitopes in two peptides, each comprising 20 amino acids. Thus, this region of the spike protein might be a target for generation of therapeutic neutralizing antibodies against SARS CoV and for vaccine development to elicit protective humoral immunity.


* Corresponding author. Mailing address: Department of Microbiology, University of Alabama at Birmingham, Room 111, 1025 18th St. South, Birmingham, AL 35294. Phone: (205) 934-4259. Fax: (205) 975-9578. E-mail: mingluo{at}uab.edu.


Journal of Virology, July 2004, p. 7217-7226, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.7217-7226.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2004 by the American Society for Microbiology. All rights reserved.