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Received on June 13, 2003
Accepted on August 29, 2003
Molecular Diagnostics and Genetics |
1 Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300 and James D. Watson Institute of Genome Sciences (WIGS), Zhijiang Campus, Zhejiang University, Hangzhou 310008, China and Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China
2 Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300 and James D. Watson Institute of Genome Sciences (WIGS), Zhijiang Campus, Zhejiang University, Hangzhou 310008, China
3 The Institute of Microbiology and Epidemiology (IME), Chinese Academy of Military Medical Sciences, Beijing 100071, China
4 The Capital Institute of Pediatrics, Beijing 100022, China
5 Department of Medicine, University of Louisville, Louisville, KY 40202
6 Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300 and James D. Watson Institute of Genome Sciences (WIGS), Zhijiang Campus, Zhejiang University, Hangzhou 310008, China and Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300 and Department of Medicine, University of Louisville, Louisville, KY 40202
* To whom correspondence should be addressed. E-mail: siqiliu{at}louisville.edu.
Background: The widespread threat of severe acute respiratory syndrome (SARS) to human life has spawned challenges to develop fast and accurate analytical methods for its early diagnosis and to create a safe antiviral vaccine for preventive use. Consequently, we thoroughly investigated the immunoreactivities with patient sera of a series of synthesized peptides from SARS-coronavirus structural proteins.
Methods: We synthesized 41 peptides ranging in size from 16 to 25 amino acid residues of relatively high hydrophilicity. The immunoreactivities of the peptides with SARS patient sera were determined by ELISA.
Results: Four epitopic sites, S599, M137, N66, and N371-404, located in the SARS-coronavirus S, M, and N proteins, respectively, were detected by screening synthesized peptides. Notably, N371 and N385, located at the COOH terminus of the N protein, inhibited binding of antibodies to SARS-coronavirus lysate and bound to antibodies in >94% of samples from SARS study patients. N385 had the highest affinity for forming peptide-antibody complexes with SARS serum.
Conclusions: Five peptides from SARS structural proteins, especially two from the COOH terminus of the N protein, appear to be highly immunogenic and may be useful for serologic assays. The identification of these antigenic peptides contributes to the understanding of the immunogenicity and persistence of SARS coronavirus.© 2003 American Association for Clinical Chemistry
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