Amino acids 1055 to 1192 in the S2 Region of severe acute respiratory syndrome Coronavirus S Protein induce neutralizing antibodies: Implications for the development of vaccines and antiviral agents

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dc.contributor.authorKeng, Choong-Tat
dc.contributor.authorZhang, Aihua
dc.contributor.authorShen, Shuo
dc.contributor.authorLip, Kuo-Ming
dc.contributor.authorFielding, Burtram C.
dc.contributor.authorTan, Timothy H.P.
dc.contributor.authorChou, Chih-Fong
dc.contributor.authorLoh, Chay Boon
dc.contributor.authorWang, Sifang
dc.contributor.authorFu, Jianlin
dc.contributor.authorYang, Xiaoming
dc.contributor.authorLim, Seng Gee
dc.contributor.authorHong, Wanjin
dc.contributor.authorTan, Yee-Joo
dc.date.accessioned2013-10-12T20:28:48Z
dc.date.available2013-10-12T20:28:48Z
dc.date.issued2005
dc.description.abstractThe spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) interacts with cellular receptors to mediate membrane fusion, allowing viral entry into host cells; hence it is recognized as the primary target of neutralizing antibodies, and therefore knowledge of antigenic determinants that can elicit neutralizing antibodies could be beneficial for the development of a protective vaccine. Here, we expressed five different fragments of S, covering the entire ectodomain (amino acids 48 to 1192), as glutathione S-transferase fusion proteins in Escherichia coli and used the purified proteins to raise antibodies in rabbits. By Western blot analysis and immunoprecipitation experiments, we showed that all the antibodies are specific and highly sensitive to both the native and denatured forms of the full-length S protein expressed in virus-infected cells and transfected cells, respectively. Indirect immunofluorescence performed on fixed but unpermeabilized cells showed that these antibodies can recognize the mature form of S on the cell surface. All the antibodies were also able to detect the maturation of the 200-kDa form of S to the 210-kDa form by pulse-chase experiments. When the antibodies were tested for their ability to inhibit SARS-CoV propagation in Vero E6 culture, it was found that the anti-S 10 antibody, which was targeted to amino acid residues 1029 to 1192 of S, which include heptad repeat 2, has strong neutralizing activities, suggesting that this region of S carries neutralizing epitopes and is very important for virus entry into cells.en_US
dc.description.accreditationWeb of Scienceen_US
dc.identifier.citationKeng, C., et al. (2005). Amino acids 1055 to 1192 in the S2 Region of severe acute respiratory syndrome Coronavirus S Protein induce neutralizing antibodies: Implications for the development of vaccines and antiviral agents, Journal of Virology, 79(6): 3289-3296en_US
dc.identifier.issn0022-538X
dc.identifier.urihttp://hdl.handle.net/10566/748
dc.language.isoenen_US
dc.privacy.showsubmitterfalse
dc.publisherAmerican Society for Microbiologyen_US
dc.rightsCopyright American Society for Microbiology. This file may be freely used for educational purposes, as long as it is not altered in any way. Acknowledgement of the authors and the source is required.
dc.source.urihttp://dx.doi.org/10.1128/JVI.79.6.3289-3296.2005
dc.status.ispeerreviewedtrue
dc.titleAmino acids 1055 to 1192 in the S2 Region of severe acute respiratory syndrome Coronavirus S Protein induce neutralizing antibodies: Implications for the development of vaccines and antiviral agentsen_US
dc.typeArticleen_US

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