The structural characterization and antigenicity of the S protein of SARS-CoV |
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Authors: | Li Jingxiang Luo Chunqing Deng Yajun Han Yujun Tang Lin Wang Jing Ji Jia Ye Jia Jiang Fanbo Xu Zhao Tong Wei Wei Wei Zhang Qingrun Li Shengbin Li Wei Li Hongyan Li Yudong Dong Wei Wang Jian Bi Shengli Yang Huanming |
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Affiliation: | Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China. |
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Abstract: | The corona-like spikes or peplomers on the surface of the virion under electronic microscope are the most striking features of coronaviruses. The S (spike) protein is the largest structural protein, with 1,255 amino acids, in the viral genome. Its structure can be divided into three regions: a long N-terminal region in the exterior, a characteristic transmembrane (TM) region, and a short C-terminus in the interior of a virion. We detected fifteen substitutions of nucleotides by comparisons with the seventeen published SARS-CoV genome sequences, eight (53.3%) of which are non-synonymous mutations leading to amino acid alternations with predicted physiochemical changes. The possible antigenic determinants of the S protein are predicted, and the result is confirmed by ELISA (enzyme-linked immunosorbent assay) with synthesized peptides. Another profound finding is that three disulfide bonds are defined at the C-terminus with the N-terminus of the E (envelope) protein, based on the typical sequence and positions, thus establishing the structural connection with these two important structural proteins, if confirmed. Phyloge-netic analysis reveals several conserved regions that might be potent drug targets. |
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Keywords: | SARS coronavirus the S protein structure antigenicity |
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