Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy | |
Qu, XX ; Hao, P ; Song, XJ ; Jiang, SM ; Liu, YX ; Wang, PG ; Rao, X ; Song, HD ; Wang, SY ; Zuo, Y ; Zheng, AH ; Luo, M ; Wang, HL ; Deng, F ; Wang, HZ ; Hu, ZH ; Ding, MX ; Zhao, GP ; Deng, HK | |
刊名 | journal of biological chemistry
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2005 | |
关键词 | ANGIOTENSIN-CONVERTING ENZYME-2 SARS-CORONAVIRUS AMINOPEPTIDASE-N FUNCTIONAL-CHARACTERIZATION NEUTRALIZING ANTIBODIES EFFICIENT REPLICATION VIRUS TYPE-1 RECEPTOR GLYCOPROTEIN EXPRESSION |
DOI | 10.1074/jbc.M500662200 |
英文摘要 | Severe acute respiratory syndrome coronavirus (SARS-CoV) is a recently identified human coronavirus. The extremely high homology of the viral genomic sequences between the viruses isolated from human (huSARS-CoV) and those of palm civet origin (pcSARSCoV) suggested possible palm civet-to-human transmission. Genetic analysis revealed that the spike ( S) protein of pcSARS-CoV and huSARS-CoV was subjected to the strongest positive selection pressure during transmission, and there were six amino acid residues within the receptor-binding domain of the S protein being potentially important for SARS progression and tropism. Using the single-round infection assay, we found that a two-amino acid substitution (N479K/T487S) of a huSARS-CoV for those of pcSARSCoV almost abolished its infection of human cells expressing the SARS-CoV receptor ACE2 but no effect upon the infection of mouse ACE2 cells. Although single substitution of these two residues had no effects on the infectivity of huSARS-CoV, these recombinant S proteins bound to human ACE2 with different levels of reduced affinity, and the two-amino acid-substituted S protein showed extremely low affinity. On the contrary, substitution of these two amino acid residues of pcSARS-CoV for those of huSRAS-CoV made pcSARS-CoV capable of infecting human ACE2-expressing cells. These results suggest that amino acid residues at position 479 and 487 of the S protein are important determinants for SARS-CoV tropism and animal-to-human transmission.; Biochemistry & Molecular Biology; SCI(E); EI; PubMed; 51; ARTICLE; 33; 29588-29595; 280 |
语种 | 英语 |
内容类型 | 期刊论文 |
源URL | [http://ir.pku.edu.cn/handle/20.500.11897/346078] ![]() |
专题 | 生命科学学院 |
推荐引用方式 GB/T 7714 | Qu, XX,Hao, P,Song, XJ,et al. Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy[J]. journal of biological chemistry,2005. |
APA | Qu, XX.,Hao, P.,Song, XJ.,Jiang, SM.,Liu, YX.,...&Deng, HK.(2005).Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy.journal of biological chemistry. |
MLA | Qu, XX,et al."Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy".journal of biological chemistry (2005). |
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