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

doi:10.1074/jbc.M500662200

CORC > 北京大学 > 生命科学学院

	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
	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).