TY - JOUR
T1 - Potent neutralization antibody elicited in mice by SARS-associated coronavirus spike protein S1 domain
AU - Zhang, Yun
AU - Yang, Fan
AU - Li, Yan han
AU - Li, Wen hui
AU - Tu, Xin ming
AU - Wei, Qiang
AU - Zhu, Hua
AU - Liu, L.
AU - Wang, Heng
AU - Qin, Chuan
AU - Yuan, Guo yong
AU - He, Wei
AU - Wang, Shu hui
PY - 2004
Y1 - 2004
N2 - OBJECTIVE: To study the antigenicity of SARS associated coronavirus (CoV) spike S1 (12-672Aa) domain. METHODS: BALB/c mice were immunized with a plasmid bearing codon-optimized SARS-CoV (Tor2 strain) S1 domain and then boosted with purified S1 protein; the SARS-CoV specific IgG antibody was tested by ELISA and neutralization antibody was determined by in vitro microneutralization assay. RESULTS: S1 domain of SARS-CoV spike, which has been demonstrated harboring the receptor binding domain, successfully elicited SARS-CoV specific IgG antibody in mouse after combined immunization with DNA and purified S1 protein; the antibody elicited solely by S1 could potently neutralize SARS-CoV (HKU-39849) in vitro, 50% of 1 000 TCID50 SARS-CoV challenged cells were protected from viral infection by a 1:1499.68 dilution of mice sera immunized with S1 protein, but negative control sera showed no protection. CONCLUSION: S1 domain of SARS-CoV spike protein, which is responsible for receptor binding, can efficiently and sufficiently induce highly potent neutralizing antibody in mice. This result suggested that S1 domain could be an effective subunit vaccines against SARS-CoV.
AB - OBJECTIVE: To study the antigenicity of SARS associated coronavirus (CoV) spike S1 (12-672Aa) domain. METHODS: BALB/c mice were immunized with a plasmid bearing codon-optimized SARS-CoV (Tor2 strain) S1 domain and then boosted with purified S1 protein; the SARS-CoV specific IgG antibody was tested by ELISA and neutralization antibody was determined by in vitro microneutralization assay. RESULTS: S1 domain of SARS-CoV spike, which has been demonstrated harboring the receptor binding domain, successfully elicited SARS-CoV specific IgG antibody in mouse after combined immunization with DNA and purified S1 protein; the antibody elicited solely by S1 could potently neutralize SARS-CoV (HKU-39849) in vitro, 50% of 1 000 TCID50 SARS-CoV challenged cells were protected from viral infection by a 1:1499.68 dilution of mice sera immunized with S1 protein, but negative control sera showed no protection. CONCLUSION: S1 domain of SARS-CoV spike protein, which is responsible for receptor binding, can efficiently and sufficiently induce highly potent neutralizing antibody in mice. This result suggested that S1 domain could be an effective subunit vaccines against SARS-CoV.
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M3 - Article
C2 - 15640862
AN - SCOPUS:33746795995
SN - 1003-9279
VL - 18
SP - 258
EP - 260
JO - Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology
JF - Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology
IS - 3
ER -