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Structural and functional analysis of an inter-Spike bivalent neutralizing antibody against SARS-CoV-2 variants.
Li, Yaning; Fan, Qing; Zhou, Bing; Shen, Yaping; Zhang, Yuanyuan; Cheng, Lin; Qi, Furong; Song, Shuo; Guo, Yingying; Yan, Renhong; Ju, Bin; Zhang, Zheng.
  • Li Y; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Zhejiang Province, Hangzhou 310024, China.
  • Fan Q; Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
  • Zhou B; Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Guangdong Province, Shenzhen 518112, China.
  • Shen Y; The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Guangdong Province, Shenzhen 518112, China.
  • Zhang Y; Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Guangdong Province, Shenzhen 518112, China.
  • Cheng L; The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Guangdong Province, Shenzhen 518112, China.
  • Qi F; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Zhejiang Province, Hangzhou 310024, China.
  • Song S; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Zhejiang Province, Hangzhou 310024, China.
  • Guo Y; Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Guangdong Province, Shenzhen 518112, China.
  • Yan R; The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Guangdong Province, Shenzhen 518112, China.
  • Ju B; Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Guangdong Province, Shenzhen 518112, China.
  • Zhang Z; The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Guangdong Province, Shenzhen 518112, China.
iScience ; 25(6): 104431, 2022 Jun 17.
Article in English | MEDLINE | ID: covidwho-1851361
ABSTRACT
The different variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have attracted most public concern because they caused "wave and wave" COVID-19 pandemic. The initial step of viral infection is mediated by the SARS-CoV-2 Spike (S) protein, which mediates the receptor recognition and membrane fusion between virus and host cells. Neutralizing antibodies (nAbs) targeting the S protein of SARS-CoV-2 have become promising candidates for clinical intervention strategy, while multiple studies have shown that different variants have enhanced infectivity and antibody resistance. Here, we explore the structure and function of STS165, a broadly inter-Spike bivalent nAb against SARS-CoV-2 variants and even SARS-CoV, contributing to further understanding of the working mechanism of nAbs.
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Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Topics: Variants Language: English Journal: IScience Year: 2022 Document Type: Article Affiliation country: J.isci.2022.104431

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Topics: Variants Language: English Journal: IScience Year: 2022 Document Type: Article Affiliation country: J.isci.2022.104431