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AXL is a candidate receptor for SARS-CoV-2 that promotes infection of pulmonary and bronchial epithelial cells.
Wang, Shuai; Qiu, Zongyang; Hou, Yingnan; Deng, Xiya; Xu, Wei; Zheng, Tingting; Wu, Peihan; Xie, Shaofang; Bian, Weixiang; Zhang, Chong; Sun, Zewei; Liu, Kunpeng; Shan, Chao; Lin, Aifu; Jiang, Shibo; Xie, Youhua; Zhou, Qiang; Lu, Lu; Huang, Jing; Li, Xu.
  • Wang S; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Qiu Z; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Hou Y; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Deng X; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Xu W; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Zheng T; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Wu P; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Xie S; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Bian W; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Zhang C; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Sun Z; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Liu K; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Shan C; Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences and Biosafety Level 3 Laboratory, Fudan University, Shanghai, 200032, China.
  • Lin A; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Jiang S; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Xie Y; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Zhou Q; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
  • Lu L; Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, 310024, China.
  • Huang J; Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, Zhejiang, 310024, China.
  • Li X; Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, 310024, China.
Cell Res ; 31(2): 126-140, 2021 02.
Article in English | MEDLINE | ID: covidwho-1015005
ABSTRACT
The current coronavirus disease 2019 (COVID-19) pandemic presents a global public health challenge. The viral pathogen responsible, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), binds to the host receptor ACE2 through its spike (S) glycoprotein, which mediates membrane fusion and viral entry. Although the role of ACE2 as a receptor for SARS-CoV-2 is clear, studies have shown that ACE2 expression is extremely low in various human tissues, especially in the respiratory tract. Thus, other host receptors and/or co-receptors that promote the entry of SARS-CoV-2 into cells of the respiratory system may exist. In this study, we found that the tyrosine-protein kinase receptor UFO (AXL) specifically interacts with the N-terminal domain of SARS-CoV-2 S. Using both a SARS-CoV-2 virus pseudotype and authentic SARS-CoV-2, we found that overexpression of AXL in HEK293T cells promotes SARS-CoV-2 entry as efficiently as overexpression of ACE2, while knocking out AXL significantly reduces SARS-CoV-2 infection in H1299 pulmonary cells and in human primary lung epithelial cells. Soluble human recombinant AXL blocks SARS-CoV-2 infection in cells expressing high levels of AXL. The AXL expression level is well correlated with SARS-CoV-2 S level in bronchoalveolar lavage fluid cells from COVID-19 patients. Taken together, our findings suggest that AXL is a novel candidate receptor for SARS-CoV-2 which may play an important role in promoting viral infection of the human respiratory system and indicate that it is a potential target for future clinical intervention strategies.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Proto-Oncogene Proteins / Receptor Protein-Tyrosine Kinases / Respiratory Mucosa / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Prognostic study Limits: Humans Language: English Journal: Cell Res Year: 2021 Document Type: Article Affiliation country: S41422-020-00460-y

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Proto-Oncogene Proteins / Receptor Protein-Tyrosine Kinases / Respiratory Mucosa / Spike Glycoprotein, Coronavirus / SARS-CoV-2 / COVID-19 Type of study: Prognostic study Limits: Humans Language: English Journal: Cell Res Year: 2021 Document Type: Article Affiliation country: S41422-020-00460-y