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10.1016/j.jbc.2022.101710

http://scihub22266oqcxt.onion/10.1016/j.jbc.2022.101710
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35150743!8828381!35150743
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suck abstract from ncbi


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pmid35150743      J+Biol+Chem 2022 ; 298 (3): 101710
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  • Integrin mediates cell entry of the SARS-CoV-2 virus independent of cellular receptor ACE2 #MMPMID35150743
  • Liu J; Lu F; Chen Y; Plow E; Qin J
  • J Biol Chem 2022[Mar]; 298 (3): 101710 PMID35150743show ga
  • Coronavirus disease 2019 (COVID-19) is a highly contagious disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It is broadly accepted that SARS-CoV-2 utilizes its spike protein to recognize the extracellular domain of angiotensin-converting enzyme 2 (ACE2) to enter cells for viral infection. However, other mechanisms of SARS-CoV-2 cell entry may occur. We show quantitatively that the SARS-CoV-2 spike protein also binds to the extracellular domain of broadly expressed integrin alpha5beta1 with an affinity comparable to that of SARS-CoV-2 binding to ACE2. More importantly, we provide direct evidence that such binding promotes the internalization of SARS-CoV-2 into non-ACE2 cells in a manner critically dependent upon the activation of the integrin. Our data demonstrate an alternative pathway for the cell entry of SARS-CoV-2, suggesting that upon initial ACE2-mediated invasion of the virus in the respiratory system, which is known to trigger an immune response and secretion of cytokines to activate integrin, the integrin-mediated cell invasion of SARS-CoV-2 into the respiratory system and other organs becomes effective, thereby promoting further infection and progression of COVID-19.
  • |*COVID-19/metabolism/virology[MESH]
  • |*SARS-CoV-2/metabolism/physiology[MESH]
  • |*Spike Glycoprotein, Coronavirus/metabolism[MESH]
  • |*Virus Internalization[MESH]
  • |Angiotensin-Converting Enzyme 2/genetics/metabolism[MESH]
  • |Humans[MESH]
  • |Integrins/metabolism[MESH]


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