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10.1042/BSR20203837

http://scihub22266oqcxt.onion/10.1042/BSR20203837
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33305306!7796194!33305306
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suck abstract from ncbi


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pmid33305306      Biosci+Rep 2021 ; 41 (1): ä
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  • Structural assessment of SARS-CoV2 accessory protein ORF7a predicts LFA-1 and Mac-1 binding potential #MMPMID33305306
  • Nizamudeen ZA; Xu ER; Karthik V; Halawa M; Arkill KP; Jackson AM; Bates DO; Emsley J
  • Biosci Rep 2021[Jan]; 41 (1): ä PMID33305306show ga
  • ORF7a is an accessory protein common to SARS-CoV1 and the recently discovered SARS-CoV2, which is causing the COVID-19 pandemic. The ORF7a protein has a structural homology with ICAM-1 which binds to the T lymphocyte integrin receptor LFA-1. As COVID-19 has a strong immune component as part of the disease, we sought to determine whether SARS-CoV2 would have a similar structural interaction with LFA-1. Using molecular docking simulations, we found that SARS-CoV2 ORF7a has the key structural determinants required to bind LFA-1 but also the related leukocyte integrin Mac-1, which is also known to be expressed by macrophages. Our study shows that SARS-CoV2 ORF7a protein has a conserved Ig immunoglobulin-like fold containing an integrin binding site that provides a mechanistic hypothesis for SARS-CoV2's interaction with the human immune system. This suggests that experimental investigation of ORF7a-mediated effects on immune cells such as T lymphocytes and macrophages (leukocytes) could help understand the disease further and develop effective treatments.
  • |Binding Sites[MESH]
  • |COVID-19/*immunology[MESH]
  • |Humans[MESH]
  • |Lymphocyte Function-Associated Antigen-1/chemistry/*immunology[MESH]
  • |Macrophage-1 Antigen/chemistry/*immunology[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Protein Conformation[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |SARS-CoV-2/chemistry/*immunology[MESH]


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