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The structural basis of accelerated host cell entry by SARS‐CoV‐2†
Author(s) -
Seyran Murat,
Takayama Kazuo,
Uversky Vladimir N.,
Lundstrom Kenneth,
Palù Giorgio,
Sherchan Samendra P.,
Attrish Diksha,
Rezaei Nima,
Aljabali Alaa A. A.,
Ghosh Shinjini,
Pizzol Damiano,
Chauhan Gaurav,
Adadi Parise,
Mohamed Abd ElAziz Tarek,
Soares Antonio G.,
Kandimalla Ramesh,
Tambuwala Murtaza,
Hassan Sk. Sarif,
Azad Gajendra Kumar,
Pal Choudhury Pabitra,
BaetasdaCruz Wagner,
SerranoAroca Ángel,
Brufsky Adam M.,
Uhal Bruce D.
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15651
Subject(s) - viral entry , protein subunit , furin , biology , coronavirus , microbiology and biotechnology , proteases , viral protein , receptor , viral structural protein , virology , binding domain , plasma protein binding , virus , binding site , viral replication , biochemistry , enzyme , covid-19 , gene , medicine , disease , pathology , infectious disease (medical specialty)
Severe acute respiratory syndrome coronavirus 2 pandemic capacity is derived from the unique structural features on its spike protein: fast viral surfing over the epithelium with flat N‐terminal domain, tight binding to ACE2 entry receptor, and furin protease utilization. In addition, the possible involvement of other components such as lipid rafts, CLRs, and neuropilin is, in combination, mediating the accelerated cell entry and other critical steps in its overwhelming contagious capacity and pandemy.