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The emerging SARS‐CoV‐2 papain‐like protease: Its relationship with recent coronavirus epidemics
Author(s) -
Kandeel Mahmoud,
Kitade Yukio,
Fayez Mahmoud,
Venugopala Katharigatta N.,
Ibrahim Abdelazim
Publication year - 2021
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.26497
Subject(s) - coronavirus , protease , middle east respiratory syndrome coronavirus , virology , papain , catalytic triad , deubiquitinating enzyme , covid-19 , biology , ubiquitin , peptide sequence , proteases , chemistry , enzyme , biochemistry , medicine , gene , disease , pathology , infectious disease (medical specialty)
The papain‐like protease (PL pro ) is an important enzyme for coronavirus polyprotein processing, as well as for virus‐host immune suppression. Previous studies reveal that a molecular analysis of PL pro indicates the catalytic activity of viral PL pro and its interactions with ubiquitin. By using sequence comparisons, molecular models, and protein–protein interaction maps, PL pro was compared in the three recorded fatal CoV epidemics, which involved severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), severe acute respiratory syndrome CoV (SARS‐CoV), and Middle East respiratory syndrome coronavirus (MERS‐CoV). The pairwise sequence comparison of SARS‐CoV‐2 PL pro indicated similarity percentages of 82.59% and 30.06% with SARS‐CoV PL pro and MERS‐CoV PL pro , respectively. In comparison with SARS‐CoV PL pro , in SARS‐CoV‐2, the PL pro had a conserved catalytic triad of C111, H278, and D293, with a slightly lower number of polar interface residues and of hydrogen bonds, a higher number of buried interface sizes, and a lower number of residues that interact with ubiquitin and PL pro . These features might contribute to a similar or slightly lower level of deubiquitinating activity in SARS‐CoV‐2 PLpro. It was, however, a much higher level compared to MERS‐CoV, which contained amino acid mutations and a low number of polar interfaces. SARS‐CoV‐2 PL pro and SARS‐CoV PL pro showed almost the same catalytic site profiles, interface area compositions and polarities, suggesting a general similarity in deubiquitination activity. Compared with MERS‐CoV, SARS‐CoV‐2 had a higher potential for binding interactions with ubiquitin. These estimated parameters contribute to the knowledge gap in understanding how the new virus interacts with the immune system.