About: Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses

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About: Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses
Creator	Chow, Hak-Fun Chuck, Chi-Pang Wong, Kam-Bo David, Chi-Cheong Wan,
Source	Medline; PMC
abstract	BACKGROUND: Coronaviruses (CoVs) can be classified into alphacoronavirus (group 1), betacoronavirus (group 2), and gammacoronavirus (group 3) based on diversity of the protein sequences. Their 3C-like protease (3CL(pro)), which catalyzes the proteolytic processing of the polyproteins for viral replication, is a potential target for anti-coronaviral infection. METHODOLOGY/PRINCIPAL FINDINGS: Here, we profiled the substrate specificities of 3CL(pro) from human CoV NL63 (group 1), human CoV OC43 (group 2a), severe acute respiratory syndrome coronavirus (SARS-CoV) (group 2b) and infectious bronchitis virus (IBV) (group 3), by measuring their activity against a substrate library of 19×8 of variants with single substitutions at P5 to P3' positions. The results were correlated with structural properties like side chain volume, hydrophobicity, and secondary structure propensities of substituting residues. All 3CL(pro) prefer Gln at P1 position, Leu at P2 position, basic residues at P3 position, small hydrophobic residues at P4 position, and small residues at P1' and P2' positions. Despite 3CL(pro) from different groups of CoVs share many similarities in substrate specificities, differences in substrate specificities were observed at P4 positions, with IBV 3CL(pro) prefers P4-Pro and SARS-CoV 3CL(pro) prefers P4-Val. By combining the most favorable residues at P3 to P5 positions, we identified super-active substrate sequences ‘VARLQ↓SGF’ that can be cleaved efficiently by all 3CL(pro) with relative activity of 1.7 to 3.2, and ‘VPRLQ↓SGF’ that can be cleaved specifically by IBV 3CL(pro) with relative activity of 4.3. CONCLUSIONS/SIGNIFICANCE: The comprehensive substrate specificities of 3CL(pro) from each of the group 1, 2a, 2b, and 3 CoVs have been profiled in this study, which may provide insights into a rational design of broad-spectrum peptidomimetic inhibitors targeting the proteases.
has issue date	2011-11-02(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0027228
bibo:pmid	22073294
has license	cc0
sha1sum (hex)	cc33658b1e2bfebb81adf4b6befe9cb37f6f6f16
schema:url	https://doi.org/10.1371/journal.pone.0027228
resource representing a document's title	Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses
has PubMed Central identifier	PMC3206940
has PubMed identifier	22073294
schema:publication	PLoS One
resource representing a document's body	covid:cc33658b1e2bfebb81adf4b6befe9cb37f6f6f16#body_text
is schema:about of	named entity 'IS A' named entity 'INFECTION' named entity 'TARGET' named entity 'POTENTIAL' named entity 'group 1' named entity 'classified' named entity 'group 3' covid:arg/cc33658b1e2bfebb81adf4b6befe9cb37f6f6f16 named entity 'POLYPROTEINS' named entity 'PROTEIN SEQUENCES' named entity 'BASED' named entity 'BETACORONAVIRUS' named entity 'PRO' named entity 'VIRAL REPLICATION' named entity 'CLASSIFIED' named entity 'CORONAVIRUSES' named entity 'GROUP 1' named entity 'LIKE' named entity 'PROTEASES' named entity 'SPECIFICITIES' named entity 'BACKGROUND' named entity 'LIKE' named entity 'THEIR' named entity 'ALPHACORONAVIRUS' named entity 'GAMMACORONAVIRUS' named entity 'SUBSTRATE' named entity 'DIVERSITY' named entity 'CORONAVIRUSES' named entity 'PROTEASE' named entity 'PROTEOLYTIC PROCESSING' named entity 'proteolytic processing' named entity 'protein' named entity 'betacoronavirus' named entity 'catalyzes' named entity 'betacoronavirus' named entity 'Substrate Specificities' named entity 'alphacoronavirus' named entity 'protease inhibitors' named entity 'line defense' named entity 'PyMOL' named entity 'IBV' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'binding pocket' named entity 'DNA sequences' named entity 'HCoV-OC43' named entity 'protease' named entity 'gastroenteritis' named entity 'mouse hepatitis virus' named entity 'active site' named entity 'HCoV-NL63' named entity 'MBP' named entity 'Cys' named entity 'FRET' named entity 'HCoV-NL63' named entity 'HKU1' named entity 'protease' named entity 'broadspectrum' named entity 'Protein' named entity 'mammals' named entity 'hydrophobicity' named entity 'EnVision' named entity 'E. coli' named entity 'IBV' named entity 'FRET' named entity '3CLpro' named entity 'protease' named entity 'cytopathic effects' named entity 'IBV' named entity 'histidine' named entity 'protease' named entity 'proteases' named entity 'protease' named entity 'IBV' named entity 'HCoV-OC43' named entity 'HCoV-NL63' named entity 'SARS-CoV'

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