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Crystallization of SARS Coronavirus 3CL Protease to Identify Inhibitor Targets
Author(s) -
Fernandes Samantha Zinnia,
Anson Brandon,
Mesecar Andrew
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.493.4
Subject(s) - outbreak , virology , coronavirus , protease , virus , sars virus , biology , protease inhibitor (pharmacology) , covid-19 , medicine , infectious disease (medical specialty) , disease , enzyme , viral load , biochemistry , pathology , antiretroviral therapy
The SARS coronavirus has been identified as the pathogen responsible for the 2003 outbreak of severe acute respiratory syndrome (SARS). This highly contagious virus, which most likely originated in Southern China, has since been found in over 32 countries, affecting about 8,500 people, and killed over 900 patients. Due to SARS ease of transmission through aerosols and the virus's high mortality rate (~10%), its reemergence is recognized as a looming threat to global health. However, neither a vaccine nor effective treatment exists to combat the illness in the event of another outbreak. The virus's 3 Chymotrypsin‐like main protease, is a major target for inhibitor studies, as it is crucial to viral replication through its proteolytic processing of polyprotein 1ab (pp1ab) at 11 different cleavage sites. This project worked to optimize the crystallization conditions for the SARS 3CL protease for use in X‐ray fragment based screening to identify possible inhibitors. The results of this step in the drug discovery study for the SARS‐CoV can be used as a basis for pioneering new scaffolds for inhibitor studies in other coronaviruses. Support or Funding Information Funding from NSF DBI “REU Site: Molecular and Biochemical Analysis of Proteins” to Purdue University, Purdue College of Biochemistry, and the Purdue College of Agriculture This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .