Open AccessPreliminary crystallographic analysis of avian infectious bronchitis virus main protease
Author(s) -
Li Jun,
Shen Wei,
Liao Ming,
Bartlam Mark
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106052341
Subject(s) - polyproteins , infectious bronchitis virus , protease , virology , coronavirus , virus , biology , avian infectious bronchitis virus , viral replication , avian infectious bronchitis , rna dependent rna polymerase , covid-19 , gene , infectious disease (medical specialty) , medicine , enzyme , rna , genetics , disease , biochemistry , pathology
Infectious bronchitis virus (IBV) is the prototype of the genus Coronavirus . It causes a highly contagious disease which affects the respiratory, reproductive, neurological and renal systems of chickens, resulting great economic losses in the poultry industry worldwide. The coronavirus (CoV) main protease (M pro ), which plays a pivotal role in viral gene expression and replication through a highly complex cascade involving the proteolytic processing of replicase polyproteins, is an attractive target for antiviral drug design. In this study, IBV M pro was overexpressed in Escherichia coli . Crystals suitable for X‐ray crystallography have been obtained using microseeding techniques and belong to space group P 6 1 22. X‐ray diffraction data were collected in‐house to 2.7 Å resolution from a single crystal. The unit‐cell parameters were a = b = 119.1, c = 270.7 Å, α = β = 90, γ = 120°. Three molecules were predicted to be present in the asymmetric unit from a calculated self‐rotation function.