%0 Journal Article
%T Proteomic analysis of purified coronavirus infectious bronchitis virus particles
%A Qingming Kong
%A Chunyi Xue
%A Xiangpeng Ren
%A Chengwen Zhang
%A Linlin Li
%A Dingming Shu
%A Yingzuo Bi
%A Yongchang Cao
%J Proteome Science
%D 2010
%I BioMed Central
%R 10.1186/1477-5956-8-29
%X Apart from the virus-encoded structural proteins, we detected 60 host proteins in the purified virions which can be grouped into several functional categories including intracellular trafficking proteins (20%), molecular chaperone (18%), macromolcular biosynthesis proteins (17%), cytoskeletal proteins (15%), signal transport proteins (15%), protein degradation (8%), chromosome associated proteins (2%), ribosomal proteins (2%), and other function proteins (3%). Interestingly, 21 of the total host proteins have not been reported to be present in virions of other virus families, such as major vault protein, TENP protein, ovalbumin, and scavenger receptor protein. Following identification of the host proteins by proteomic methods, the presence of 4 proteins in the purified IBV preparation was verified by western blotting and immunogold labeling detection.The results present the first standard proteomic profile of IBV and may facilitate the understanding of the pathogenic mechanisms.Infectious bronchitis virus (IBV), the coronavirus of domestic chickens that causes acute, highly contagious respiratory disease, is one of the most important causes of economic loss in the poultry industry. IBV is an enveloped virus with continuous, positive and single-stranded RNA genome, which is the largest of any RNA virus characterized[1] and encodes four types of structural proteins. The spike (S) glycoprotein, together with small envelope (E) protein and matrix (M) glycoprotein, consists of the viral envelope, whereas the nucleocapsid (N) protein interacts with genomic RNA of the virus to form the viral nucleocapsid, in the invariable order 5'-S-E-M-N-3'. Proteins S, E, and M have been studied for their important roles in receptor binding and virus budding. S mediates attachment to cellular receptors and entry by fusion with cell membranes, whereas M interacting with S and N proteins is an essential component of virion and plays pivotal roles in virion assembly, budding and maturation
%U http://www.proteomesci.com/content/8/1/29