NDLI: Triplet amino acids located at positions 145/146/147 of the RNA polymerase of very virulent infectious bursal disease virus contribute to viral virulence.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gao, Li Li, Kai Qi, Xiaole Gao, Honglei Gao, Yulong Qin, Liting Wang, Yongqiang Shen, Nan Kong, Xiangang Wang, Xiaomei
Description	Author Affiliation: Gao L ( Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, PR China.)
Abstract	Infectious bursal disease virus (IBDV) causes an economically significant disease of chickens worldwide. The emergence of very virulent IBDV (vvIBDV) has brought more challenges for effective prevention of this disease. The molecular basis for the virulence of vvIBDV is not fully understood. In this study, 20 IBDV strains were analysed phylogenically and clustered in three branches based on their full-length B segments. The amino acid triplet located at positions 145/146/147 of VP1 was found highly conserved in branch I non-vvIBDVs as asparagine/glutamic acid/glycine (NEG), in branch II vvIBDVs as threonine/glutamic acid/glycine (TEG) and in branch III vvIBDVs as threonine/aspartic acid/asparagine (TDN). Further studies showed that the three amino acids play a critical role in the replication and pathogenicity of vvIBDV. Substitution of the TDN triplet with TEG or NEG reduced viral replication and pathogenicity of the vvIBDV HuB-1 strain in chickens. However, the replication of the attenuated IBDV Gt strain was reduced in chicken embryo fibroblast cells, whilst it was enhanced in the bursa by substituting NEG with TEG or TDN. The exchange of the three amino acids was also found to be capable of affecting the polymerase activity of VP1. The important role of segment B in the pathogenicity of IBDV was confirmed in this study. These results also provided new insights into the mechanism of the virulence of vvIBDVs and may offer new targets for their attenuation to develop potential vaccines using reverse genetics.
File Format	HTM / HTML
ISSN	00221317
Issue Number	Pt 4
Volume Number	95
e-ISSN	14652099
Journal	Journal of General Virology
Language	English
Publisher	Microbiology Society
Publisher Date	2014-04-01
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Research Support, Non-u.s. Gov't Discipline Virology Virulence Cells, Cultured Dna-directed Rna Polymerases Phylogeny Virulence Factors Amino Acids Mutagenesis, Site-directed Journal Article Viral Structural Proteins Virology Pathogenicity Infectious Bursal Disease Virus Animals Virus Replication Chickens Fibroblasts Genetics Bursa Of Fabricius Amino Acid Substitution Cluster Analysis Dna Mutational Analysis
Content Type	Text
Resource Type	Article
Subject	Virology

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