scholarly journals Identification of Infectious Bursal Disease Virus Quasispecies in Commercial Vaccines and Field Isolates of This Double-Stranded RNA Virus

Virology ◽  
2002 ◽  
Vol 304 (1) ◽  
pp. 105-113 ◽  
Author(s):  
Daral J. Jackwood ◽  
Susan E. Sommer
2009 ◽  
Vol 386 (3) ◽  
pp. 891-901 ◽  
Author(s):  
Daniel Luque ◽  
Irene Saugar ◽  
María Teresa Rejas ◽  
José L. Carrascosa ◽  
José F. Rodríguez ◽  
...  

Author(s):  
Christopher J. Kasanga ◽  
T. Yamaguchi ◽  
H.M. Munang’andu ◽  
P.N. Wambura ◽  
K. Ohya ◽  
...  

Infectious bursal disease virus (IBDV) is a bi-segmented RNA virus, which belongs to the genus Avibirnavirus of the family Birnaviridae. Two serotypes, 1 and 2, exist in IBDV. The serotype 1 IBDVs are the causative agents of infectious bursal disease (IBD) in chickens worldwide and lead to immunosuppression in young birds. Genome re-assortment has been speculated to occur and contribute to the emergence of new IBDV strains. However, evidence was lacking until recently when two re-assortant viruses were detected in China. In this study, we determined the complete nucleotide sequence of an IBDV, designated KZC-104, from a confirmed natural IBD outbreak in Lusaka, Zambia in 2004. The genome consisted of 3074 and 2651 nucleotides in the coding regions of segments A and B, respectively. Alignment of both nucleotide and deduced amino acid sequences, and phylogenetic analysis revealed that the genome segment A of KZC-104 was derived from a very virulent strain, whereas its segment B was derived from a classical attenuated strain. On BLAST search, the full-length segments A and B sequences showed 98% closest nucleotide homology to the very virulent strain D6948 and 99.8% closest nucleotide homology to the classical attenuated strain D78, respectively. This is a unique IBDV reassortant strain, which has emerged in nature involving segment B of a live attenuated vaccine. This observation provides direct evidence for the involvement of vaccine strains in the emergence of reassortant IBDV in the field. Taken together, these findings suggest an additional risk of using live IBDV vaccines, which may act as genetic donors for genome re-assortment. Further studies are required to investigate the epidemiology and biological characteristics of reassortant strains so that the appropriate and safe IBDV vaccines can be recommended.


2009 ◽  
Vol 4 (2) ◽  
pp. e16-e16
Author(s):  
Nazir Ahmed Lone ◽  
Shafqat Fatima Rehmani ◽  
Shahana Urooj Kazmi ◽  
Rana Muzaffar ◽  
Taseer Ahmed Khan ◽  
...  

2004 ◽  
Vol 85 (8) ◽  
pp. 2221-2229 ◽  
Author(s):  
Ursula I. von Einem ◽  
Alexander E. Gorbalenya ◽  
Horst Schirrmeier ◽  
Sven-Erik Behrens ◽  
Tobias Letzel ◽  
...  

Segment B of the bisegmented, double-stranded RNA genome of infectious bursal disease virus (IBDV) encodes the viral protein VP1. This has been presumed to represent the RNA-dependent RNA polymerase (RdRp) as it contains motifs that are typical for the RdRp of plus-strand RNA viruses. Here it is demonstrated that baculovirus-expressed wild-type but not motif A mutated VP1 acts as an RdRp on IBDV-specific RNA templates. Thus, on a plus-strand IBDV segment A cRNA template, minus-strand synthesis occurred in such a way that a covalently linked double-stranded RNA product was generated (by a ‘copy-back’ mechanism). Importantly, enzyme activity was observed only with templates that comprised the 3′ non-coding region of plus-strand RNAs transcribed from IBDV segments A and B, indicating template specificity. RdRp activity was shown to have a temperature optimum of 37 °C and required magnesium ions for enzyme activity. Thus, it has been demonstrated unequivocally that VP1 represents the RdRp of IBDV.


2001 ◽  
Vol 75 (22) ◽  
pp. 10815-10828 ◽  
Author(s):  
José R. Castón ◽  
Jorge L. Martı́nez-Torrecuadrada ◽  
Antonio Maraver ◽  
Eleuterio Lombardo ◽  
José F. Rodrı́guez ◽  
...  

ABSTRACT Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is a double-stranded RNA virus. The IBDV capsid is formed by two major structural proteins, VP2 and VP3, which assemble to form a T=13 markedly nonspherical capsid. During viral infection, VP2 is initially synthesized as a precursor, called VPX, whose C end is proteolytically processed to the mature form during capsid assembly. We have computed three-dimensional maps of IBDV capsid and virus-like particles built up by VP2 alone by using electron cryomicroscopy and image-processing techniques. The IBDV single-shelled capsid is characterized by the presence of 260 protruding trimers on the outer surface. Five classes of trimers can be distinguished according to their different local environments. When VP2 is expressed alone in insect cells, dodecahedral particles form spontaneously; these may be assembled into larger, fragile icosahedral capsids built up by 12 dodecahedral capsids. Each dodecahedral capsid is an empty T=1 shell composed of 20 trimeric clusters of VP2. Structural comparison between IBDV capsids and capsids consisting of VP2 alone allowed the determination of the major capsid protein locations and the interactions between them. Whereas VP2 forms the outer protruding trimers, VP3 is found as trimers on the inner surface and may be responsible for stabilizing functions. Since elimination of the C-terminal region of VPX is correlated with the assembly of T=1 capsids, this domain might be involved (either alone or in cooperation with VP3) in the induction of different conformations of VP2 during capsid morphogenesis.


Virology ◽  
1988 ◽  
Vol 163 (1) ◽  
pp. 240-242 ◽  
Author(s):  
Margaret M. Morgan ◽  
Ian G. Macreadie ◽  
Vincent R. Harley ◽  
Peter J. Hudson ◽  
Ahmed A. Azad

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