Summary: Birnavirus VP2 protein
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Birnaviridae Edit Wikipedia article
|Group:||Group III (dsRNA)|
|Birnavirus RNA dependent RNA polymerase (VP1)|
|Birnavirus VP2 protein|
crystal structure of infectious bursal disease virus vp2 subviral particle
|Birnavirus VP3 protein|
|Birnavirus VP4 protein|
|Birnavirus VP5 protein|
Birnaviridae is a family of viruses. Salmonid fish, young sexually immature chickens, and insects serve as natural hosts. There are currently six species in this family, divided among 4 genera. Diseases associated with this family include: IPNV: infectious pancreatic necrosis in salmonid fish, causes significant losses to the aquaculture industry. chronic infection in adult, and acute viral disease in young salmonid fish.
The Birnaviridae genome encodes several proteins:
Birnaviridae RNA-directed RNA polymerase (VP1), which lacks the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RNA-directed RNA polymerases.
The large RNA segment, segment A, of birnaviruses codes for a polyprotein (N-VP2-VP4-VP3-C)  that is processed into the major structural proteins of the virion: VP2, VP3 (a minor structural component of the virus), and into the putative protease VP4. VP4 protein is involved in generating VP2 and VP3. recombinant VP3 is more immunogenic than recombinant VP2.
Infectious pancreatic necrosis virus (IPNV), a birnavirus, is an important pathogen in fish farms. Analyses of viral proteins showed that VP2 is the major structural and immunogenic polypeptide of the virus. All neutralizing monoclonal antibodies are specific to VP2 and bind to continuous or discontinuous epitopes. The variable domain of VP2 and the 20 adjacent amino acids of the conserved C-terminal are probably the most important in inducing an immune response for the protection of animals.
Non structural protein VP5 is found in RNA segment A. The function of this small viral protein is unknown. It is believed to be involved in influencing apoptosis, but studies are not completely concurring. The protein can not be found in the virion.
Viruses in Birnaviridae are non-enveloped, with icosahedral and Single-shelled geometries, and T=13 symmetry. The diameter is around 70 nm. Genomes are linear and segmented, around 15.2.3-3kb in length. The genome codes for 5 to 6 proteins.
|Genus||Structure||Symmetry||Capsid||Genomic arrangement||Genomic segmentation|
Viral replication is cytoplasmic. Entry into the host cell is achieved by penetration into the host cell. Replication follows the double-stranded RNA virus replication model. Double-stranded rna virus transcription is the method of transcription. Salmonid fish, young sexually immature chickens, and insects serve as the natural host. Transmission routes are contact.
|Genus||Host details||Tissue tropism||Entry details||Release details||Replication site||Assembly site||Transmission|
|Avibirnavirus||Birds||None||Cell receptor endocytosis||Budding||Cytoplasm||Cytoplasm||Contact|
|Aquabirnavirus||Salmonid fish||None||Cell receptor endocytosis||Budding||Cytoplasm||Cytoplasm||Contact|
|Blosnavirus||Blotched snakehead fish||None||Unknown||Budding||Cytoplasm||Cytoplasm||Unknown|
|Entomobirnavirus||Insects: diptera||None||Cell receptor endocytosis||Budding||Cytoplasm||Cytoplasm||Unknown|
- "Viral Zone". ExPASy. Retrieved 12 June 2015.
- ICTV. "Virus Taxonomy: 2014 Release". Retrieved 12 June 2015.
- Shwed PS, Dobos P, Cameron LA, Vakharia VN, Duncan R (May 2002). "Birnavirus VP1 proteins form a distinct subgroup of RNA-dependent RNA polymerases lacking a GDD motif". Virology. 296 (2): 241–250. doi:10.1006/viro.2001.1334. PMID 12069523.
- Jagadish MN, Staton VJ, Hudson PJ, Azad AA (March 1988). "Birnavirus precursor polyprotein is processed in Escherichia coli by its own virus-encoded polypeptide". J. Virol. 62 (3): 1084–7. PMC . PMID 2828658.
- Moon CH, Do JW, Cha SJ, Bang JD, Park MA, Yoo DJ, Lee JM, Kim HG, Chung DK, Park JW (October 2004). "Comparison of the immunogenicity of recombinant VP2 and VP3 of infectious pancreatic necrosis virus and marine birnavirus". Arch. Virol. 149 (10): 2059–68. PMID 15669113.
- Heppell J, Tarrab E, Lecomte J, Berthiaume L, Arella M (December 1995). "Strain variability and localization of important epitopes on the major structural protein (VP2) of infectious pancreatic necrosis virus". Virology. 214 (1): 40–9. doi:10.1006/viro.1995.9956. PMID 8525637.
- Nobiron I, Galloux M, Henry C, Torhy C, Boudinot P, Lejal N, Da Costa B, Delmas B (February 2008). "Genome and polypeptides characterization of Tellina virus 1 reveals a fifth genetic cluster in the Birnaviridae family". Virology. 371 (2): 350–61. doi:10.1016/j.virol.2007.09.022. PMID 17976679.
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Birnavirus VP2 protein Provide feedback
Jagadish MN, Staton VJ, Hudson PJ, Azad AA; , J Virol 1988;62:1084-1087.: Birnavirus precursor polyprotein is processed in Escherichia coli by its own virus-encoded polypeptide. PUBMED:2828658 EPMC:2828658
Heppell J, Tarrab E, Lecomte J, Berthiaume L, Arella M; , Virology 1995;214:40-49.: Strain variability and localization of important epitopes on the major structural protein (VP2) of infectious pancreatic necrosis virus. PUBMED:8525637 EPMC:8525637
This tab holds annotation information from the InterPro database.
InterPro entry IPR002662
Infectious pancreatic necrosis virus (IPNV), a birnavirus, is an important pathogen in fish farms. Analyses of viral proteins showed that VP2 is the major structural and immunogenic polypeptide of the virus [PUBMED:8525637, PUBMED:17976679]. All neutralizing monoclonal antibodies are specific to VP2 and bind to continuous or discontinuous epitopes. The variable domain of VP2 and the 20 adjacent amino acids of the conserved C-terminal are probably the most important in inducing an immune response for the protection of animals [PUBMED:8525637].
The large RNA segment of the Birnaviridae codes for a polyprotein (N-VP2-VP4-VP3-C), most of which is then processed to generate the constituent polypeptides. VP4 protein is involved in generating VP2 and VP3 [PUBMED:2828658]. Recombinant VP3 is more immunogenic than recombinant VP2 [PUBMED:15669113].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||structural molecule activity (GO:0005198)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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The clan contains a set of viral coat protein families and peptidase A6. The only known peptidase activity is an autolytic cleavage releasing a 44-residue C-terminal fragment. The reaction is very slow and only occurs within the assembled virion. There is debate whether this is actually a true peptidase. The virion with these coat or capsid proteins are icosahedral viruses containing sixty triangular coat protein units, each unit consisting of three proteins. The coat protein consists of two subdomains, an eight-stranded beta-barrel on the surface and a three-helix bundle on the inner face.
The clan contains the following 26 members:Astro_capsid_N Birna_VP2 Bromo_coat Calici_coat Calici_coat_C Capsid-VNN Carmo_coat_C Circo_capsid Como_LCP Como_SCP CRPV_capsid Cucumo_coat Dicistro_VP4 Luteo_coat Nepo_coat Nepo_coat_C Nepo_coat_N Peptidase_A21 Peptidase_A6 Pico_P1A Rhv SP2 TT_ORF1 Tymo_coat Viral_coat VP4_2
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Seed source:||Pfam-B_946 (release 4.2)|
|Number in seed:||4|
|Number in full:||4|
|Average length of the domain:||439.00 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||42.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Birna_VP2 domain has been found. There are 61 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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