Picornavirus Capsid Proteins. 2020 May;21(3):e50. However, a 27 nucleotide region that encodes a glycine-rich domain at the N-terminal region of VP2 was deleted in the PPV-NE/09 strain. Major capsid protein VP1 is a viral protein that is the main component of the polyomavirus capsid.VP1 monomers are generally around 350 amino acids long and are capable of self-assembly into an icosahedral structure consisting of 360 VP1 molecules organized into 72 pentamers. Help. NLM Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Zheng HH, Wang LQ, Fu PF, Zheng LL, Chen HY, Liu F. Virol J. Vet. Infect Genet Evol. Major splicing isoform produced by deletion of the initiating AUG for VP1 and downstream translation of VP2. Viruses. Subgenomic RNA encodes the capsid protein and VP2 minor structural protein which is expressed through RNA termination-reinitiation. Expression of the outer capsid protein, VP2, from a full length cDNA clone of genome segment 2 of bluetongue serotype 1 from South Africa, using both Sp6 and vaccinia expression systems and a comparison of the nucleic acid sequence of this segment with those of other serotypes. Oh WT, Kim RY, Nguyen VG, Chung HC, Park BK. Despite evidence that the Norwalk virus (NV) minor structural protein VP2 is present in infectious virions, the available crystallographic and electron cryomicroscopy structures of NV have not revealed the location of VP2. USA.gov. Genome Announc. 1C ), consistent with only VP3 being essential for capsid assembly ( 9 ). Protein sets from fully sequenced genomes. The capsid is composed 60 asymmetric units made of 2 protein (T=2*), for a total of 120 capsid proteins. The VP2 gene encoded a 570aa-long protein which could be recognized by anti-PPV-VP2 monoclonal antibody 3C9. Sci. The version number for both the entry and the canonical sequence are also displayed.
,This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (reviewed) or to the computer-annotated TrEMBL section (unreviewed).
,This section contains any relevant information that doesn't fit in any other defined sections
, The European Molecular Biology Laboratory, State Secretariat for Education, Research and Innovation, adhesion receptor-mediated virion attachment to host cell, clathrin-dependent endocytosis of virus by host cell, entry receptor-mediated virion attachment to host cell, microtubule-dependent intracellular transport of viral material towards nucleus, permeabilization of host organelle membrane involved in viral entry into host cell, viral entry via permeabilization of inner membrane, Clathrin-mediated endocytosis of virus by host, Viral attachment to host adhesion receptor, Viral penetration via permeabilization of host membrane, Canis lupus familiaris (Dog) (Canis familiaris), Felis catus (Cat) (Felis silvestris catus). This is also the sequence that appears in the downloadable versions of the entry. UniProtKB. It contains a phospholipase A2-like region and nuclear localization signals that might be exposed by capsid modifications during virus entry (By similarity). of multiple genes (paralogs). in UniProtKB/Swiss-Prot.,This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.
,This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. Annotation systems. Participates in host cell receptor binding together with VP1. A virulent strain NE/09 of porcine parvovirus (PPV) was isolated from mummified swine fetus samples in China and its capsid protein VP2 gene was analyzed. Sequence archive. Phylogenetic analysis of porcine parvoviruses from swine samples in China. UniRef. Viruses. This section is only present in reviewed entries, i.e. 7:592. doi: 10.3389/fvets.2020.00592. According to the phylogenetic relationship of the VP2 gene of PPV-NE/09, the isolate was a new mutant strain of PPV prevailing in China. Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of a combination of VP1 (5‑6 copies) and VP2 (54‑55 copies). The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Participates in host cell receptor binding together with VP1. Protein sets from fully sequenced genomes. Capsid Protein; Protein VP2; View all Topics. Help pages, FAQs, UniProtKB manual, documents, news archive and Biocuration projects. Exposure of nuclear localization signal probably allows nuclear import of capsids (By similarity). capsids contain 360 copies of viral protein 1 (VP1), arranged in 72 pentamers on an icosahedral lattice (Rayment et al., 1982). Useful for immunolocalization studies of capsid formation in combination with monoclonal antibody A20 (Cat.No.
The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) Molecular epidemiology and evolution of porcine parvoviruses. Thus assembly of the outer capsid on the core particle must be a tightly controlled process during virus maturation. It also includes information pertinent to the sequence(s), including length and molecular weight. This … UniRef. This site needs JavaScript to work properly. Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Please enable it to take advantage of the complete set of features! Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. The dominant protein VP2 provides an “anti-receptor”,which The VP2 gene encoded a 570aa-long protein which could be recognized by anti-PPV-VP2 monoclonal antibody 3C9. Perspectives on the Evolution of Porcine Parvovirus. In this study, VP2 gene sequences of CPV-2 were amplified from rectal swabs of 14 diarrhetic raccoon dogs (Nyctereutes procyonoides) in Hebei province, China, in 2016 and 2017. A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VP1 pentamer, has been determined at 2.2 Å resolution. Sequence analysis revealed that the VP2 gene of PPV-NE/09 had close sequence similarity with the VP2 gene of other PPV strains. Porcine parvovirus nonstructural protein NS1 activates NF-κB and it involves TLR2 signaling pathway. An in vitro assembly system was used to investigate the role of VP2 in the assembly of recombinant VP1 pentamers. Unreviewed-Annotation score: -Protein inferred from homology i. The VP1 Capsid Protein of Adeno-Associated Virus Type 2 is Carrying a Phospholipase A2 Domain Required for Virus Infectivity. VP1+VP2 VP3 VP3 clip VP1 VP2 VP3 VP3 clip VP1+VP2+VP3 Ma 59,805 RPLC-MS METHOD OPTIMIZATION AAV capsids are composed of three viral proteins (VP1, VP2, and VP3) at an approximately 1:1:10 ratio with the masses between 50 and 85 kDa. Sequence clusters. Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. UniParc. from the sequence. A complex of the polyomavirus internal protein VP2/ VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli. Additionally, this section gives relevant information on each alternative protein isoform. VP1 and VP2 are products of the same gene that are generated by alternative splicing of viral mRNA but VP1 has an additional 143aa in its N‑terminus compared to VP2. The internal proteins overlap in sequence (Figure 1) and a single copy of either VP2 or VP3 associates with Citation: Mishu ID, Akter S, Alam ASMRU, Hossain MA and Sultana M (2020) In silico Evolutionary Divergence Analysis Suggests the Potentiality of Capsid Protein VP2 in Serotype-Independent Foot-and-Mouth Disease Virus Detection. The much smaller VP4 protein has a more extended structure, and lies at the interface between the capsid and the RNA genome. PepMix™ BKV (capsid protein VP2) References: Read References with PepMix™ Peptide Pools - Infectious Diseases. You are using a version of browser that may not display all the features of this website. Help. Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Protein knowledgebase. Help. VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell. UniProtKB.