Disease relevance of VP2

• The VP1 protein is the most highly conserved between the rotaviruses of groups A and C. The genome segment 2 encodes the VP2 protein [1].
• Rather, the formation of initiation complexes also requires the core lattice protein (VP2), a virion component that forms a T = 1 icosahedral shell that encapsidates the segmented dsRNA genome [2].
• Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer [3].
• To further define the role of VP1 and VP2 in the synthesis of dsRNA from viral mRNA, recombinant baculoviruses containing gene 1 (rBVg1) and gene 2 (rBVg2) of SA11 rotavirus were generated and used to express recombinant VP1 (rVP1) and rVP2, respectively [4].
• Binding did not appear to be nucleotide sequence specific, because RNA from uninfected cells and an unrelated RNA virus bound to VP2 and to NS31 as did rotavirus RNA [5].

High impact information on VP2

• Coexpression of VP2 and VP6 produces double layered VLP [6].
• Nucleotide sequence of the gene encoding for the RNA binding protein (VP2) of RF bovine rotavirus [7].
• In this study, we show that NSP5 interacts with VP2 in infected cells [8].
• The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3 [9].
• The amino terminus of the innermost capsid protein VP2 possesses a nonspecific single-stranded RNA and dsRNA binding activity, and the amino terminus is also essential for the incorporation of the polymerase enzyme VP1 and guanylyltransferase VP3 into the core of the virion [3].

Biological context of VP2

• The VLPs maintained the structural and functional characteristics of native particles, as determined by electron microscopic examination of the particles, the presence of nonneutralizing and neutralizing epitopes on VP4 and VP7, and hemagglutination activity of the VP2/4/6/7 VLPs [10].
• We have shown that rotavirus 2/6 viruslike particles composed of proteins VP2 and VP6 (2/6-VLPs) administered to mice intranasally with cholera toxin (CT) induced protection from rotavirus challenge, as measured by virus shedding [11].
• For bovine rotavirus, the evidence suggests that, of all the virus-specific proteins, VP2 and NS31 are most likely to interact with RNA during transcription and replication or virus assembly or both [5].
• Comparison of the VP1 and VP2 amino acid sequences with those determined for other strains indicates that certain features of these proteins are conserved [12].
• Comparative sequence analysis indicated that the ts phenotype of tsF VP2 is due to an Ala-->Asp substitution at position 387 [13].

Anatomical context of VP2

• In contrast to expression in eukaryotic cells, VP6 and VP2 did not form virus-like particles in our bacterial system [14].

Associations of VP2 with chemical compounds

• Electrophoretic analysis indicated that replicase particles, purified by centrifugation on CsCl and glycerol gradients, were similar to SS particles, containing the structural proteins VP1, VP2, and VP6 [15].

Physical interactions of VP2

• Rotavirus cores contain the double-stranded RNA (dsRNA) genome, RNA polymerase VP1, and guanylyltransferase VP3 and are enclosed within a lattice formed by the RNA-binding protein VP2 [4].
• The ability of VP6 to interact with VP2 was examined by several assays, including electron microscopy, coimmunoprecipitation, purification of VLP2/6, and monitoring of the transcriptase activity of reconstituted DLP [16].

Regulatory relationships of VP2

• To locate the amino terminus of VP2 within the core, we have used electron cryomicroscopy and image reconstruction to determine the three-dimensional structures of recombinant virus-like particles that contain either full-length or amino-terminal-deleted forms of VP2 coexpressed with the intermediate capsid protein VP6 [3].

Other interactions of VP2

• Characterization of VP1, VP2 and VP3 gene segments of a human rotavirus closely related to porcine strains [17].
• The data presented showed evidence, for the first time, of an interaction between VP2 and a nonstructural rotavirus protein [8].
• Self-assembled virus like particles (VLPs) composed by VP2, VP6 and VP7 rotavirus proteins (VLPs 2/6/7) were produced in 5l scale using the insect cells/baculovirus expression system [18].
• Viral proteins involved in RNA replication include the RNA polymerase (VP1), the core scaffold protein (VP2) and the non-structural RNA-binding proteins (NSP2 and NSP5) [19].

Analytical, diagnostic and therapeutic context of VP2

• To determine which of the core proteins, VP1, VP2, or VP3, recognizes the template mRNA during RNA replication, SA11 open cores were incubated with 32P-labeled RNA probes of viral and nonviral origin and the reaction mixtures were analyzed for the formation of RNA-protein complexes by gel mobility shift assay [20].
• Analysis of expressed rVP2 particles by SDS-PAGE showed these particles were composed of three major VP2-related proteins, called bands A, B, and C, with apparent molecular weights of 94K, 85K, and 77K, respectively [21].
• Peptide mapping revealed that all three proteins were related to VP2 [22].
• Virus-like particles containing the rotavirus (RV) internal proteins VP2 and VP6 (2/6-VLP) have been shown to induce serum and fecal antibodies as well as protection in mice after intranasal administration with a mutant of E. coli toxin, LT-R192G [23].
• A polymerase chain reaction (PCR) assay was used to detect and differentiate picornaviruses (PVs), using primers homologous to the 5' non-coding and VP2 regions of the PV genome [24].

References