Disease relevance of VP1

• 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].
• 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 [2].
• 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].
• Based on the dendrogram established from the sequence alignment around the polymerase module region, and sequence identity within the alignment, P1 of plant-infecting RDV was evolutionarily compared with VP1, lambda 3, and VP1 of three other animal-infecting members of the family, rota-, reo-, and bluetongue viruses [4].
• Sequence analysis of VP1 and VP7 genes suggests occurrence of a reassortant of G2 rotavirus responsible for an epidemic of gastroenteritis [5].

High impact information on VP1

• The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core [6].
• Despite their replication-defective phenotype, mutant RNAs with complementary 5' and 3' termini were shown to competitively interfere with the replication of wild-type mRNA and to bind the viral RNA polymerase VP1 as efficiently as wild-type RNA [7].
• 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 [2].
• Photoaffinity labeling of rotavirus VP1 with 8-azido-ATP: identification of the viral RNA polymerase [8].
• Partial nucleotide sequences of the VP1 gene were analysed and appeared to be similar among the major G2 strains from the same epidemic (identity > 98%), whereas the identity of the VP1 genes of the major G2 strains of the 1993 epidemic to those of previous seasons was only about 84% [5].

Biological context of VP1

• The predicted amino acid sequence revealed that VP1 is basic, with a net positive charge of 18 at pH 7 [9].
• The nucleotide sequence of gene segment 1, which encodes VP1 of porcine rotavirus strain Gottfried, was determined [9].
• Gottfried VP1 also shares consensus sequences with certain GTP-binding proteins; however, we could not detect any GTP-binding activity in VP1 [9].
• Phylogenetic analysis of the VP1/2A region showed the presence of a unique sequence: genotype IA [10].

Other interactions of VP1

• Characterization of VP1, VP2 and VP3 gene segments of a human rotavirus closely related to porcine strains [11].
• Monospecific polyclonal antisera were raised in guinea-pigs against the calf rotavirus polypeptides VP1, VP2, VP3 + 4, VP4.2, VP6, VP7.1, VP7.2 and VP10 [12].
• The amino acid sequence homology between PO-13 and mammalian rotaviruses ranged from 76-77% (VP1) to 16-18% (NSP1) [13].

Analytical, diagnostic and therapeutic context of VP1

• 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 [14].
• DSP-crosslinking of infected cell lysates and immunoprecipitation also revealed that NS35 interacts with the putative viral RNA polymerase VP1 [15].

References