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Gene Review

VP3  -  guanylyltransferase

Rotavirus C

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Disease relevance of VP3

  • The VP3 gene of human group C rotavirus [1].
  • It was found that incorporation of the inner capsid proteins into single-shelled particles occurred rapidly, while VP7 and VP3 appeared in mature double-shelled particles with a lag time of 10 to 15 min [2].
  • The geometric mean titer of serum neutralizing antibody to a reassortant virus (CJN-M) that contained VP7 of CJN and VP3 of another human rotavirus was 12.7 times less than that of antibody to CJN before infection and 20.3 times less after infection [3].
  • The primary translation product predicted on the basis of the plasmid construction was a hybrid protein in which the 98 amino-terminal amino acids of phage MS2 polymerase were followed by amino acids 42 to 387 of the VP3 protein, which included the region containing the cleavage sites associated with trypsin enhancement of infectivity [4].
  • Vaccination with double-shelled SA11 virions also elicited cross-reacting antibodies to the outer shell proteins VP3 and/or VP7 which neutralized rotavirus seven times more efficiently than antisera to single-shelled SA11 virus [5].

High impact information on VP3

  • Analysis of single (VP3)-gene-substitution reassortants indicated that VP3 was as potent an immunogen as VP7 [6].
  • The nucleotide sequence of the VP3 gene of porcine rotavirus OSU [7].
  • The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core [8].
  • Here, we have characterized the RNA-binding activity of VP3, a minor protein component of the core of rotavirions that has been proposed to function as the viral guanylyltransferase and to direct the capping of the 11 transcripts synthesized from the segmented double-stranded RNA (dsRNA) genome of these viruses [9].
  • The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3 [10].

Biological context of VP3

  • Alignment with the porcine group C VP3 equivalent gene showed the human gene is one amino acid longer, and that the proteins have 84.1% amino acid sequence identity [1].
  • Analogy with the group A rotaviruses suggested that the genome segment 4 encodes the group C rotavirus guanylyltransferase [1].
  • Cleavage of VP3 was not required for virus assembly, and specific cleavage of the polypeptides occurred only on assembled particles [11].
  • These data suggest that such a phenotype is not due to alteration of a VP3 function related to transcription [12].
  • This indicates that viral morphogenesis is halted after the initial viral transcription and before RNA replication, suggesting that VP3 may be required as part of the replicase system but not for subviral particle assembly [12].

Anatomical context of VP3


Associations of VP3 with chemical compounds

  • In addition, there is conservation of arginine at the two trypsin cleavage sites as well as conservation of clusters of amino acids in different regions of the two VP3 cleavage products, VP8 and VP5 [15].
  • This reassortant derived 10 genes, including gene 4 encoding VP3, from the OSU strain and only gene 9, encoding a major neutralization glycoprotein (VP7), from the Gottfried strain and was thus designated VP3:5; VP7:4 [16].
  • UV cross-linking showed that VP3 specifically binds SAM [17].

Regulatory relationships of VP3

  • Analysis of single gene 4 substitution reassortants confirmed our previous finding that VP3 was as potent in stimulating neutralizing antibodies as VP7 [18].

Other interactions of VP3

  • Characterization of VP1, VP2 and VP3 gene segments of a human rotavirus closely related to porcine strains [19].
  • Partial characterization of its remaining VP1, VP2 and VP3 genes along with a porcine rotavirus strain (HP140) uncovered their close genetic relation to porcine strains [19].
  • The presence of VP6 with VPdelta2 did not result in encapsidation of VP1 and VP3 [10].
  • We propose that the genome segment 3 product be called VP3 and that the gene 4 product be named VP4 from now on [20].

Analytical, diagnostic and therapeutic context of VP3


  1. The VP3 gene of human group C rotavirus. Samarbaf-Zadeh, A.R., Lambden, P.R., Green, S.M., Deng, Y., Caul, E.O., Clarke, I.N. Virus Genes (1996) [Pubmed]
  2. Two forms of VP7 are involved in assembly of SA11 rotavirus in endoplasmic reticulum. Kabcenell, A.K., Poruchynsky, M.S., Bellamy, A.R., Greenberg, H.B., Atkinson, P.H. J. Virol. (1988) [Pubmed]
  3. Relative concentrations of serum neutralizing antibody to VP3 and VP7 proteins in adults infected with a human rotavirus. Ward, R.L., Knowlton, D.R., Schiff, G.M., Hoshino, Y., Greenberg, H.B. J. Virol. (1988) [Pubmed]
  4. Synthesis in Escherichia coli and immunological characterization of a polypeptide containing the cleavage sites associated with trypsin enhancement of rotavirus SA11 infectivity. Arias, C.F., Lizano, M., López, S. J. Gen. Virol. (1987) [Pubmed]
  5. Cross-neutralizing antibodies induced by single serotype vaccination of cows with rotavirus. Brüssow, H., Walther, I., Fryder, V., Sidoti, J., Bruttin, A. J. Gen. Virol. (1988) [Pubmed]
  6. Independent segregation of two antigenic specificities (VP3 and VP7) involved in neutralization of rotavirus infectivity. Hoshino, Y., Sereno, M.M., Midthun, K., Flores, J., Kapikian, A.Z., Chanock, R.M. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  7. The nucleotide sequence of the VP3 gene of porcine rotavirus OSU. Nishikawa, K., Gorziglia, M. Nucleic Acids Res. (1988) [Pubmed]
  8. Rotavirus nonstructural protein NSP5 interacts with major core protein VP2. Berois, M., Sapin, C., Erk, I., Poncet, D., Cohen, J. J. Virol. (2003) [Pubmed]
  9. RNA-binding and capping activities of proteins in rotavirus open cores. Patton, J.T., Chen, D. J. Virol. (1999) [Pubmed]
  10. The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3. Zeng, C.Q., Estes, M.K., Charpilienne, A., Cohen, J. J. Virol. (1998) [Pubmed]
  11. Proteolytic enhancement of rotavirus infectivity: molecular mechanisms. Estes, M.K., Graham, D.Y., Mason, B.B. J. Virol. (1981) [Pubmed]
  12. Function of rotavirus VP3 polypeptide in viral morphogenesis. Vásquez, M., Sandino, A.M., Pizarro, J.M., Fernández, J., Valenzuela, S., Spencer, E. J. Gen. Virol. (1993) [Pubmed]
  13. Infectious rotavirus enters cells by direct cell membrane penetration, not by endocytosis. Kaljot, K.T., Shaw, R.D., Rubin, D.H., Greenberg, H.B. J. Virol. (1988) [Pubmed]
  14. Identification of cytotoxic T cell epitopes on the VP3 and VP6 rotavirus proteins. Franco, M.A., Lefevre, P., Willems, P., Tosser, G., Lintermanns, P., Cohen, J. J. Gen. Virol. (1994) [Pubmed]
  15. Sequence of the fourth gene of human rotaviruses recovered from asymptomatic or symptomatic infections. Gorziglia, M., Green, K., Nishikawa, K., Taniguchi, K., Jones, R., Kapikian, A.Z., Chanock, R.M. J. Virol. (1988) [Pubmed]
  16. Infection immunity of piglets to either VP3 or VP7 outer capsid protein confers resistance to challenge with a virulent rotavirus bearing the corresponding antigen. Hoshino, Y., Saif, L.J., Sereno, M.M., Chanock, R.M., Kapikian, A.Z. J. Virol. (1988) [Pubmed]
  17. Rotavirus open cores catalyze 5'-capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase. Chen, D., Luongo, C.L., Nibert, M.L., Patton, J.T. Virology (1999) [Pubmed]
  18. Analysis by plaque reduction neutralization assay of intertypic rotaviruses suggests that gene reassortment occurs in vivo. Hoshino, Y., Sereno, M.M., Midthun, K., Flores, J., Chanock, R.M., Kapikian, A.Z. J. Clin. Microbiol. (1987) [Pubmed]
  19. Characterization of VP1, VP2 and VP3 gene segments of a human rotavirus closely related to porcine strains. Varghese, V., Ghosh, S., Das, S., Bhattacharya, S.K., Krishnan, T., Karmakar, P., Kobayashi, N., Naik, T.N. Virus Genes (2006) [Pubmed]
  20. Identification of the simian rotavirus SA11 genome segment 3 product. Liu, M., Offit, P.A., Estes, M.K. Virology (1988) [Pubmed]
  21. Cross-reactive neutralization epitopes on VP3 of human rotavirus: analysis with monoclonal antibodies and antigenic variants. Taniguchi, K., Morita, Y., Urasawa, T., Urasawa, S. J. Virol. (1987) [Pubmed]
  22. Sequence analysis of the guanylyltransferase (VP3) of group A rotaviruses. Cook, J.P., McCrae, M.A. J. Gen. Virol. (2004) [Pubmed]
  23. Characterization of rotavirus guanylyltransferase activity associated with polypeptide VP3. Pizarro, J.L., Sandino, A.M., Pizarro, J.M., Fernández, J., Spencer, E. J. Gen. Virol. (1991) [Pubmed]
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