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Gene Review

RMVgp4  -  coat protein

Ribgrass mosaic virus

 
 
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Disease relevance of CP

  • The internal ribosome entry sites (IRES), IRES(CP,148)(CR) and IRES(MP,75)(CR), precede the coat protein (CP) and movement protein (MP) genes of crucifer-infecting tobamovirus (crTMV), respectively [1].
  • Expression of tobacco mosaic virus (TMV) coat protein (CP) in plants confers resistance to infection by TMV and related tobamoviruses [2].
  • The replacement of the CP gene in RNA 3 by a mutant gene encoding a CP defective in virion formation did not affect cell-to-cell transport of the chimera's with a functional MP [3].
  • The activities of the bromovirus 3a proteins were enhanced by coexpression of the cognate CP but the activity of CMV 3a Delta C33 was not [4].
  • Complementation of movement-deficient potato virus X (PVX) coat protein (CP) mutants, namely PVX.CP-Xho lacking the 18 C-terminal amino acid residues and PVX.DeltaCP lacking the entire CP gene, was studied by transient co-expression with heterologous proteins [5].
 

High impact information on CP

  • The results suggest that wt CP has a positive effect on the production of MP, whereas the CP(T42W) has a negative effect on MP accumulation and/or function [2].
  • It was previously shown that, unlike the type member of the genus Tobamovirus (TMV U1), a crucifer-infecting tobamovirus (crTMV) contains a 148 nt internal ribosome entry site (IRES)(CP,148)(CR) upstream of the coat protein (CP) gene [6].
  • (ii) "deltaNPT-CP" transcripts contained partially truncated neomycin phosphotransferase I gene and CP gene [7].
  • Frameshift mutations designed to cause premature termination of translation were introduced into either the 30-kDa movement protein (MP) gene or the coat protein (CP) gene [8].
  • Phylogenetic analysis of these CP ORFs resulted in a tree with three clusters each containing at least one of the approved species RMV, TVCV and 1ptYoMV/WMoV in which our isolates were distributed [9].
 

Biological context of CP

  • The 126/183-kDa RNA-dependent RNA polymerase (RdRp), 33-kDa movement protein (MP) and 18-kDa coat protein (CP) cistrons are located at nt 63-3401/4901, 4807-5718, and 5721-6197 on the genome, respectively [10].
  • An environmentally safe Tobacco Mosaic Virus (TMV)-based expression replicon was constructed that lacks movement protein (MP) and coat protein (CP), and which expresses the green fluorescent protein (GFP) gene from a full CP subgenomic promoter [11].
  • The nucleotide and amino acid sequences of the CP of CMMoV were 39.6% to 49.2% and 25.8% to 40.3% identical to other seventeen tobamoviruses, respectively [12].
  • In this study, a TMV-based vector was designed such that a fragment encoding 15 amino acids of the poliovirus peptide (PVP) derived from the viral capsid proteins VP3 and VP1 of poliovirus type 1 Sabin was inserted downstream of the six-base 3' context nucleotide sequence of the TMV coat protein (CP) gene [13].

References

  1. Polypurine (A)-rich sequences promote cross-kingdom conservation of internal ribosome entry. Dorokhov, Y.L., Skulachev, M.V., Ivanov, P.A., Zvereva, S.D., Tjulkina, L.G., Merits, A., Gleba, Y.Y., Hohn, T., Atabekov, J.G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. Characterization of mutant tobacco mosaic virus coat protein that interferes with virus cell-to-cell movement. Bendahmane, M., Szecsi, J., Chen, I., Berg, R.H., Beachy, R.N. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Cell-to-cell movement of Alfalfa mosaic virus can be mediated by the movement proteins of Ilar-, bromo-, cucumo-, tobamo- and comoviruses and does not require virion formation. Sánchez-Navarro, J.A., Carmen Herranz, M., Pallás, V. Virology (2006) [Pubmed]
  4. Cucumovirus- and bromovirus-encoded movement functions potentiate cell-to-cell movement of tobamo- and potexviruses. Tamai, A., Kubota, K., Nagano, H., Yoshii, M., Ishikawa, M., Mise, K., Meshi, T. Virology (2003) [Pubmed]
  5. Cell-to-cell movement of potato virus X involves distinct functions of the coat protein. Fedorkin, O., Solovyev, A., Yelina, N., Zamyatnin, A., Zinovkin, R., Mäkinen, K., Schiemann, J., Yu Morozov, S. J. Gen. Virol. (2001) [Pubmed]
  6. An internal ribosome entry site located upstream of the crucifer-infecting tobamovirus coat protein (CP) gene can be used for CP synthesis in vivo. Dorokhov, Y.L., Ivanov, P.A., Komarova, T.V., Skulachev, M.V., Atabekov, J.G. J. Gen. Virol. (2006) [Pubmed]
  7. A tobamovirus genome that contains an internal ribosome entry site functional in vitro. Ivanov, P.A., Karpova, O.V., Skulachev, M.V., Tomashevskaya, O.L., Rodionova, N.P., Dorokhov YuL, n.u.l.l., Atabekov, J.G. Virology (1997) [Pubmed]
  8. In vivo complementation of infectious transcripts from mutant tobacco mosaic virus cDNAs in transgenic plants. Holt, C.A., Beachy, R.N. Virology (1991) [Pubmed]
  9. The phylogenetic structure of the cluster of tobamovirus species serologically related to ribgrass mosaic virus (RMV) and the sequence of streptocarpus flower break virus (SFBV). Heinze, C., Lesemann, D.E., Ilmberger, N., Willingmann, P., Adam, G. Arch. Virol. (2006) [Pubmed]
  10. The complete sequence of a Singapore isolate of odontoglossum ringspot virus and comparison with other tobamoviruses. Chng, C.G., Wong, S.M., Mahtani, P.H., Loh, C.S., Goh, C.J., Kao, M.C., Chung, M.C., Watanabe, Y. Gene (1996) [Pubmed]
  11. Assessment of the effectiveness of a nuclear-launched TMV-based replicon as a tool for foreign gene expression in plants in comparison to direct gene expression from a nuclear promoter. Man, M., Epel, B.L. Transgenic Res. (2006) [Pubmed]
  12. Cactus mild mottle virus is a new cactus-infecting tobamovirus. Min, B.E., Chung, B.N., Kim, M.J., Ha, J.H., Lee, B.Y., Ryu, K.H. Arch. Virol. (2006) [Pubmed]
  13. In Planta production of immunogenic poliovirus peptide using tobacco mosaic virus-based vector system. Fujiyama, K., Saejung, W., Yanagihara, I., Nakado, J., Misaki, R., Honda, T., Watanabe, Y., Seki, T. J. Biosci. Bioeng. (2006) [Pubmed]
 
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