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Gene Review

CP  -  coat protein

Tomato mottle Taino virus

 
 
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Disease relevance of CP

  • Tomato leaf curl geminivirus (ToLCV) requires coat protein (CP) for the accumulation of ssDNA in protoplasts and in plants but not for systemic infection and symptom development in plants [1].
  • To determine whether the gene 5 protein (g5p), a ssDNA binding protein from Escherichia coli phage M13, could restore the accumulation of ssDNA, ToLCV that lacked the CP gene was modified to express g5p or g5p fused to the N-terminal 66 amino acids of CP (CP66:6G:g5) [1].
  • We also show that a CP mutant of the related bean golden mosaic virus (BGMV), which can infect beans systemically, is confined to the inoculated leaves of N. benthamiana [2].
  • We have shown previously that the movement protein (MP) and coat protein (CP) of Maize streak virus (MSV) are both required for systemic infection [3].
 

High impact information on CP

  • In the absence of CP, infected protoplasts accumulate reduced levels of ssDNA and increased amounts of double-stranded DNA (dsDNA), compared to accumulation in the presence of wild-type virus [1].
  • The high levels of dsDNA accumulation during infections with the modified viruses suggested a direct role for CP in viral DNA replication [1].
  • These results indicate that domains of the CP facilitate several aspects of geminivirus movement, including nuclear import and export and transport of the viral genome to the cell periphery [4].
  • The coat protein (CP) of geminiviruses is involved in a number of processes during the life cycle of the virus [4].
  • We therefore suggest that, although GroEL-CP interaction in the hemolymph is a necessary condition for circulative transmission, the nontransmissibility of AbMV-Is is not the result of lack of binding to GroEL in the B. tabaci hemolymph, but most likely results from an inability to cross the gut/hemolymph barrier [5].
 

Biological context of CP

  • Distinct viral sequence elements mediate expression and derepression in phloem and activation in mesophyll, suggesting that TrAP interacts with different components of the cellular transcription machinery to accomplish CP gene expression in different cell types, and underscoring the intricacy and complexity of virus-host interactions [6].
  • The complete nucleotide sequences of DNA-A of UgV (2799 nt) and of a Tanzanian isolate of EACMV (2801 nt) were determined and are extremely similar, except for the coat protein (CP) gene [7].
  • Using transgenes consisting of complete and truncated versions of the CP promoter fused to the GUS reporter gene, we show in the studies presented here that TrAP is required for CP gene expression in both mesophyll and phloem tissues [6].
  • Virus relationships were predicted by distance and parsimony analyses using the A component (bipartite viruses) or full genome (monopartite viruses), CP gene, core CP, or the 200 5'-nucleotides (nt) of the CP [8].
 

Anatomical context of CP

  • To determine whether AbMV-Is particles were rapidly degraded in the hemolymph as a result of their inability to interact with GroEL, we have isolated a GroEL gene from B. tabaci and used a yeast two-hybrid assay to compare binding of the CP of TYLCV-Is and AbMV-Is to the insect GroEL [5].
 

Regulatory relationships of CP

  • Surprisingly, TrAP appears to induce CP expression by different mechanisms in different cell types: it may activate the CP promoter in mesophyll cells, and acts to derepress the promoter in phloem tissue [6].
 

Analytical, diagnostic and therapeutic context of CP

References

  1. A phage single-stranded DNA (ssDNA) binding protein complements ssDNA accumulation of a geminivirus and interferes with viral movement. Padidam, M., Beachy, R.N., Fauquet, C.M. J. Virol. (1999) [Pubmed]
  2. Host and viral factors determine the dispensability of coat protein for bipartite geminivirus systemic movement. Pooma, W., Gillette, W.K., Jeffrey, J.L., Petty, I.T. Virology (1996) [Pubmed]
  3. Interaction of the movement and coat proteins of Maize streak virus: implications for the transport of viral DNA. Liu, H., Boulton, M.I., Oparka, K.J., Davies, J.W. J. Gen. Virol. (2001) [Pubmed]
  4. Subcellular targeting of the coat protein of African cassava mosaic geminivirus. Unseld, S., Höhnle, M., Ringel, M., Frischmuth, T. Virology (2001) [Pubmed]
  5. The GroEL protein of the whitefly Bemisia tabaci interacts with the coat protein of transmissible and nontransmissible begomoviruses in the yeast two-hybrid system. Morin, S., Ghanim, M., Sobol, I., Czosnek, H. Virology (2000) [Pubmed]
  6. Regulation of a geminivirus coat protein promoter by AL2 protein (TrAP): evidence for activation and derepression mechanisms. Sunter, G., Bisaro, D.M. Virology (1997) [Pubmed]
  7. Evidence that DNA-A of a geminivirus associated with severe cassava mosaic disease in Uganda has arisen by interspecific recombination. Zhou, X., Liu, Y., Calvert, L., Munoz, C., Otim-Nape, G.W., Robinson, D.J., Harrison, B.D. J. Gen. Virol. (1997) [Pubmed]
  8. The core region of the coat protein gene is highly useful for establishing the provisional identification and classification of begomoviruses. Brown, J.K., Idris, A.M., Torres-Jerez, I., Banks, G.K., Wyatt, S.D. Arch. Virol. (2001) [Pubmed]
  9. Interaction of DNA with the movement proteins of geminiviruses revisited. Hehnle, S., Wege, C., Jeske, H. J. Virol. (2004) [Pubmed]
  10. Diversity and distribution of begomoviruses infecting tomato in India. Reddy, R.V., Colvin, J., Muniyappa, V., Seal, S. Arch. Virol. (2005) [Pubmed]
 
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