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Gene Review:

TEVgp1 - polyprotein

Tobacco etch virus

Carrington, J.C. et al., Kim, D.H. et al., Fanigliulo, A. et al., Fuji, S. et al., Dougherty, W.G. et al., et al.

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Disease relevance of TEVgp1

The polyprotein encoded by plant potyviruses is proteolytically processed to at least eight mature products by viral-encoded proteinases [1].
By using cell-free systems to manipulate and express cloned cDNA sequences, a 25-amino acid segment containing a putative proteolytic cleavage site of the TEV polyprotein has been introduced into the TEV capsid protein sequence [2].
Its polyprotein differs substantially from Yam mosaic virus (YMV) (50% amino acid sequence identity) and fourteen other potyvirus species examined (44-59% identity) [3].

High impact information on TEVgp1

All known or predicted cleavage sites in the TEV polyprotein are flanked by the conserved sequence motif Glu-Xaa-Xaa-Tyr-Xaa-Gln-Ser or Gly, with the scissile bond located between the Gln-Ser or Gly dipeptide [2].
The tobacco etch potyvirus (TEV) genome encodes a polyprotein that is processed by three virus-encoded proteinases [4].
The nuclear inclusion protein a (NIa) of turnip mosaic potyvirus is a protease processing the viral polyprotein into functional proteins [5].
The point mutation of Trp-212 to Ser, Gly-213 to Ser, or Ile-217 to Asp drastically abolished the catalytic activity, demonstrating that Trp-212, Gly-213, and Ile-217 are important for the processing of 6K1-Cl polyprotein [5].
Mutants (one in P1 and one in HCpro) presumably affected in polyprotein processing also did not replicate in plants or protoplasts [6].

Biological context of TEVgp1

It contains a single open reading frame (ORF) encoding a polyprotein of 3130 amino acids (aa) with a calculated Mr of 356,793 [3].
Alignment of the amino acid sequence of the BYMV-S polyprotein with those of other potyviruses identified nine putative proteolytic cleavage sites [7].

Anatomical context of TEVgp1

Post-translational processing of the tobacco etch virus 49-kDa small nuclear inclusion polyprotein: identification of an internal cleavage site and delimitation of VPg and proteinase domains [8].

Analytical, diagnostic and therapeutic context of TEVgp1

It consists of 9699 nucleotides (nt) excluding the 3' terminal poly(A) tail and contains an open reading frame of 9186 nt, encoding the putative polyprotein of 3061 amino acids.In ELISA, the isolate reacted with a monoclonal antibody specific for PVY(C) but not with antibodies against PVY(N) or PVY(O) [9].

References

The 35-kDa protein from the N-terminus of the potyviral polyprotein functions as a third virus-encoded proteinase. Verchot, J., Koonin, E.V., Carrington, J.C. Virology (1991) [Pubmed]
A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing. Carrington, J.C., Dougherty, W.G. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
Complete nucleotide sequence of the genomic RNA of a Japanese yam mosaic virus, a new potyvirus in Japan. Fuji, S., Nakamae, H. Arch. Virol. (1999) [Pubmed]
The tobacco etch potyvirus 6-kilodalton protein is membrane associated and involved in viral replication. Restrepo-Hartwig, M.A., Carrington, J.C. J. Virol. (1994) [Pubmed]
Effects of internal cleavages and mutations in the C-terminal region of NIa protease of turnip mosaic potyvirus on the catalytic activity. Kim, D.H., Hwang, D.C., Kang, B.H., Lew, J., Han, J., Song, B.D., Choi, K.Y. Virology (1996) [Pubmed]
Mutational analysis of the tobacco vein mottling virus genome. Klein, P.G., Klein, R.R., Rodríguez-Cerezo, E., Hunt, A.G., Shaw, J.G. Virology (1994) [Pubmed]
The complete nucleotide sequence of bean yellow mosaic potyvirus RNA. Guyatt, K.J., Proll, D.F., Menssen, A., Davidson, A.D. Arch. Virol. (1996) [Pubmed]
Post-translational processing of the tobacco etch virus 49-kDa small nuclear inclusion polyprotein: identification of an internal cleavage site and delimitation of VPg and proteinase domains. Dougherty, W.G., Parks, T.D. Virology (1991) [Pubmed]
Characterisation of Potato virus Y nnp strain inducing veinal necrosis in pepper: a naturally occurring recombinant strain of PVY. Fanigliulo, A., Comes, S., Pacella, R., Harrach, B., Martin, D.P., Crescenzi, A. Arch. Virol. (2005) [Pubmed]

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