Abstract
Cell-to-cell movement of cowpea mosaic virus particles in plants takes place with the help of tubules that penetrate presumably modified plasmodesmata. These tubules, which are built up by the virus-encoded 48-kDa movement protein (MP), are also formed on single protoplast cells. To determine whether the MP contains different functional domains, the effect of mutations in its coding region was studied. Mutations between amino acids 1 and 313 led to complete abolishment of the tubule-forming capacity, while a deletion in the C-terminal region resulted in tubules that could not take up virus particles. From these observations, it is concluded that the MP contains at least two distinct domains, one that is involved in tubule formation and that spans amino acids 1 and 313 and a second that is probably involved in the incorporation of virus particles in the tubule and that is located in the C terminus between amino acids 314 and 331.
Full Text
The Full Text of this article is available as a PDF (635.5 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Deom C. M., Lapidot M., Beachy R. N. Plant virus movement proteins. Cell. 1992 Apr 17;69(2):221–224. doi: 10.1016/0092-8674(92)90403-y. [DOI] [PubMed] [Google Scholar]
- Eggen R., Verver J., Wellink J., De Jong A., Goldbach R., van Kammen A. Improvements of the infectivity of in vitro transcripts from cloned cowpea mosaic virus cDNA: impact of terminal nucleotide sequences. Virology. 1989 Dec;173(2):447–455. doi: 10.1016/0042-6822(89)90557-6. [DOI] [PubMed] [Google Scholar]
- Gafny R., Lapidot M., Berna A., Holt C. A., Deom C. M., Beachy R. N. Effects of terminal deletion mutations on function of the movement protein of tobacco mosaic virus. Virology. 1992 Apr;187(2):499–507. doi: 10.1016/0042-6822(92)90452-u. [DOI] [PubMed] [Google Scholar]
- Kasteel D., Wellink J., Verver J., van Lent J., Goldbach R., van Kammen A. The involvement of cowpea mosaic virus M RNA-encoded proteins in tubule formation. J Gen Virol. 1993 Aug;74(Pt 8):1721–1724. doi: 10.1099/0022-1317-74-8-1721. [DOI] [PubMed] [Google Scholar]
- Osman T. A., Ingles P. J., Miller S. J., Buck K. W. A spontaneous red clover necrotic mosaic virus mutant with a truncated movement protein. J Gen Virol. 1991 Aug;72(Pt 8):1793–1800. doi: 10.1099/0022-1317-72-8-1793. [DOI] [PubMed] [Google Scholar]
- Thomas C. L., Maule A. J. Identification of structural domains within the cauliflower mosaic virus movement protein by scanning deletion mutagenesis and epitope tagging. Plant Cell. 1995 May;7(5):561–572. doi: 10.1105/tpc.7.5.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wellink J., Verver J., van Kammen A. Mutational analysis of AUG codons of cowpea mosaic virus M RNA. Biochimie. 1993;75(8):741–747. doi: 10.1016/0300-9084(93)90105-2. [DOI] [PubMed] [Google Scholar]
- Wellink J., van Lent J. W., Verver J., Sijen T., Goldbach R. W., van Kammen A. The cowpea mosaic virus M RNA-encoded 48-kilodalton protein is responsible for induction of tubular structures in protoplasts. J Virol. 1993 Jun;67(6):3660–3664. doi: 10.1128/jvi.67.6.3660-3664.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van Bokhoven H., Verver J., Wellink J., van Kammen A. Protoplasts transiently expressing the 200K coding sequence of cowpea mosaic virus B-RNA support replication of M-RNA. J Gen Virol. 1993 Oct;74(Pt 10):2233–2241. doi: 10.1099/0022-1317-74-10-2233. [DOI] [PubMed] [Google Scholar]
- van Lent J., Storms M., van der Meer F., Wellink J., Goldbach R. Tubular structures involved in movement of cowpea mosaic virus are also formed in infected cowpea protoplasts. J Gen Virol. 1991 Nov;72(Pt 11):2615–2623. doi: 10.1099/0022-1317-72-11-2615. [DOI] [PubMed] [Google Scholar]
- van der Vossen E. A., Notenboom T., Bol J. F. Characterization of sequences controlling the synthesis of alfalfa mosaic virus subgenomic RNA in vivo. Virology. 1995 Oct 1;212(2):663–672. doi: 10.1006/viro.1995.1524. [DOI] [PubMed] [Google Scholar]
