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Expression of cowpea mosaic virus coat protein precursor in transgenic tobacco plants

D. L. Nida^1,

¹ Department of Plant Pathology, University of Kentucky, Lexington, Kentucky 40546, U.S.A.
and² Department of Virus Research, John Innes Institute, John Innes Centre for Plant Science Research, Norwich NR4 7UH, U.K.

Tobacco, Nicotiana tabacum L., supports cowpea mosaic virus (CPMV) replication and cell-to-cell movement, and thus may serve as a model system to study coat protein-mediated protection against CPMV. A chimeric gene consisting of the cauliflower mosaic virus 35S promoter, CPMV 60K coat proteins-precursor (CP-P) coding region, and the nopaline synthase polyadenylation signal was transferred to tobacco cv. Burley 21 via the Agrobacterium tumefaciens binary vector system. Gene integration and expression in the transgenic tobacco plants were confirmed by Southern and RNA dot blot analyses. Accumulation of CPMV 60K CP-P in transgenic plants, up to 2 µg/g of wet weight tissue, was detected by ELISA and Western blots. The results of Western blots and immunosorbent electron microscopy further indicated that CPMV CP-P neither undergoes auto-proteolysis to generate the mature viral coat proteins nor assembles into virus-like capsids, suggesting that processing of the CP-P may be required for virus assembly. Because CPMV neither induces symptoms in tobacco nor moves systemically, evaluation of the reactions of the transgenic plants to virus inoculation was based on virus accumulation in the inoculated leaves. Results from such infectivity experiments did not differentiate between CP-P expressers and vector-transformed plants. The transgenic tobacco plants expressing CP-P should provide valuable material for investigating comovirus polyprotein processing and capsid assembly in vivo.

Present address: Monsanto Agricultural Company, New Products Division, 700 Chesterfield Village Parkway, Chesterfield, Missouri 63198, U.S.A.

Received 2 July 1991; accepted 17 September 1991.

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