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Journal of Virology, February 2004, p. 1591-1594, Vol. 78, No. 3
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.3.1591-1594.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
J. Pouwels,2,
J. W. M. van Lent,1* T. Bisseling,2 R. W. Goldbach,1 and J. Wellink2
Laboratory of Virology, Department of Plant Sciences, Wageningen University, 6709 PD Wageningen,1 Laboratory of Molecular Biology, Department of Plant Sciences, Wageningen University, 6703 HA Wageningen, The Netherlands2
Received 21 July 2003/ Accepted 9 October 2003
The movement protein (MP) of Cowpea mosaic virus forms tubules in plasmodesmata to enable the transport of mature virions. Here it is shown that the MP is capable of specifically binding riboguanosine triphosphate and that mutational analysis suggests that GTP binding plays a role in the targeted transport of the MP. Furthermore, the MP is capable of binding both single-stranded RNA and single-stranded DNA in a non-sequence-specific manner, and the GTP- and RNA-binding sites do not overlap.
C.M.C. and J.P. contributed equally to this work.
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