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Journal of Virology, November 1998, p. 9247-9256, Vol. 72, No. 11
Department of Microbiology, University of
Illinois at Urbana-Champaign, Urbana, Illinois 61801
Received 16 December 1996/Accepted 18 July 1998
The movement of bipartite geminiviruses such as squash leaf curl
virus (SqLCV) requires the cooperative interaction of two essential
virus-encoded movement proteins, BR1 and BL1. While the viral coat
protein AR1 is not essential for systemic infection, genetic studies
demonstrate that its presence masks the defective phenotype of certain
BR1 missense mutants, thus suggesting that coat protein does interact
with the viral movement pathway. To further examine the mechanism of
this interaction, we have constructed alanine-scanning mutants of AR1
and studied them for the ability to mask the infectivity defects of
appropriate BR1 mutants, for the ability to target to the nucleus and
to bind viral single-stranded DNA (ssDNA) and multimerize, and for
effects on the accumulation of replicated viral ssDNA. We identified a
specific region of AR1 required for masking of appropriate BR1 mutants
and showed that this same region of AR1 was also important for ssDNA
binding and the accumulation of viral replicated ssDNA. This region of AR1 also overlapped that involved in multimerization of the coat protein. We also found that the accumulation in protoplasts of single-stranded forms of a recombinant plasmid that included the SqLCV
replication origin but was too large to be encapsidated was dependent
on the presence of AR1 but did not appear to require encapsidation.
These findings extend our model for SqLCV movement, demonstrating that
coat protein affects viral movement through its ability to induce the
accumulation of replicated viral ssDNA genomes. They further suggested
that encapsidation was not required for the AR1-dependent accumulation
of viral ssDNA.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Bipartite Geminivirus Coat Protein Aids BR1
Function in Viral Movement by Affecting the Accumulation of Viral
Single-Stranded DNA

and
*
Corresponding author. Present address: Department of
Plant Pathology, Cornell University, Ithaca, NY 14853. Phone: (607)
255-7830. Fax: (607) 255-4471. E-mail: sgl5{at}cornell.edu.
Present address: Department of Genetics and Development, College of
Physicians and Surgeons, Columbia University, New York, NY 10032.
Present address: Laboratory of Viral Diseases, National Institute
of Allergy and Infectious Diseases, National Institutes of Health,
Bethesda, MD 20892.
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