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Journal of Virology, August 2001, p. 7739-7743, Vol. 75, No. 16
Friedrich Miescher Institute, CH-4002 Basel,
Switzerland
Received 22 March 2001/Accepted 7 May 2001
All plant pararetroviruses belong to the Caulimoviridae
family. This family contains six genera of viruses with different biological, serological, and molecular characteristics. Although some
important mechanisms of viral replication and host infection are
understood, much remains to be discovered about the many functions of
the viral proteins. The focus of this study, the virion-associated protein (VAP), is conserved among all members of the group and contains
a coiled-coil structure that has been shown to assemble as a tetramer
in the case of cauliflower mosaic virus. We have used the yeast
two-hybrid system to characterize self-association of the VAPs of four
distinct plant pararetroviruses, each belonging to a different genus of
Caulimoviridae. Chemical cross-linking confirmed that VAPs
assemble into tetramers. Tetramerization is thus a common property of
these proteins in plant pararetroviruses. The possible implications of
this conserved feature for VAP function are discussed.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.16.7739-7743.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Tetramerization Is a Conserved Feature of the
Virion-Associated Protein in Plant Pararetroviruses
and
*
Corresponding author. Mailing address: Friedrich
Miescher Institute, P.O. Box 2543, CH-4002 Basel, Switzerland. Phone:
41 61 6977266. Fax: 41 61 6973976. E-mail: hohn{at}fmi.ch.
Present address: CHUQ, Centre de Recherche en Infectiologie,
Quèbec, Quèbec G1V4G2, Canada.
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