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	<id>https://gydb.org/index.php?action=history&amp;feed=atom&amp;title=Virus_associated_protein</id>
	<title>Virus associated protein - Revision history</title>
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	<updated>2026-06-09T17:30:10Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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		<id>https://gydb.org/index.php?title=Virus_associated_protein&amp;diff=676&amp;oldid=prev</id>
		<title>imported&gt;Gydbwiki at 13:03, 31 May 2010</title>
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		<updated>2010-05-31T13:03:04Z</updated>

		<summary type="html">&lt;p&gt;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;[[Category:Retroelements]]&lt;br /&gt;
The &amp;quot;virion-associated protein&amp;quot; (VAP) encoded by many but not all caulimoviruses is essential for plant infection ([[Literature:100697|Stavolone ''et al.'' 2001]]), and can participate in the virus movement ([[Literature:100594|Stavolone ''et al.'' 2005]]). VAP contains coiled-coil motifs  ([[Literature:100697|Stavolone ''et al.'' 2001]]; [[Literature:100738|Hoh ''et al.'' 2010]]) which are bundles of two or more amphipathic helices, characterized by an heptad repeat of hydrophobic and hydrophilic amino acids. &lt;br /&gt;
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Studies based on four ''Caulimovirus'' species suggest that VAPs assemble as a tetramer ([[Literature:100697|Stavolone ''et al.'' 2001]]) and that the C-terminal region of the &amp;quot;Aphid transmission factor&amp;quot; (ATF) apparently interacts with VAP through the coiled-coil domains ([[Literature:100700|Leh ''et al.'' 1999]]). VAP has been associated with the virion ([[Literature:100700|Leh ''et al.'' 1999]]; [[Literature:100799|Schmidt ''et al.'' 1994]]) but it is not essential for genome packaging ([[Literature:100798|Kobayashi ''et al.'' 2002]]).  Stavolone ''et al.'' ([[Literature:100594|2005]]) suggest that VAP is not a scaffolding protein but a late addition during the assembly process that plays a role in the virus spread process. In fact, VAP is indispensable for spreading virus infection within the host plant ([[Literature:100594|Stavolone ''et al.'' 2005]]) and may act as the arm of the virus particle anchored into the capsid shell ([[Literature:100748|Leclerc ''et al.'' 2001]]). VAP also interacts with the C-terminal coiled coil domain of &amp;quot;Movement protein&amp;quot; (MOV), which oligomerizes as a parallel trimer that interacts with the VAP N-terminal coiled coil ([[Literature:100594|Stavolone ''et al.'' 2005]]). This MOV-VAP interaction suggests that VAP is involved in virus movement ([[Literature:100594|Stavolone ''et al.'' 2005]]). The figure below shows a three-dimensional structure of the virion-associated protein p3 from the ''Caulimovirus'' CaMV, according to the work of [[Literature:100738|Hoh ''et al.'' 2010]].&lt;br /&gt;
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&amp;lt;center&amp;gt;[[File:VAP_grande.png]]&amp;lt;/center&amp;gt;&lt;br /&gt;
&amp;lt;center&amp;gt;'''''3D image of VAP-CaMV (PDB id:3f6n) available on [http://www.ebi.ac.uk/pdbsum/3f6n PDBSum] database'''''&amp;lt;/center&amp;gt;&lt;/div&gt;</summary>
		<author><name>imported&gt;Gydbwiki</name></author>
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