Potyvirus aphid transmission requires helper component and homologous coat protein for maximal efficiency

1998 ◽  
Vol 143 (11) ◽  
pp. 2159-2172 ◽  
Author(s):  
S. Flasinski ◽  
B. G. Cassidy
Keyword(s):  
Coat Protein ◽  
Aphid Transmission ◽  
Helper Component ◽  
Maximal Efficiency

scholarly journals A Specific Interaction between Coat Protein and Helper Component Correlates with Aphid Transmission of a Potyvirus

Virology ◽  
1997 ◽  
Vol 231 (1) ◽  
pp. 141-147 ◽  
Author(s):  
Stéphane Blanc ◽  
Juan-José López-Moya ◽  
Renyuan Wang ◽  
Sandra García-Lampasona ◽  
David W. Thornbury ◽  
...  
Keyword(s):  
Coat Protein ◽  
Specific Interaction ◽  
Aphid Transmission ◽  
Helper Component

Aphid transmission of a potyvirus depends on suitability of the helper component and the N terminus of the coat protein

2004 ◽  
Vol 150 (2) ◽  
pp. 287-298 ◽  
Author(s):  
A. Dombrovsky ◽  
H. Huet ◽  
N. Chejanovsky ◽  
B. Raccah
Keyword(s):  
Coat Protein ◽  
Aphid Transmission ◽  
Helper Component ◽  
N Terminus

scholarly journals Biochemical Characterization of the Helper Component of Cauliflower Mosaic Virus

2001 ◽  
Vol 75 (18) ◽  
pp. 8538-8546 ◽  
Author(s):  
Eugenie Hebrard ◽  
Martin Drucker ◽  
Denis Leclerc ◽  
Thomas Hohn ◽  
Marilyne Uzest ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Biochemical Characterization ◽  
Active Form ◽  
Recombinant Baculovirus ◽  
Aphid Transmission ◽  
Cauliflower Mosaic Virus ◽  
Biologically Active ◽  
Size Exclusion ◽  
Viral Gene ◽  
Helper Component

ABSTRACT The helper component of Cauliflower mosaic virus is encoded by viral gene II. This protein (P2) is dispensable for virus replication but required for aphid transmission. The purification of P2 has never been reported, and hence its biochemical properties are largely unknown. We produced the P2 protein via a recombinant baculovirus with a His tag fused at the N terminus. The fusion protein was purified by affinity chromatography in a soluble and biologically active form. Matrix-assisted laser desorption time-of-flight mass spectrometry demonstrated that P2 is not posttranslationally modified. UV circular dichroism revealed the secondary structure of P2 to be 23% α-helical. Most α-helices are suggested to be located in the C-terminal domain. Using size exclusion chromatography and aphid transmission testing, we established that the active form of P2 assembles as a huge soluble oligomer containing 200 to 300 subunits. We further showed that P2 can also polymerize as long paracrystalline filaments. We mapped P2 domains involved in P2 self-interaction, presumably through coiled-coil structures, one of which is proposed to form a parallel trimer. These regions have previously been reported to also interact with viral P3, another protein involved in aphid transmission. Possible interference between the two types of interaction is discussed with regard to the biological activity of P2.

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