The Potato virus X TGBp3 protein associates with the ER network for virus cell-to-cell movement

Potato virus X (PVX) TGBp3 is required for virus cell-to-cell movement. Cell-to-cell movement of TGBp3 was studied using biolistic bombardment of plasmids expressing GFP:TGBp3. TGBp3 moves between cells in Nicotiana benthamiana, but requires TGBp1 to move in N. tabacum leaves. In tobacco leaves GFP:...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2003-04, Vol.309 (1), p.135-151
Main Authors: Krishnamurthy, Konduru, Heppler, Marty, Mitra, Ruchira, Blancaflor, Elison, Payton, Mark, Nelson, Richard S, Verchot-Lubicz, Jeanmarie
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biolistics
Cell-to-cell movement
Endoplasmic Reticulum - virology
Green Fluorescent Proteins
Life Sciences (General)
Luminescent Proteins - genetics
Molecular Sequence Data
Nicotiana - virology
Plasmodesmata transport
Potato virus X
Potexvirus
Potexvirus - physiology
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Solanum tuberosum - virology
Triple gene block
Viral Nonstructural Proteins - chemistry
Viral Nonstructural Proteins - genetics
Viral Nonstructural Proteins - metabolism
Virus movement
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Summary:Potato virus X (PVX) TGBp3 is required for virus cell-to-cell movement. Cell-to-cell movement of TGBp3 was studied using biolistic bombardment of plasmids expressing GFP:TGBp3. TGBp3 moves between cells in Nicotiana benthamiana, but requires TGBp1 to move in N. tabacum leaves. In tobacco leaves GFP:TGBp3 accumulated in a pattern resembling the endoplasmic reticulum (ER). To determine if the ER network is important for GFP:TGBp3 and for PVX cell-to-cell movement, a single mutation inhibiting membrane binding of TGBp3 was introduced into GFP:TGBp3 and into PVX. This mutation disrupted movement of GFP:TGBp3 and PVX. Brefeldin A, which disrupts the ER network, also inhibited GFP:TGBp3 movement in both Nicotiana species. Two deletion mutations, that do not affect membrane binding, hindered GFP:TGBp3 and PVX cell-to-cell movement. Plasmids expressing GFP:TGBp2 and GFP:TGBp3 were bombarded to several other PVX hosts and neither protein moved between adjacent cells. In most hosts, TGBp2 or TGBp3 cannot move cell-to-cell.
ISSN:0042-6822
1096-0341
DOI:10.1016/S0042-6822(02)00102-2