scholarly journals Cell-to-Cell Movement of the PVX 12K, 8K, or Coat Proteins May Depend on the Host, Leaf Developmental Stage, and the PVX 25K Protein

Virology ◽  
2002 ◽  
Vol 300 (2) ◽  
pp. 269-281 ◽  
Author(s):  
Konduru Krishnamurthy ◽  
Ruchira Mitra ◽  
Mark E. Payton ◽  
Jeanmarie Verchot-Lubicz
2001 ◽  
Vol 82 (1) ◽  
pp. 35-44 ◽  
Author(s):  
Huanting Liu ◽  
Margaret I. Boulton ◽  
Karl J. Oparka ◽  
Jeffrey W. Davies

We have shown previously that the movement protein (MP) and coat protein (CP) of Maize streak virus (MSV) are both required for systemic infection. Towards understanding the roles of these two proteins in virus movement, each was expressed in E. coli and interactions of the MP with viral DNA or CP were investigated using south-western, gel overlay and immunoprecipitation assays. Unlike the CP, the MP did not bind to viral DNA but it interacted with the CP in vitro and an MP–CP complex was detected in extracts from MSV-infected maize, indicating the potential for an interaction in vivo. Microinjection showed that the MP could prevent the nuclear transport of an MSV CP–DNA complex in maize and tobacco cells. These results are consistent with a model in which the MP diverts a CP–DNA complex from the nucleus (where viral DNA replication takes place) to the cell periphery, and in co-operation with the CP, mediates the cell-to-cell movement of the viral DNA. In this respect, the MSV MP and CP have functional analogy with the BC1 and BV1 proteins, respectively, of the Begomovirus genus of the Geminiviridae.


2012 ◽  
Vol 93 (8) ◽  
pp. 1814-1824 ◽  
Author(s):  
Anna Maria Vaira ◽  
Hyoun-Sub Lim ◽  
Gary R. Bauchan ◽  
Robert A. Owens ◽  
Angela Natilla ◽  
...  

The genome of Lolium latent virus (LoLV; genus Lolavirus, family Alphaflexiviridae) is encapsidated by two carboxy-coterminal coat protein (CP) variants (about 28 and 33 kDa), in equimolar proportions. The CP ORF contains two 5′-proximal AUGs encoding Met 1 and Met 49, respectively promoting translation of the 33 and 28 kDa CP variants. The 33 kDa CP N-terminal domain includes a 42 aa sequence encoding a putative chloroplast transit peptide, leading to protein cleavage and alternative derivation of the approximately 28 kDa CP. Mutational analysis of the two in-frame start codons and of the putative proteolytic-cleavage site showed that the N-terminal sequence is crucial for efficient cell-to-cell movement, functional systemic movement, homologous CP interactions and particle formation, but is not required for virus replication. Blocking production of the 28 kDa CP by internal initiation shows no major outcome, whereas additional mutation to prevent proteolytic cleavage at the chloroplast membrane has a dramatic effect on virus infection.


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