Compatibility of the movement protein and the coat protein of cucumoviruses is required for cell-to-cell movement.
For the cell-to-cell movement of cucumoviruses both the movement protein (MP) and the coat protein (CP) are required. These are not reversibly exchangeable between Cucumber mosaic virus (CMV) and Tomato aspermy virus (TAV). The MP of CMV is able to function with the TAV CP (chimera RT), but TAV MP is unable to promote the cell-to-cell movement in the presence of CMV CP (chimera TR). To gain further insight into the non-infectious nature of the TR recombinant, RNA 3 chimeras were constructed with recombinant MPs and CPs. The chimeric MP and one of the CP recombinants were infectious. The other recombinant CP enabled virus movement only after the introduction of two point mutations (Glu-->Lys and Lys-->Arg at aa 62 and 65, respectively). The mutations served to correct the CP surface electrostatic potential that was altered by the recombination. The infectivity of the TR virus on different test plants was restored by replacing the sequence encoding the C-terminal 29 aa of the MP with the corresponding sequence of the CMV MP gene or by exchanging the sequence encoding the C-terminal 15 aa of the CP with the same region of TAV. The analysis of the recombinant clones suggests a requirement for compatibility between the C-terminal 29 aa of the MP and the C-terminal two-thirds of the CP for cell-to-cell movement of cucumoviruses.
Salánki
Katalin
K
Agricultural Biotechnology Center, Szent-Györgyi Albert u. 4, H-2100 Gödöllő, Hungary.
Gellért
Ákos
Á
Department of Theoretical Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.|Agricultural Biotechnology Center, Szent-Györgyi Albert u. 4, H-2100 Gödöllő, Hungary.
Huppert
Emese
E
Agricultural Biotechnology Center, Szent-Györgyi Albert u. 4, H-2100 Gödöllő, Hungary.
Náray-Szabó
Gábor
G
Protein Modelling Group, Hungarian Academy of Sciences - Eötvös Lóránd University, Pázmány Péter Sétány 1/A, H-1117 Budapest, Hungary.
Balázs
Ervin
E
Agricultural Biotechnology Center, Szent-Györgyi Albert u. 4, H-2100 Gödöllő, Hungary.
D019943:Amino Acid Substitution; D001693:Biological Transport, Active; D036022:Capsid Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D027462:Chenopodium / Q000821:virology; D027465:Chenopodium quinoa / Q000821:virology; D003198:Computer Simulation; D017799:Cucumovirus / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D053830:Plant Viral Movement Proteins; D010944:Plants / Q000821:virology*; D030821:Plants, Genetically Modified; D011487:Protein Conformation; D011523:Protoplasts / Q000821:virology; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D055672:Static Electricity; D014026:Nicotiana / Q000821:virology; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D014774:Virulence
D036022:Capsid Proteins; D053830:Plant Viral Movement Proteins; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins