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ARS Home » Plains Area » Lincoln, Nebraska » Wheat, Sorghum and Forage Research » Research » Publications at this Location » Publication #304242
Title: Multiple roles of Wheat streak mosaic virus coat protein in virus biology

Author
item Tatineni, Satyanarayana - Ts
item MCMECHAN, ANTHONY - University Of Nebraska
item HEIN, GARY - University Of Nebraska

Submitted to: American Phytopathological Society
Publication Type: Abstract Only
Publication Acceptance Date: 3/15/2014
Publication Date: 6/1/2014
Citation: Tatineni, S., Mcmechan, A.J., Hein, G.L. 2014. Multiple roles of Wheat streak mosaic virus coat protein in virus biology. American Phytopathological Society. 94-S.

Interpretive Summary:

Technical Abstract: Wheat streak mosaic virus (WSMV) is an economically important member of the Potyviridae family impacting wheat production in the Great Plains region. The role of WSMV coat protein (CP) in virus biology was examined by introducing a series of point or deletion mutations into the CP cistron, and it was found that WSMV is unusually tolerant of extensive CP deletions. The N-terminal amino acids (aa) 6 to 27 and 85 to 100 are required for efficient virion assembly and cell-to-cell movement, while the C-terminal 65 aa are dispensable for virion assembly but required for cell-to-cell movement. This suggests that the C-terminus of CP functions as a dedicated determinant for cell-to-cell movement. In contrast, aa 36 to 84 are expendable for virion assembly and systemic infection, and deletion of aa 58 to 84 induced more severe symptoms than the wild-type virus, suggesting that CP functions as a suppressor of virulence. Moreover, efficient systemic infection by WSMV mutants with precise exchange of aa between 36 and 84 with nonviral aa could facilitate expression and display of specialty peptides/epitopes embedded into virions. Furthermore, aa 58 to 100 are required for transmission by the wheat curl mites; however, aa 6 to 27, 36 to 57 and the C-terminal 14 aa are dispensable for mite transmission. Our studies revealed that WSMV CP possesses distinct functional domains involved in virion assembly, virus movement, host range, suppression of virulence, and mite transmission.