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Title: INTERACTION BETWEEN A MAIZE SPHINGOSINE KINASE-LIKE PROTEIN AND THE MAIZE CHLOROTIC DWARF VIRUS COAT PROTEIN 1

Author
item Willie, Kristen
item Redinbaugh, Margaret
item MATTHIES, I - OSU
item SAUER, M - OSU
item SANKAR, U - OSU
item SIMCOX, K - OSU
item BOUCHARD, R - OSU
item PRATT, R - OSU

Submitted to: Phytopathology
Publication Type: Abstract Only
Publication Acceptance Date: 3/15/2005
Publication Date: 8/30/2005
Citation: Willie, K.J., Redinbaugh, M.G., Matthies, I., Sauer, M., Sankar, U., Simcox, K., Bouchard, R., Pratt, R.C. 2005. Interaction between a maize sphingosine kinase-like protein and the maize chlorotic dwarf virus coat protein 1 [abstract]. Phytopathology. 95:S87.

Interpretive Summary:

Technical Abstract: Specific interactions between virus and host proteins are required for both virus susceptibility (i.e., replication and movement) and resistance in plants. To begin to characterize these interactions at the molecular level, the coat protein 1 (CP1) of Maize chlorotic dwarf virus (MCDV) was used as bait in a yeast two-hybrid system to identify virus-binding proteins from susceptible maize. The prey clone 12-15 protein interacted very strongly and specifically with the MCDV CP1, and was selected for further characterization. Transcripts encoded by 12-15 were expressed at low levels in both susceptible and resistant maize. While MCDV is a phloem-limited virus, no tissue-specific distribution of the 12-15 transcript was found. The 12-15 cDNA sequence was identical to nt 389 to 1226 of a contig of maize EST sequences (AY104898) and the open reading frame (ORF) encoded an apparent diacylglycerol kinase catalytic domain. ORF proteins encoded by both 12-15 and AY104898 were expressed in E. coli. The expressed proteins did not bind to MCDV virions in virus overlay assays. This result was similar to that found for the Arabidopsis TIP protein which interacted with free Turnip crinkle virus (TCV) coat protein but not with the assembled TCV virion. Current work is focused on generation of antibodies to the expressed proteins and identification of specific interactions between MCDV CP1 protein monomers.