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ARS Home » Southeast Area » Athens, Georgia » U.S. National Poultry Research Center » Toxicology & Mycotoxin Research » Research » Publications at this Location » Publication #294066
Title: The virally encoded killer proteins from Ustilago maydis

Author
item ALLEN, ARON - Danforth Plant Science Center
item ISLAMOVIC, EMIR - University Of Georgia
item KAUR, JAGDEEP - Danforth Plant Science Center
item Gold, Scott
item SHAH, DILIP - Danforth Plant Science Center
item SMITH, THOMAS - Danforth Plant Science Center

Submitted to: Fungal Biology Reviews
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/9/2012
Publication Date: 1/15/2013
Publication URL: http://handle.nal.usda.gov/10113/56427
Citation: Allen, A., Islamovic, E., Kaur, J., Gold, S.E., Shah, D., Smith, T.J. 2013. The virally encoded killer proteins from Ustilago maydis. Fungal Biology Reviews. 26(4):166-173. dx.doi.org/10.1016/j.fbr.2012.10.001

Interpretive Summary: The structure and functional analysis of the Ustilago maydis virally encoded killer toxins KP4 and KP6 are described. Their use as antifungal agents against U. maydis and other fungi in transgenic plants is discussed.

Technical Abstract: Several strains of Ustilago maydis, a causal agent of corn smut disease, exhibit a 'killer' phenotype that is due to persistent infection by double-stranded RNA Totiviruses. These viruses produce potent killer proteins that are secreted by the host. This is a rare example of virus/host symbiosis in that these viruses are dependent upon host survival and, to that end, produce antifungal proteins that kill competing, uninfected strains of U. maydis. Two of the best-studied examples of this killer phenomenon are U. maydis strains P4 and P6 that secrete killer proteins KP4 and KP6, respectively. The mature form of KP4 is comprised of 105 residues while KP6 consists of two subunits, a and b chains, 76 and 82 residues in length, respectively. KP6 is not homologous to any known protein, and only recently has KP4 been shown to have possible homologs in pathogenic fungi. While very little is known as to the mode of action of KP6, we have shown that KP4 blocks L-type Ca2þ channels in fungi and animal cells in a reversible and cytostatic manner. In contrast, preliminary results suggest that KP6 acts via a completely different mechanism and is a potent cytolytic antifungal protein. When KP4 is expressed in maize, the resulting transgenic lines are nearly immune to U. maydis infection. Therefore, a greater understanding of the modes of action of these potent antifungal proteins could lead to development of broadspectrum antifungal agents.