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ARS Home » Northeast Area » Frederick, Maryland » Foreign Disease-Weed Science Research » Research » Publications at this Location » Publication #241323
Title: Proteomic analysis of germinating urediniospores of Phakopsora pachyrhizi, causal agent of Asian Soybean Rust

Author
item Luster, Douglas - Doug
item McMahon, Michael - Mike
item Carter, Melissa
item Fortis, Laurie
item Nunez, Alberto

Submitted to: Proteomics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/6/2010
Publication Date: 10/1/2010
Citation: Luster, D.G., Mcmahon, M.B., Carter, M.L., Fortis, L.L., Nunez, A. 2010. Proteomic analysis of germinating urediniospores of Phakopsora pachyrhizi, causal agent of Asian Soybean Rust. Proteomics. 7:3549-3557.

Interpretive Summary: Asian Soybean Rust (ASR) is a serious pathogen of soybean. It is unique in that ASR has a wide host range and infects plants by direct penetration through leaf cells. In order to understand the early events in the infection process, it is important to identify and characterize proteins in the fungus that causes ASR. Because ASR only grows on the host plant, and cannot be grown in culture, germinating spores represent the only life stage applicable to such studies. We have applied a proteomic approach to identify over 100 ASR proteins, with functions critical to growth and development of the fungal pathogen. This information is valuable for researchers to design experiments for identifying the host response to ASR.

Technical Abstract: Phakopsora pachyrhizi is an obligate pathogen that causes Asian Soybean Rust (ASR). ASR has an unusually broad host range and infects by direct penetration through the leaf cuticle. In order to understand the early events in the infection process, it is important to identify and characterize proteins in P. pachyrhizi. Germination of the urediniospore is the first stage in the infection process and represents the only critical life stage applicable to studies with this obligate pathogen. We have applied a 2-DE and mass spectrometry approach to identify 117 proteins from a public database and a custom database of EST sequences. Proteins with roles in primary metabolism, energy transduction, stress, cellular regulation and signaling were identified in this study.