Identification of Stringent Response-Related and Potential Serological Proteins Released from Bacillus anthracis Overexpressing the RelA/SpoT Homolog,Rsh
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Authors: | Se Kye Kim Moon Kyoo Park Sang Hoon Kim Kwang Gun Oh Kyoung Hwa Jung Chong-Hae Hong Jang W Yoon Young Gyu Chai |
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Institution: | 1. Department of Molecular and Life Sciences, Hanyang University, 1271, Ansan, 426-791, Gyeonggi-do, Republic of Korea 2. Department of Bioprocess Technology, BioPolytechnic College, Nonsan, 320-905, Republic of Korea 3. College of Veterinary Medicine, Kangwon National University, Chuncheon, 200-701, Republic of Korea 4. Department of Nanobiotechnology, Hanyang University, Seoul, 133-791, Republic of Korea
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Abstract: | RelA and SpoT synthesize ppGpp, a key effector molecule that facilitates the adaptation of bacteria to nutrient starvation and other stresses, known as the stringent response. To investigate the role of Rsh Bant , a putative RelA/SpoT homolog (encoded by BAS4302) in Bacillus anthracis, we examined the alteration of the secretome profiles after the overexpression of a functional His-Rsh Bant protein in the B. anthracis strain Sterne at the stationary growth phase. In the ppGpp-deficient E. coli mutant strain CF1693, overexpression of Rsh Bant restored a ppGpp-dependent growth defect on minimal glucose media. The secretome profiles obtained using a two-dimensional electrophoresis (2-DE) analysis were altered by overexpression of Rsh Bant in B. anthracis. Among the 66 protein spots differentially expressed >1.5-fold, the 29 proteins were abundant for further identification using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Functional categorization of those proteins implicated their involvement in various biological activities. Taken together, our results imply that overexpression of a functional His-Rsh Bant can lead to the increased levels of intracellular ppGpp in B. anthracis, resulting in the significant changes in its secretome profiling. The stringent response-controlled proteins identified are likely useful as potential targets for serodiagnostic applications. |
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