2017 Fiscal Year Final Research Report
Comprehensive analysis of moonlighting proteins of lactic acid bacteria and its application to multifunctional markers
| Project/Area Number |
15K21259
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied microbiology
Animal production science
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| Research Institution | Tokai University (2016-2017)
Miyagi University (2015) |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Keywords | 多機能性タンパク質 / GAPDH / GroEL / ムーンライティングプロテイン / 重金属 / 腸管付着性 / 乳酸菌 / 菌体表層タンパク質 |
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| Outline of Final Research Achievements |
Moonlighting protein is a multifunctional protein possessed by lactic acid bacteria, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and GroEL are representative moonlighting proteins. Many proteins such as glycolytic enzymes, heat shock proteins, and ribosomal proteins were identified by proteome analysis of PBS extract from bacterial cell surface.
Next, rGAPDH and rGroEL showed the ability to bind to type A blood type antigen. The relationship between GAPDH and heavy metal tolerance in lactic acid bacteria were researched. In a cadmium, it was suggested that the cell surface GAPDH adsorbs cadmium and contributes to alleviating the toxicity. In a mercury, however, mercury may be toxic by taking it into the bacterial cell after adsorption. Mercury is also adsorbed by GAPDH whereas cytotoxicities were enhanced in the presence of cell surface GAPDH. It suggests that mercury may be incorporated into the bacterial cells after adsorption.
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| Free Research Field |
応用微生物学
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