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Reports Outline Enzyme Precursors Study Results from Beijing Institute of Biotechnology (Proteomic analysis of the interaction of Bifidobacterium...

September 8, 2014



Reports Outline Enzyme Precursors Study Results from Beijing Institute of Biotechnology (Proteomic analysis of the interaction of Bifidobacterium longum NCC2705 with the intestine cells Caco-2 and identification of plasminogen receptors)

By a News Reporter-Staff News Editor at Proteomics Weekly -- Current study results on Enzymes and Coenzymes have been published. According to news reporting originating from Beijing, People's Republic of China, by NewsRx correspondents, research stated, "To identify proteins with a potential role in the interaction of Bifidobacterium longum with intestinal epithelial cells, we profiled the protein response of B. longum NCC2705 following interaction with Caco-2 cells. Thirty-one protein spots, belonging to a total of 23 proteins, which exhibited a change in abundance of at least 3-fold were identified in B. longum NCC2705 following co-culture with Caco-2 cells, and were subsequently identified."

Our news editors obtained a quote from the research from the Beijing Institute of Biotechnology, "Changes in expression were confirmed at the transcriptional level for a selection of these proteins. Enolase (Eno) and elongation factor Tu (EF-Tu) were amongst the proteins that showed the most prominent increase in abundance. Interaction of these proteins with plasminogen (Pig) was analyzed by Pig overlay assays, glutathione S-transferase (GST)-pull down, and western blot analysis. The results suggested that EF-Tu and Eno serve as surface receptors for B. longum NCC2705 binding to human plasminogen. Purified GST EF-Tu and GST Eno inhibited adhesion of B. longum NCC2705 to Caco-2 cells. Collectively, our data suggest that Eno and EF-Tu moonlight as adhesions, and are possibly involved in the protective role played by B. longum NCC2705 in defense against enteric pathogens. Biological significance The interaction of bifidobacteria with the human host plasminogen/plasmin system confirms the existence of a new component in the molecular cross-talk between bacteria and the host."

According to the news editors, the research concluded: "Our study analyzed proteins EF-Tu and Eno with Plg binding activity, and they can inhibit adhesion of B. longum NCC2705 to Caco-2 cells, suggesting their role in the bacterial adherent to the enterocyte surface."

For more information on this research see: Proteomic analysis of the interaction of Bifidobacterium longum NCC2705 with the intestine cells Caco-2 and identification of plasminogen receptors. Journal of Proteomics, 2014;108():89-98. Journal of Proteomics can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Journal of Proteomics - www.elsevier.com/wps/product/cws_home/713351)

The news editors report that additional information may be obtained by contacting X. Wei, Beijing Inst Biotechnol, Beijing 100850, People's Republic of China. Additional authors for this research include X.B. Yan, X.N. Chen, Z. Yang, H. Li, D.Y. Zou, X. He, S.M. Wang, Q. Cui, W. Liu, D. Zhurina, X.S. Wang, X.N. Zhao, L.Y. Huang, M. Zeng, Q.N. Ye, C.U. Riedel and J. Yuan (see also Enzymes and Coenzymes).

Keywords for this news article include: Beijing, People's Republic of China, Asia, Beta-Globulins, Blood Proteins, Caco-2 Cells, Enzyme Precursors, Enzymes and Coenzymes, Plasminogen, Proteomics

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Proteomics Weekly


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