title: Identification of surface-associated proteins of Bifidobacterium animalis ssp. lactis KLDS 2.0603 by enzymatic shaving.
abstract: Bifidobacteria are commensal microorganisms of the human and animal intestinal tract, and their surface proteins can mediate bacterial communication and chemical sensing in the environment, as well as facilitate interactions between bacteria and the host. However, a systematic study of the outer surface-associated proteome of bifidobacteria has not been undertaken. In the present study, the proteins located on the surface of Bifidobacterium animalis ssp. lactis KLDS 2.0603 were systematically identified by a nongel proteomic approach, which consisted of the shaving of the bacterial surface with trypsin and an analysis of the released peptides by liquid chromatography-tandem mass spectrometry. A total of 105 surface-associated proteins were found, of which 15 proteins could potentially be involved in adhesion and interactions between bifidobacteria and the host. The proteins related to adhesion and interaction between bacteria and the host include pilus structure proteins (Fim A, Fim B), 10 moonlighting proteins, an NLP/P60 family protein, an immunogenic secreted protein, and a putative sugar-binding secreted protein. The results provide the basis for future studies on the molecular mechanisms of the interactions between bifidobacteria and the host.
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China; College of Life Sciences, Jiamusi University, Jiamusi 154007, People's Republic of China.
authors.forename: Dequan
authors.initials: D
authors.lastname: Zhu
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China.
authors.forename: Yu
authors.initials: Y
authors.lastname: Sun
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China.
authors.forename: Fei
authors.initials: F
authors.lastname: Liu
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China.
authors.forename: Aili
authors.initials: A
authors.lastname: Li
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China.
authors.forename: Limei
authors.initials: L
authors.lastname: Yang
authors.affiliation: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin 150030, People's Republic of China. Electronic address: xchmeng@hotmail.com.
authors.forename: Xiang-Chen
authors.initials: XC
authors.lastname: Meng
mesh_terms: D001386:Azides / Q000737:chemistry; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D000069982:Bifidobacterium animalis / Q000235:genetics* / Q000378:metabolism; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D011419:Propidium / Q000031:analogs & derivatives / Q000737:chemistry; D060888:Real-Time Polymerase Chain Reaction; D014357:Trypsin / Q000737:chemistry
chemical_list: D001386:Azides; D001426:Bacterial Proteins; D008565:Membrane Proteins; C533957:propidium monoazide; D011419:Propidium; D014357:Trypsin
keywords: interaction between probiotics and host; probiotics; shotgun proteomics; surface proteins