Proteome profile and primary function exploration of Vagococcus fluvialis
CAO Yu1, ZHOU Ting1, DUAN Xiao-lei2, CHEN Ze-hui1, YANG Huan1, MIN Xun1,2
1. Department of Laboratory Medicine of the Affiliated hospital, Zunyi Medical College, Zunyi 563003, China; 2. School of Laboratory Medicine, Zunyi Medical College, Zunyi 563000, China
Abstract:Based on the high-precision mass spectrometry platform, the proteomics analysis was first applied on Vagococcus fluvialis to identify the protein components and explore the primary biological functions. The Vagococcus fluvialis was isolated from the infected puncture fluid of lower left femur from a patient in China. By using liquid chromatography-tandem mass spectrometry and label free quantification technology, the most comprehensive proteome profile of Vagococcus fluvialis was constructed, containing 1 372 proteins. All mass spectrometry profiles were analyzed using the MaxQuant software; the identified proteins were then annotated according to biological processes, molecular functions and cellular components Gene Ontology, as well as KEGG pathway analysis. As results, most proteins are involved in the basic biological processes, including transcription, translation, metabolism and biosynthesis. The top ten proteins with most identified intensities are enzymes and ribosomal proteins, among which, the Enolase and Phosphoglycerate kinase are key enzymes involved in glycolysis, and could be involved in bacterial virulence. In summary, the proteome profile dataset constructed in this study would provide better understanding on pathogenic mechanisms of Vagococcus fluvialis at the level of protein expression.
曹喻, 周婷, 段晓雷, 陈泽慧, 杨欢, 闵迅. 河流漫游球菌蛋白质组鉴定及功能初探[J]. 中国人兽共患病学报, 2020, 36(11): 900-906.
CAO Yu, ZHOU Ting, DUAN Xiao-lei, CHEN Ze-hui, YANG Huan, MIN Xun. Proteome profile and primary function exploration of Vagococcus fluvialis. Chinese Journal of Zoonoses, 2020, 36(11): 900-906.
[1] Collins MD, Ash C, Farrow JA, et al.16S ribosomal ribonucleic acid sequence analyses of lactococci and related taxa. Description of Vagococcus fluvialis gen. nov., sp. nov[J]. J Appl Bacteriol, 1989, 67(4):453-460. DOI: 10.1111/j.1365-2672.1989.tb02516.x [2] Schmidtke LM, Carson J.Characteristics of Vagococcus salmoninarum isolated from diseased salmonid fish[J]. J Appl Bacteriol, 1994, 77(2): 229-236. DOI: 10.1111/j.1365-2672.1994.tb03068.x [3] Wallbanks S, Martinez-Murcia AJ, Fryer JL, et al.16S rRNA sequence determination for members of the genus Carnobacterium and related lactic acid bacteria and description of Vagococcus salmoninarum sp.nov.[J]. Int J Syst Bacteriol, 1990, 40(3): 224-230. DOI: 10.1099/00207713-40-3-224 [4] Lawson PA, Foster G, Falsen E, et al. Vagococcus lutrae sp. nov., isolated from the common otter (Lutra lutra)[J]. Int J Syst Bacteriol, 1999, 49 Pt 3: 1251-1254. DOI: 10.1099/00207713-49-3-1251 [5] Hoyles L, Lawson PA, Foster G, et al. Vagococcus fessus sp. nov., isolated from a seal and a harbour porpoise[J]. Int J Syst Evol Microbiol, 2000, 50 Pt 3: 1151-1154. DOI: 10.1099/00207713-50-3-1151 [6] Shewmaker PL, Steigerwalt AG, Morey RE, et al.Vagococcus carniphilus sp. nov., isolated from ground beef[J]. Int J Syst Evol Microbiol, 2004, 54(Pt 5): 1505-1510. DOI: 10.1099/ijs.0.02908-0 [7] Teixeira LM, Carvalho MG, Merquior VL, et al.Phenotypic and genotypic characterization of Vagococcus fluvialis, including strains isolated from human sources[J]. J Clin Microbiol, 1997, 35(11): 2778-2781. DOI: 10.1128/JCM.35.11.2778-2781.1997 [8] Al-Ahmad A, Pelz K, Schirrmeister JF, et al.Characterization of the first oral vagococcus isolate from a root-filled tooth with periradicular lesions[J]. Curr Microbiol,2008, 57(3): 235-238. DOI: 10.1007/s00284-008-9182-0 [9] Schirrmeister JF, Liebenow AL, Pelz K, et al.New bacterial compositions in root-filled teeth with periradicular lesions[J]. J Endod, 2009, 35(2): 169-174. DOI: 10.1016/j.joen.2008.10.024 [10] Garcia V, Abat C, Rolain JM.Report of the first Vagococcus lutrae human infection, Marseille, France[J]. New Microbes New Infect, 2016, 9: 56-57. DOI: 10.1016/j.nmni.2015.11.008 [11] Darzi AAWA, Nour KA. Vagococcus fluvialis causing severe infective endocarditis presenting with embolic stroke: A case report[J]. J Clin Exp Cardiolog, 2016, 7: 8(Suppl) 44-48. DOI: 10.4172/2155-9880.C1.047 [12] Khemiri A, Jouenne T, Cosette P.Proteomics dedicated to biofilmology: What have we learned from a decade of research[J]. Med Microbiol Immunol, 2016, 205(1): 1-19. DOI: 10.1007/s00430-015-0423-0 [13] Gregory D, Chaudet H, Lagier JC, et al.How mass spectrometric approaches applied to bacterial identification have revolutionized the study of human gut microbiota[J]. Expert Rev Proteomics, 2018, 15(3): 217-229. DOI: 10.1080/14789450.2018.1429271 [14] Saleh S, Staes A, Deborggraeve S, et al.Targeted proteomics for studying pathogenic bacteria[J]. Proteomics, 2019: e1800435. DOI: 10.1002/pmic.201800435 [15] 周婷, 曹喻, 段晓雷. 首次从人左股骨下段术后感染穿刺液中分离河流漫游球菌[J]. 中华医院感染学杂志, 2019, 29(18): 2825-2829. DOI: 10.11816/cn.ni.2019-190582 [16] Bradford MM.A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding[J]. Anal Biochem, 1976,72: 248-254. DOI: 10.1006/abio.1976.9999 [17] Cox J, Mann M.MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification[J]. Nat Biotechnol, 2008, 26(12): 1367-1372. DOI: 10.1038/nbt.1511 [18] Tyanova S, Temu T, Cox J.The MaxQuant computational platform for mass spectrometry-based shotgun proteomics[J]. Nat Protoc, 2016, 11(12): 2301-2319. DOI: 10.1038/nprot.2016.136 [19] Consortium TU.UniProt: the universal protein knowledgebase[J]. Nucleic Acids Res, 2017, 45(D1): D158-D169. DOI: 10.1093/nar/gkw1099 [20] Schwanhausser B, Busse D, Li N, et al.Global quantification of mammalian gene expression control[J]. Nature, 2011, 473(7347): 337-342. DOI: 10.1038/nature10098 [21] Ashburner M, Ball CA, Blake JA, et al.Gene ontology: tool for the unification of biology. The gene ontology consortium[J]. Nat Genet, 2000, 25(1): 25-29. DOI: 10.1038/75556 [22] Ogata H, Goto S, Sato K, et al.KEGG: Kyoto Encyclopedia of Genes and Genomes[J]. Nucleic Acids Res, 1999, 27(1): 29-34. DOI: 10.1093/nar/27.1.29 [23] Bergmann S, Rohde M, Chhatwal GS, et al.alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface[J]. Mol Microbiol, 2001, 40(6): 1273-1287. DOI: 10.1046/j.1365-2958.2001.02448.x [24] Gottschalk M, Dubreuil JD, Esgleas M, et al. The alpha-enolase of Streptococcus suis: a previously well-known and well-characterized protein[J]. J Infect Dis,2010, 201(11): 1775-1776; author reply 1776-1777. DOI: 10.1086/652417 [25] Yu X, Zheng L, Yang J, et al.Characterization of essential enolase in Staphylococcus aureus[J]. World J Microbiol Biotechnol, 2011, 27(4): 897-905. DOI: 10.1007/s11274-010-0532-2 [26] Blom AM, Bergmann S, Fulde M, et al.Streptococcus pneumoniae phosphoglycerate kinase is a novel complement inhibitor affecting the membrane attack complex formation[J]. J Biol Chem,2014, 289(47): 32499-32511. DOI: 10.1074/jbc.M114.610212 [27] Boone TJ, Tyrrell GJ.Identification of the actin and plasminogen binding regions of group B streptococcal phosphoglycerate kinase[J]. J Biol Chem, 2012, 287(34): 29035-29044. DOI: 10.1074/jbc.M112.361261