{"database":"PeptideAtlas","file_versions":[],"scores":null,"additional":{"submitter":["Bell C, Smith GT, Sweredoski MJ, Hess S"],"disease":[""],"software":["TPP"],"full_dataset_link":["'https://db.systemsbiology.net/sbeams/cgi/PeptideAtlas/ManageTable.cgi?TABLE_NAME=AT_sample&sample_id=4897'"],"synonyms":[""],"submitter_email":["","polishhammer@gmail.com"],"repository":["PeptideAtlas"],"sample_protocol":[""],"data_protocol":[""],"omics_type":["Proteomics"],"pubmed":[""],"instrument_platform":["LTQ FT"],"project_tag":[""],"species":["Mycobacterium Tuberculosis"],"publication":[""],"pubmed_abstract":["Approximately, one-third of the world's population is infected with Mycobacterium tuberculosis, the causative agent of tuberculosis. Secreted and membrane proteins that interact with the host play important roles for the pathogenicity of the bacteria and are potential drug targets or components of vaccines. In this present study, subcellular fractionation in combination with membrane enrichment was used to comprehensively analyze the M. tuberculosis proteome. The proteome of the M. tuberculosis cell wall, membrane, cytosol, lysate, and culture filtrate was defined with a high coverage. Exceptional enrichment for membrane proteins was achieved using wheat germ agglutinin (WGA)-affinity two-phase partitioning, a technique that has to date not yet been exploited for the enrichment of mycobacterial membranes. Overall, 1051 M. tuberculosis protein groups including 183 transmembrane proteins have been identified by LC-MS/MS analysis using stringent database search criteria with a minimum of two peptides and an estimated FDR of less than 1%. With many mycobacterial antigens and lipoglycoproteins identified, the results from this study suggest that many of the newly discovered proteins could represent potential candidates mediating host-pathogen interactions. In addition, this data set provides experimental information about protein localization and thus serves as a valuable resource for M. tuberculosis proteome research."],"pubmed_title":["Characterization of the Mycobacterium tuberculosis proteome by liquid chromatography mass spectrometry-based proteomics techniques: a comprehensive resource for tuberculosis research."],"pubmed_authors":["Bell Christina C, Smith Geoffrey T GT, Sweredoski Michael J MJ, Hess Sonja S"],"pubmed_title_synonyms":["Mass Spectrum Analysis, Koch's Disease, Research and Development, Priorities, Bacillus tuberculosis, Mass Spectrum, Bacterium tuberculosis, Koch Disease, Mycobacterium tuberculosis (Zopf 1883) Lehmann and Neumann 1896 (Approved Lists 1980), Activity, Analyses, Infections, Kochs Disease, Peptidomics, Research, Laboratory, Mycobacterium tuberculosis H37Rv, Liquid Chromatography, Spectrometry, total expressed protein, Research Priorities, Spectrum Analyses, Mycobacterium tuberculosis Infections, Spectrum Analysis, Research Activities., Activities, Spectroscopy, MS, Priority, Mycobacterium tuberculosis var. hominis, Mass, Infection, Tuberculosis, Mycobacterium tuberculosis, Development and Research, Analysis, Research Priority, Mycobacterium tuberculosis Infection, Tuberculoses, Research Activity, Laboratory Research, Proteomes, Mass Spectrum Analyses, active tuberculosis, Mass Spectroscopy, Mycobacterium tuberculosis typus humanus"],"description_synonyms":["Membrane Tissue, membrane, transmembrane, PRSS, enzymes, Biocatalysts, Tissues, membrane region, beta-Trypsin, Tissue, Tripcellim, Alpha-Chymotrypsin Choay, integral to membrane, enzyme activity, Membrane, Alphacutanée, beta Trypsin, Trypure, Avazyme, Membrane Tissues, Enzyme, Biocatalyst, region of membrane, whole membrane, integral component of membrane."],"name_synonyms":["LUZP5, Membrane Tissue, membrane, transmembrane, CAP-G2, 5830426I05Rik, Tissues, general secretion pathway-associated complex, Luzp5, membrane region, Tissue, integral to membrane, Membrane, T2SS-associated complexes, Membrane Tissues, Sec-dependent secretion system-associated complex, mCAP-G2, region of membrane, whole membrane, main terminal branch, integral component of membrane., CAPG2, MTB, Mtb, hCAP-G2"],"pubmed_abstract_synonyms":["liquid chromatography tandem mass spectroscopy, Integral Membrane Proteins, host organism, Pathogen Interaction, Product, Activity, determination, Host Pathogen Relations, Laboratory, Surface Proteins, Membrane-Associated Proteins, protein, Integral, infectivity, Pathogen-Host Interaction, School-Age, Membrane Tissues, Polypeptides, Techniques, peptido, Pathogen Host Interactions, Method, Mycobacterium tuberculosis var. hominis, Pharmaceutical Product, Antigen, Tuberculosis, Research Activity, protein aggregate, Laboratory Research, Host-Pathogen Relation, Pathogen Interactions, Wheat, Koch's Disease, Cell Walls, Priorities, Bacillus tuberculosis, Bacterium tuberculosis, Koch Disease, Eubacteria, LCMSMS, peptides, Surface, membrane region, Tissue, wheat, Estimated, Tricum aestivum, common wheat, Host Pathogen Interactions, Bacteria Woese et al. 2024, Bacteria <bacteria>, Methodological Studies, medicine, Prokaryotae, Pharmaceutical, Durum Wheat, Triticum turgidum, Surface Protein, Membrane Associated Proteins, Procaryotae, Research Priority, establishment and maintenance of asymmetric protein localization, Membrane Protein, protein localisation, LC-MS2, Membrane Tissue, Mycobacterium tuberculosis (Zopf 1883) Lehmann and Neumann 1896 (Approved Lists 1980), PLATEST, Data Set, Triticum vulgare, LC-MS/MS, integral to membrane, Research Priorities, Triticum turgidum subsp. durum, Procedure, results, Interaction, School Age, Pathogenicity, prokaryotes, Pharmaceutic, Agglutinin, Research and Development, Populations, Cell Membrane Protein, Host-Pathogen, Membrane-Associated, Triticum sativum, Relation, Cell Membrane Proteins, Methodological, Methodological Study, Host-Pathogen Interaction, Activities, liquid chromatography-tandem mass spectroscopy, Cytosols, asymmetric protein localisation, School-Age Population, Polypeptide, Mycobacterium tuberculosis Infection, establishment and maintenance of protein localization, Proteomes, active tuberculosis, Platelets, Prokaryota, Integral Membrane, Triticum aestivum, Procedures, Gene, eubacteria, Triticum aestivum subsp. aestivum, protein-containing complex, LC-MS-MS, culture filtrate, method, Host-Pathogen Relations, Relations, Membrane-Associated Protein, integral component of membrane, method used in an experiment, Host Pathogen Interaction, LC-MSMS, Studies, Gene Products, Bacteriobiota, Technique, Walls, Drugs, Cell Membrane, School-Age Populations, study, asymmetric protein localization, Infections, Research, Tissues, Triticum aestivum8, Triticum spelta, Triticum aestivam, Population, Mycobacterium tuberculosis Infections, Monera, Research Activities., Bacteria (ex Cavalier-Smith 1987), Study, drugs, bread wheat, lysate, region of membrane, channel localizer activity, Host Pathogen, peptidos, Mycobacterium tuberculosis, fungi, Development and Research, Preparation, School Age Population, Pharmaceuticals, Products, membrane, Triticum durum, bacteria, culture medium, Kochs Disease, protein complex, drug, Proteins, total expressed protein, Cell Surface, Cell Surface Protein, Cell, Peptide, LC/MS/MS, Priority, native protein, Pathogen-Host Interactions, Protein, Canadian hard winter wheat, chemical analysis, Infection, Membrane Proteins, whole membrane, Tuberculoses, Cell Surface Proteins, Data Base, Membrane Associated Protein, Wall, transmembrane, Pharmaceutic Preparations, Pathogen-Host, Durum, Mycobacterium tuberculosis H37Rv, culture supernatant, Membrane, School Age Populations, Drug, plan specification, Protein Gene Products, Gene Proteins, Preparations, Durum Wheats, Integral Membrane Protein, Vaccine, Host, prokaryote, liquid chromatography tandem mass spectrometry, Peptid, virulence, assay, Pathogen Host Interaction, Pharmaceutical Products, Interactions, Mycobacterium tuberculosis typus humanus, Pharmaceutical Preparation"],"additional_accession":[]},"is_claimable":false,"name":"Mtb_Triple_Digest_membrane","description":"The digestive enzymes are trypsin, chymotrypsin and Lysc, membrane","dates":{"publication":"2012-12-31","export":"2016-03-29"},"accession":"PAe003635","cross_references":{"pubmed":["22053987"]}}