{"database":"MassIVE","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://massive-ftp.ucsd.edu/v04/MSV000089990/"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":0,"searchCount":0},"additional":{"submitter":["Laurence Florens"],"full_dataset_link":["https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=cb51d464c1fe436aa7ded590680a5985"],"submitter_email":["laf@stowers.org"],"sample_protocol":[""],"repository":["MassIVE"],"file_size":["830"],"ptm_modification":["MOD:01060 - \"A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.\"","MOD:00719 - \"A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues.\""],"data_protocol":[""],"omics_type":["Proteomics"],"instrument_platform":["LTQ (Thermo Scientific instrument model)"],"species":["Borrelia Burgdorferi B31 (ncbitaxon:224326)"],"submitter_affiliation":["The Stowers Institute for Medical Research"],"pubmed_abstract":["Borrelia spirochetes are unique among diderm bacteria in their lack of lipopolysaccharide (LPS) in the outer membrane (OM) and their abundance of surface-exposed lipoproteins with major roles in transmission, virulence, and pathogenesis. Despite their importance, little is known about how surface lipoproteins are translocated through the periplasm and the OM. Here, we characterized Borrelia burgdorferi BB0838, a distant homolog of the OM LPS assembly protein LptD. Using a CRISPR interference approach, we showed that BB0838 is required for cell growth and envelope stability. Upon BB0838 knockdown, surface lipoprotein OspA was retained in the inner leaflet of the OM, as determined by its inaccessibility to in situ proteolysis but its presence in OM vesicles. The topology of the OM porin/adhesin P66 remained unaffected. Quantitative mass spectrometry of the B. burgdorferi membrane-associated proteome confirmed the selective periplasmic retention of surface lipoproteins under BB0838 knockdown conditions. Additional analysis identified a single in situ protease-accessible BB0838 peptide that mapped to a predicted β-barrel surface loop. Alphafold Multimer modeled a B. burgdorferi LptB<sub>2</sub> FGCAD complex spanning the periplasm. Together, this suggests that BB0838/LptD<sub>Bb</sub> facilitates the essential terminal step in spirochetal surface lipoprotein secretion, using an orthologous OM component of a pathway that secretes LPS in proteobacteria."],"pubmed_title":["A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane."],"pubmed_authors":["He Huan H, Pramanik Ankita S AS, Swanson Selene K SK, Johnson David K DK, Florens Laurence L, Zückert Wolfram R WR"],"pubmed_abstract_synonyms":["biochemical pathways, CG32067, Proteobacteria, Porin, Ghrfr, Pore Proteins, determination, C85233, positive regulation by symbiont of host non-apoptotic programmed cell death, PORIN, Periplasmic Spaces, protein, Circulating, sci, PPS1, infectivity, Space, SUB, Borrelia burgdorferi, peptide, Membrane Tissues, Polypeptides, protein polypeptide chains, DSmurf, peptido, DmelCG12298, GRP1, DmPorin1, Grp1, pathogenesis, HOW, How, envelope, Borrelia, SCRAMBLED, Analysis, neurological Lyme disease, protein aggregate, Lyme neuroborreliosis, KIF20A, l(3)j5D5, integumentum commune, Relapsing Fever Borrelia, 24B, Borrelia burgdorffragment, Mass Spectrum Analysis, l(3)j4A5, viral infection, periplasm, Eubacteria, Circulating Lipoproteins, stimulation by symbiont of host programmed cell death, anon-WO02059370.56, peptides, ATP-dependent proteolysis, Analyses, catabolism, Bannworth's syndrome, non-developmental growth of a unicellular organism, OFC6, PTPSTEP, membrane region, Tissue, PPS, stru, Bodily, Borrelia burdorferi, proteins, metabolic process resulting in cell growth, l(3)S053606, CG10293, Protein Degradation, retention, Bacteria Woese et al. 2024, l(3)j5B5, dp66, Secretion, proteobacteria, Bacteria <bacteria>, VDAC-1, Prokaryotae, Smurf, l(2)k08110, Secretions, cleft lip and/or palate with mucous cysts of lower lip, cellular growth, DVDAC, biotransformation, Procaryotae, purple photosynthetic bacteria and relatives, associated, CG4943, GPH, D-smurf, Lyme disease, Pore Protein, 2410142G14Rik, Membrane Tissue, 0904/17, Periplasms, Degradations, external covering of organism, plural), external secretion, metabolism resulting in cell growth, Shc, STRUBBELIG, integral to membrane, organism surface, lit, VWS1, Purple Bacteria, Lipopolysaccharide, Lack, membranous organ component, Borreliella burgdorferi caused disease or disorder, Spectrum Analysis, predicted, Spectroscopy, exocrine gland fluid/secretion, Bodily Secretion, Lipoglycans, SZ1, Digestion, non-developmental cell growth, Steere's disease, 3.1.3.48, Lyme borreliosis, Pathogenicity, modulation by symbiont of host system process, neuroborreliosis, prokaryotes, secretion, Pore, Rasl2-8, little, Spirochetes, outer membrane exporter porin, membrane of organ, DmelCG4943, Step, CG11628, Borrelia burgdorferi infection, Protein Digestions, Spectrometry, Striatum-enriched protein-tyrosine phosphatase, Borreliella burgdorferi infectious disease, exposed, Lyme Disease Spirochete, Ran/M1, porin, integumentary system, STEP, activation by symbiont of host programmed cell death, l(3)rN672, Lipoproteins, Periplasmic Space, anon-EST:Liang-2.39, Polypeptide, dermal system, exocrine gland secretion, Borrelia burgdorferi sensu stricto, Proteomes, Borreliella burgdorferi disease or disorder, p66/68-like, Prokaryota, pinna (narrow), AT1G11140, GRP1/cytohesin 1, exocrine gland fluid, CG8000, exocrine gland fluid or secretion, P62, dSmurf1, regulation by symbiont of host system process, Degradation, number, P66, cg6647, P68, Gene, Periplasmic, eubacteria, Spectrum Analyses, protein-containing complex, presence, CG12298, CG11633, cytohesin/GRP1, surface, polypeptide chain, induction by organism of non-apoptotic programmed cell death in other organism during symbiotic interaction, integral component of membrane, Gene Products, Mass, p66, lip pit syndrome, Bacteriobiota, Proteobacteriota, Mass Spectroscopy, DmelCG6647, Spirochete, Ly87, l(3)s2612, DmVDAC, growth of cell, p66shc, Tissues, LPS, Lps, mei-1794, pinnae (narrow, l(2)SH2 0323, ShcA, causes, Vdac, anon-WO0118547.361, Bacteria, Protein Degradations, Monera, Bacteria (ex Cavalier-Smith 1987), lipopolysaccharides, secreted substance, extruding from, d-smurf, Neural-specific protein-tyrosine phosphatase, bodily secretion, DmelCG32067, l(2)k05123, causality, DmelCG10293, region of membrane, peptidos, SRF9, fungi, VDAC, PIT, Lyme disease spirochete, membrane, bacteria, activation by organism of non-apoptotic programmed cell death in other organism, hemolysin activity, pinnule (narrow), degradation, Lipoprotein, clone 2.39, protein complex, exits through, Proteins, total expressed protein, stepk, CG7983, qkr, Dsmurf, Protein Digestion, l(3)S090417, POR-1, murein sacculus, Digestions, Peptide, STRUBBELIG-RECEPTOR FAMILY 9, dSmurf, polypeptide, cell expansion, \"Alphaproteobacteriota\" Whitman et al. 2018, count in organism, Alphaproteobacteriota, Bannwarth syndrome, MS, native protein, natural protein, Proteolyses, PPP1R128, Smurf ubiquitin ligase, KH93F, Protein, chemical analysis, whole membrane, peptidoglycan, VWS, Spaces, l(2)SH0323, Mass Spectrum Analyses, who, CYH1, Mass Spectrum, transmembrane, Purple., biodegradation, storage, body surface, Dub, Who/How, Ran|M1, Membrane, DmelCG11628, Protein Gene Products, Gene Proteins, prokaryote, qkr[93F], CG6647, Peptid, virulence, l(3)01814, assay, sequestering, T19D16.8, SCM"],"name_synonyms":["biochemical pathways, Lyme disease spirochete, external covering of organism, exocrine gland fluid, degradation, Lipoprotein, exocrine gland fluid or secretion, protein complex, phospholipid scrambling, external secretion, Arts, Sprain, Proteins, flippase, Gene, organism surface, protein, Circulating, protein-containing complex, strain, Borrelia burgdorferi, exocrine gland fluid/secretion, Bodily Secretion, surface, protein polypeptide chains, native protein, natural protein, polypeptide chain, Protein, Strain, Gene Products, secretion, cultivar, protein aggregate, Sprains, integumentum commune, Borrelia burgdorffragment, Industrial Arts, Circulating Lipoproteins, biodegradation, body surface, catabolism, Bodily, Borrelia burdorferi, proteins, ecotype, Lyme Disease Spirochete, Protein Gene Products, Gene Proteins, secreted substance, Secretion, bodily secretion, integumentary system, Secretions, Lipoproteins, biotransformation, Strains, Industrial., Strains and Sprains, dermal system, exocrine gland secretion, Borrelia burgdorferi sensu stricto"],"pubmed_title_synonyms":["Borrelia burgdorffragment, Borrelia burgdorferi, Lyme disease spirochete, surface, external covering of organism, Circulating Lipoproteins, integumentary system, body surface, Lipoproteins, Borrelia burdorferi, organism surface, Circulating, Lipoprotein., dermal system, Borrelia burgdorferi sensu stricto, Lyme Disease Spirochete, integumentum commune"],"description_synonyms":["biochemical pathways, Lyme disease spirochete, external covering of organism, exocrine gland fluid, degradation, Lipoprotein, exocrine gland fluid or secretion, protein complex, phospholipid scrambling, external secretion, Arts, Sprain, Proteins, flippase, Gene, organism surface, protein, Circulating, protein-containing complex, strain, Borrelia burgdorferi, exocrine gland fluid/secretion, Bodily Secretion, surface, protein polypeptide chains, native protein, natural protein, polypeptide chain, Protein, Strain, Gene Products, secretion, cultivar, protein aggregate, Sprains, integumentum commune, Borrelia burgdorffragment, Industrial Arts, Circulating Lipoproteins, biodegradation, body surface, catabolism, Bodily, Borrelia burdorferi, proteins, ecotype, Lyme Disease Spirochete, Protein Gene Products, Gene Proteins, secreted substance, Secretion, bodily secretion, integumentary system, Secretions, Lipoproteins, biotransformation, Strains, Industrial., Strains and Sprains, dermal system, exocrine gland secretion, Borrelia burgdorferi sensu stricto"],"citation_count":["0"],"additional_accession":["PXD035604"]},"is_claimable":false,"name":"Identification of the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.","description":"To identify the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.","dates":{"publication":"Wed Jul 27 14:47:00 BST 2022"},"accession":"MSV000089990","cross_references":{"pubmed":["37170643"]}}