Relevant bibliographies by topics / Outer membrane proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Outer membrane proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 January 2023

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Journal articles on the topic "Outer membrane proteins"

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Ishikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh, and Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly." Journal of Cell Biology 166, no. 5 (August 23, 2004): 621–27. http://dx.doi.org/10.1083/jcb.200405138.

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Mitochondrial outer and inner membranes contain translocators that achieve protein translocation across and/or insertion into the membranes. Recent evidence has shown that mitochondrial β-barrel protein assembly in the outer membrane requires specific translocator proteins in addition to the components of the general translocator complex in the outer membrane, the TOM40 complex. Here we report two novel mitochondrial outer membrane proteins in yeast, Tom13 and Tom38/Sam35, that mediate assembly of mitochondrial β-barrel proteins, Tom40, and/or porin in the outer membrane. Depletion of Tom13 or Tom38/Sam35 affects assembly pathways of the β-barrel proteins differently, suggesting that they mediate different steps of the complex assembly processes of β-barrel proteins in the outer membrane.
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Hancock, R. E. W., R. Siehnel, and N. Martin. "Outer membrane proteins of Pseudomonas." Molecular Microbiology 4, no. 7 (July 1990): 1069–75. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00680.x.

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Winter, A. J. "Outer membrane proteins of Brucella." Annales de l'Institut Pasteur / Microbiologie 138, no. 1 (January 1987): 87–89. http://dx.doi.org/10.1016/0769-2609(87)90081-0.

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Otzen, Daniel E., and Kell K. Andersen. "Folding of outer membrane proteins." Archives of Biochemistry and Biophysics 531, no. 1-2 (March 2013): 34–43. http://dx.doi.org/10.1016/j.abb.2012.10.008.

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Im, Wonpil. "Bacterial Outer Membranes and Interactions with Membrane Proteins." Biophysical Journal 108, no. 2 (January 2015): 370a. http://dx.doi.org/10.1016/j.bpj.2014.11.2030.

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Mayer, A., R. Lill, and W. Neupert. "Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria." Journal of Cell Biology 121, no. 6 (June 15, 1993): 1233–43. http://dx.doi.org/10.1083/jcb.121.6.1233.

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Nuclear-encoded proteins destined for mitochondria must cross the outer or both outer and inner membranes to reach their final sub-mitochondrial locations. While the inner membrane can translocate preproteins by itself, it is not known whether the outer membrane also contains an endogenous protein translocation activity which can function independently of the inner membrane. To selectively study the protein transport into and across the outer membrane of Neurospora crassa mitochondria, outer membrane vesicles were isolated which were sealed, in a right-side-out orientation, and virtually free of inner membranes. The vesicles were functional in the insertion and assembly of various outer membrane proteins such as porin, MOM19, and MOM22. Like with intact mitochondria, import into isolated outer membranes was dependent on protease-sensitive surface receptors and led to correct folding and membrane integration. The vesicles were also capable of importing a peripheral component of the inner membrane, cytochrome c heme lyase (CCHL), in a receptor-dependent fashion. Thus, the protein translocation machinery of the outer mitochondrial membrane can function as an independent entity which recognizes, inserts, and translocates mitochondrial preproteins of the outer membrane and the intermembrane space. In contrast, proteins which have to be translocated into or across the inner membrane were only specifically bound to the vesicles, but not imported. This suggests that transport of such proteins involves the participation of components of the intermembrane space and/or the inner membrane, and that in these cases the outer membrane translocation machinery has to act in concert with that of the inner membrane.
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Lopez, Job E., William F. Siems, Guy H. Palmer, Kelly A. Brayton, Travis C. McGuire, Junzo Norimine, and Wendy C. Brown. "Identification of Novel Antigenic Proteins in a Complex Anaplasma marginale Outer Membrane Immunogen by Mass Spectrometry and Genomic Mapping." Infection and Immunity 73, no. 12 (December 2005): 8109–18. http://dx.doi.org/10.1128/iai.73.12.8109-8118.2005.

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ABSTRACT Immunization with purified Anaplasma marginale outer membranes induces complete protection against infection that is associated with CD4+ T-lymphocyte-mediated gamma interferon secretion and immunoglobulin G2 (IgG2) antibody titers. However, knowledge of the composition of the outer membrane immunogen is limited. Recent sequencing and annotation of the A. marginale genome predicts at least 62 outer membrane proteins (OMP), enabling a proteomic and genomic approach for identification of novel OMP by use of IgG serum antibody from outer membrane vaccinates. Outer membrane proteins were separated by two-dimensional electrophoresis, and proteins recognized by total IgG and IgG2 in immune sera of outer membrane-vaccinated cattle were detected by immunoblotting. Immunoreactive protein spots were excised and subjected to liquid chromatography-tandem mass spectrometry. A database search of the A. marginale genome identified 24 antigenic proteins that were predicted to be outer membrane, inner membrane, or membrane-associated proteins. These included the previously characterized surface-exposed outer membrane proteins MSP2, operon associated gene 2 (OpAG2), MSP3, and MSP5 as well as recently identified appendage-associated proteins. Among the 21 newly described antigenic proteins, 14 are annotated in the A. marginale genome and include type IV secretion system proteins, elongation factor Tu, and members of the MSP2 superfamily. The identification of these novel antigenic proteins markedly expands current understanding of the composition of the protective immunogen and provides new candidates for vaccine development.
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Schwaiger, M., V. Herzog, and W. Neupert. "Characterization of translocation contact sites involved in the import of mitochondrial proteins." Journal of Cell Biology 105, no. 1 (July 1, 1987): 235–46. http://dx.doi.org/10.1083/jcb.105.1.235.

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Import of proteins into the mitochondrial matrix requires translocation across two membranes. Translocational intermediates of mitochondrial proteins, which span the outer and inner membrane simultaneously and thus suggest that translocation occurs in one step, have recently been described (Schleyer, M., and W. Neupert, 1985, Cell, 43:339-350). In this study we present evidence that distinct membrane areas are involved in the translocation process. Mitochondria that had lost most of their outer membrane by digitonin treatment (mitoplasts) still had the ability to import proteins. Import depended on proteinaceous structures of the residual outer membrane and on a factor that is located between the outer and inner membranes and that could be extracted with detergent plus salt. Translocational intermediates, which had been preformed before fractionation, remained with the mitoplasts under conditions where most of the outer membrane was subsequently removed. Submitochondrial vesicles were isolated in which translocational intermediates were enriched. Immunocytochemical studies also suggested that the translocational intermediates are located in areas where outer and inner membranes are in close proximity. We conclude that the membrane-potential-dependent import of precursor proteins involves translocation contact sites where the two membranes are closely apposed and are linked in a stable manner.
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Lee, Joonseong, and Wonpil Im. "Modeling and Simulation of Outer Membrane Proteins in Pseudomonas Aeruginosa Outer Membranes." Biophysical Journal 114, no. 3 (February 2018): 241a. http://dx.doi.org/10.1016/j.bpj.2017.11.1344.

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Hazlett, Karsten R. O., David L. Cox, Marc Decaffmeyer, Michael P. Bennett, Daniel C. Desrosiers, Carson J. La Vake, Morgan E. La Vake, et al. "TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability." Journal of Bacteriology 187, no. 18 (September 15, 2005): 6499–508. http://dx.doi.org/10.1128/jb.187.18.6499-6508.2005.

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ABSTRACT The outer membrane of Treponema pallidum, the noncultivable agent of venereal syphilis, contains a paucity of protein(s) which has yet to be definitively identified. In contrast, the outer membranes of gram-negative bacteria contain abundant immunogenic membrane-spanning β-barrel proteins mainly involved in nutrient transport. The absence of orthologs of gram-negative porins and outer membrane nutrient-specific transporters in the T. pallidum genome predicts that nutrient transport across the outer membrane must differ fundamentally in T. pallidum and gram-negative bacteria. Here we describe a T. pallidum outer membrane protein (TP0453) that, in contrast to all integral outer membrane proteins of known structure, lacks extensive β-sheet structure and does not traverse the outer membrane to become surface exposed. TP0453 is a lipoprotein with an amphiphilic polypeptide containing multiple membrane-inserting, amphipathic α-helices. Insertion of the recombinant, nonlipidated protein into artificial membranes results in bilayer destabilization and enhanced permeability. Our findings lead us to hypothesize that TP0453 is a novel type of bacterial outer membrane protein which may render the T. pallidum outer membrane permeable to nutrients while remaining inaccessible to antibody.
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Dissertations / Theses on the topic "Outer membrane proteins"

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Chalton, David Allen. "Engineering of outer membrane proteins." Thesis, University of Newcastle Upon Tyne, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.430336.

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Cox, Katherine L. "Molecular dynamics of outer membrane proteins." Thesis, University of Oxford, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.427881.

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Millar, Douglas G. "Assembly pathways of outer mitochondrial membrane proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0022/NQ29951.pdf.

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Millar, Douglas G. "Assembly pathways of outer mitochondrial membrane proteins." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=42046.

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The pathway of membrane insertion and assembly of a signal anchor sequence specific for the outer mitochondrial membrane has been investigated. Signal anchor protein insertion into the outer membrane, in vitro, was found to overlap with a general import pathway followed by the outer membrane protein, porin, as well as matrix-targeted proteins. However, signal anchor protein insertion did not require a postreceptor import step involved in porin insertion and matrix protein translocation. Also, in contrast to the membrane insertion of porin, signal anchor protein insertion did not require nucleoside triphosphates for transfer of bound precursor to the membrane assembled form. Following outer membrane integration, a hybrid protein containing the signal anchor sequence of yeast Tom70 was found to assemble into homodimers. Dimerization was mediated by the transmembrane domain. A sequence motif containing alanine residues clustered on one face of the predicted membrane-spanning $ alpha$-helix was important for dimerization, perhaps allowing favourable close packing of the transmembrane helices.
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Gagnon, Jean-Nicolas. "Molecular interactions of bacterial outer membrane proteins." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=81333.

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Transport of iron-siderophores and vitamin B12 across the outer membrane (OM) of Gram-negative bacteria requires energy from the proton motive force delivered by the TonB/ExbB/ExbD complex. TonB-dependent OM receptors such as FhuA, FepA, FecA and BtuB possess a Ton box: a conserved motif located proximal to their N-terminus that has been shown to interact with TonB. However, other sites on OM receptors have been proposed to participate in interactions with TonB. To identify novel sites of interactions with TonB, we selected TonB-binding peptides from a random library of peptides displayed on phages. Fifteen peptides displayed sequence similarities to known TonB-dependent OM receptors. Of the fifteen, eight were mapped to regions of FhuA, FepA and FecA for which crystal structures are available. DNA sequences for selected peptides were fused to malE and displayed at the N-terminus of the E. coli maltose binding protein (MBP) for further characterization. Surface plasmon resonance experiments revealed that when the peptides were monovalently displayed on MBP, they retained TonB-binding activity thereby permitting assessments of their binding characteristics. In vitro and in vivo assays demonstrated that only FhuA-mapping peptides could disrupt TonB-FhuA interactions, indicating that TonB selectively binds to multiple regions distinct for each OM receptor.
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Bond, Peter J. "Simulation studies of bacterial outer membrane proteins." Thesis, University of Oxford, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.419258.

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Melillo, Amanda Adeline. "Identification of Francisella tularensis Outer Membrane Proteins." University of Toledo Health Science Campus / OhioLINK, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=mco1121867713.

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Habib, Shukry James. "Biogenesis and function of mitochondrial outer membrane proteins." Diss., [S.l.] : [s.n.], 2006. http://edoc.ub.uni-muenchen.de/archive/00006312.

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Yue, Kevin Kin Man. "Assembly of outer membrane proteins in Escherichia coli." Thesis, University of Liverpool, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.257436.

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Crago, Aimee Marie. "Virulence-related outer membrane proteins of Salmonella typhimurium." Thesis, University of Cambridge, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.624399.

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Books on the topic "Outer membrane proteins"

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Sun, Frank. Identification of Porphyromonas (Bacteroides) Gingivalis outer membrane proteins that bind to and degrade human matrix proteins. [Toronto: Faculty of Dentistry, University of Toronto, 1992.

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Mortimer, Peter G. S. The role of Esherichia coli outer membrane proteins in determining the accumulation of and susceptibility to antibiotics. Birmingham: University of Birmingham, 1991.

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Maciver, Isobel. The effect of haem limitation and iron restriction on outer membrane proteins and on respiratory systems of non typable Haemophilus influenzae. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1989.

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Characterization of the maltose regulon of Vibrio cholerae: Involvement of maltose in production of outer membrane proteins and secretion of virulence factors. Uppsala: Swedish University of Agricultural Sciences, Dept. of Molecular Genetics, Uppsala Genetic Center, 1993.

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Shand, Geoffrey Harold. Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginasa. Birmingham: University of Aston. Department of Pharmaceutical Sciences, 1985.

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Kraak, Wilma A. G. Outer membrane protein typing of Haemophilus influenzae: An epidemiological tool in type b and non-encapsulated strains. Oxford: Oxford Polytechnic, 1990.

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The Periplasm. ASM Press, 2006.

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Bacterial and eukaryotic porins: Structure, function, mechanism. Weinheim [Germany]: Wiley-VCH, 2004.

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Bacterial and Eukaryotic Porins: Structure, Function, Mechanism. Wiley-VCH, 2004.

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Lennon, Rachel, and Neil Turner. The molecular basis of glomerular basement membrane disorders. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0320_update_001.

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The glomerular basement membrane (GBM) is a condensed network of extracellular matrix molecules which provides a scaffold and niche to support the function of the overlying glomerular cells. Within the glomerulus, the GBM separates the fenestrated endothelial cells, which line capillary walls from the epithelial cells or podocytes, which cover the outer aspect of the capillaries. In common with basement membranes throughout the body, the GBM contains core components including collagen IV, laminins, nidogens, and heparan sulphate proteoglycans. However, specific isoforms of these proteins are required to maintain the integrity of the glomerular filtration barrier.Across the spectrum of glomerular disease there is alteration in glomerular extracellular matrix (ECM) and a number of histological patterns are recognized. The GBM can be thickened, expanded, split, and irregular; the mesangial matrix may be expanded and glomerulosclerosis represents a widespread accumulation of ECM proteins associated with loss of glomerular function. Whilst histological patterns may follow a sequence or provide diagnostic clues, there remains limited understanding about the mechanisms of ECM regulation and how this tight control is lost in glomerular disease. Monogenic disorders of the GBM including Alport and Pierson syndromes have highlighted the importance of both collagen IV and laminin isoforms and these observations provide important insights into mechanisms of glomerular disease.
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Book chapters on the topic "Outer membrane proteins"

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Mirus, Oliver, Alexander Hahn, and Enrico Schleiff. "Outer Membrane Proteins." In Prokaryotic Cell Wall Compounds, 175–228. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-05062-6_6.

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Hancock, Robert E. W., and Elizabeth A. Worobec. "Outer Membrane Proteins." In Pseudomonas, 139–67. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-0120-0_5.

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Lugtenberg, Ben J. J. "Outer Membrane Proteins." In The Rhizobiaceae, 45–53. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-5060-6_3.

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Nanda, Vikas, Daniel Hsieh, and Alexander Davis. "Prediction and Design of Outer Membrane Protein–Protein Interactions." In Membrane Proteins, 183–96. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-583-5_10.

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Tommassen, Jan, and Romé Voulhoux. "Biogenesis of Outer Membrane Proteins." In Protein Secretion Pathways in Bacteria, 83–97. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0095-6_5.

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Owen, Peter, Patrick Caffrey, Lars-Goran Josefsson, and Mary Meehan. "Outer Membrane Proteins: Old and New." In Microbial Surface Components and Toxins in Relation to Pathogenesis, 127–39. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-8995-8_15.

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Derrick, Jeremy, John E. Heckels, and Mumtaz Virji. "Major Outer Membrane Proteins of Meningococci." In Handbook of Meningococcal Disease, 181–215. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527608508.ch10.

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Heckels, John E. "Outer membrane proteins and IgA protease." In Gonococci and Meningococci, 343–44. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1383-7_55.

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Grijpstra, Jan, Martine P. Bos, and Jan Tommassen. "Assembly of Bacterial Outer Membrane Proteins." In Methods in Molecular Biology, 223–37. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-245-2_14.

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van der Helm, Dick. "Structure of Outer Membrane Receptor Proteins." In Iron Transport in Bacteria, 49–65. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555816544.ch4.

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Conference papers on the topic "Outer membrane proteins"

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Soares, T. A., T. P. Straatsma, Theodore E. Simos, and George Maroulis. "Towards Simulations of Outer Membrane Proteins in Lipopolysaccharide Membranes." In COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836008.

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She, Rong, Fei Chen, Ke Wang, Martin Ester, Jennifer L. Gardy, and Fiona S. L. Brinkman. "Frequent-subsequence-based prediction of outer membrane proteins." In the ninth ACM SIGKDD international conference. New York, New York, USA: ACM Press, 2003. http://dx.doi.org/10.1145/956750.956800.

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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins are associated with the cytoplasmic face of the plasma membrane and probably interact with transmembrane glycoproteins. We have raised monoclonal antibodies to the purified plasma membrane preparation in order to investigate the nature of these glycoprotein-cytoskeletal interactions. In two fusion experiments, out of 804 tested, 104 hybrids secreted antibody to the membrane preparation and of these 24 were selected for further study. Initial assays were by ELISA using either the membrane preparation or whole fixed platelets as the target antigen. The specificity of the antibodies was investigated further by immunoblotting of SDS gels of total platelet proteins prepared under reducing and nonreducing conditions, by immunofluorescence, by immunohisto-chemistry and by crossed immunoelectrophoresis. The majority of the antibodies recognise major surface glycoproteins; of these, four bind to glycoprotein Ib under all conditions examined while another seven recognise the glycoprotein IIb/IIIa complex as detected by crossed immunoelectrophoresis. Three antibodies recognise the actin binding protein and these cross-react with the smooth muscle protein filamin in a number of different species. Further characterisation of these antibodies in both structural and functional terms will be presented.We are grateful to the Smith and Nephew Foundation for financial support for these studies
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Wang, Zhijun, Qiangyan Pan, Lifeng Yang, Chunyan Xu, Feng Yu, Liang Li, and Jianhua He. "Recognition of outer membrane proteins using adaptive neuro-fuzzy inference systems." In 2014 11th International Conference on Fuzzy Systems and Knowledge Discovery (FSKD). IEEE, 2014. http://dx.doi.org/10.1109/fskd.2014.6980843.

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Zou, Lingyun, Qingshan Ni, and Fuquan Hu. "EBGW_OMP: A sequence-based method for accurate prediction of outer membrane proteins." In 2014 IEEE Conference on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2014. http://dx.doi.org/10.1109/cibcb.2014.6845502.

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Ying-xue Qin and Qing-pi Yan. "The antigenicity of the flagellin, outer membrane proteins and lipopolysaccharide of Vibrio harveyi." In 2010 International Conference on Bioinformatics and Biomedical Technology. IEEE, 2010. http://dx.doi.org/10.1109/icbbt.2010.5478956.

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Ju, Wen, and H. D. Cheng. "Discrimination of Outer Membrane Proteins using Reformulated Support Vector Machine based on Neutrosophic Set." In 11th Joint Conference on Information Sciences. Paris, France: Atlantis Press, 2008. http://dx.doi.org/10.2991/jcis.2008.77.

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Unitt, A., C. Rodrigues, J. Bray, K. Jolley, C. Tang, M. Maiden, and O. Harrison. "O09.6 Typing outer membrane vesicle proteins of Neisseria gonorrhoeae provides insight into antimicrobial resistance." In Abstracts for the STI & HIV World Congress, July 14–17 2021. BMJ Publishing Group Ltd, 2021. http://dx.doi.org/10.1136/sextrans-2021-sti.103.

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Marjuki, Henju, Nadav Topaz, Sandeep Joseph, Kim Gernert, Ellen Kersh, and Xin Wang. "O01.1 Genetic similarity of gonococcal homologs to meningococcal outer membrane proteins of serogroup B vaccine." In Abstracts for the STI & HIV World Congress (Joint Meeting of the 23rd ISSTDR and 20th IUSTI), July 14–17, 2019, Vancouver, Canada. BMJ Publishing Group Ltd, 2019. http://dx.doi.org/10.1136/sextrans-2019-sti.104.

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Fontes, Silvia, Thais Araujo, Fernando Conte, Patrícia Neves, Rodrigo Silva, Tatiana Rozental, and Elba Lemos. "In silico studies of Coxiella burnetii outer membrane proteins (OMPs) as basis to Q fever diagnosis development." In IV International Symposium on Immunobiologicals & VII Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2019. http://dx.doi.org/10.35259/isi.sact.2019_32727.

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Reports on the topic "Outer membrane proteins"

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Dunn, Bruce E., Martin J. Blaser, and Edward L. Snyder. Two-Dimensional Gel Electrophoresis and Immunoblotting of Campylobacter Outer Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, April 1987. http://dx.doi.org/10.21236/ada265461.

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Blaser, Martin J. Studies of the Outer Membrane Proteins of Campylobacter Jejuni for Vaccine Development. Fort Belvoir, VA: Defense Technical Information Center, November 1991. http://dx.doi.org/10.21236/ada245442.

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Palmer, Guy H., Eugene Pipano, Terry F. McElwain, Varda Shkap, and Donald P. Knowles, Jr. Development of a Multivalent ISCOM Vaccine against Anaplasmosis. United States Department of Agriculture, July 1993. http://dx.doi.org/10.32747/1993.7568763.bard.

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Anaplasmosis is an arthropod+borne disease of cattle caused by the rickettsia Anaplasma marginale and an impediment to efficient production of healthy livestock in both Israel and the United States. Our research focuses on development of a recombinant membrane surface protein (MSP) immunogen to replace current vaccines derived from the blood of infected cattle. The risk of widespread transmission of both known and newly emergent pathogens has prevented licensure of live blood-based vaccines in the U.S. and is a major concern for their continued use in Israel. Briefly, we accomplished the following in our BARD supported research: i) characterization of the intramolecular and intermolecular relationships of the native Major Surface Proteins (MSP) in the outer membrane; ii) expression, purification, and epitope characterization of the recombinant MSP-2, MSP-3, MSP-4, and MSP-5 proteins required to construct the recombinant ISCOM; iii) demonstration that the outer membrane-Quil A induces CD4+ T lymphocytes specific for the outer membrane polypeptides; iv) identification of CD4+ T lymphocytes that recognize outer membrane polypeptide epitopes conserved among other wise antigenically distinct strains; v) determination that immunization with the outer membrane-Quil A construct does not affect the ability of ticks to acquire or transmit A. marginale; and vi) demonstration that the outer membrane-Quil A construct induces complete protection against rickettsemia upon homologous challenge and significant protection against challenge with antigenically distinct strains, including tick transmission. Importantly, the level of protection against homologous challenge in the MSP vaccinates was comparable to that induced by live blood-based vaccines and demonstrates that development of a new generation of vaccines is feasible.
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4

Elbaum, Michael, and Peter J. Christie. Type IV Secretion System of Agrobacterium tumefaciens: Components and Structures. United States Department of Agriculture, March 2013. http://dx.doi.org/10.32747/2013.7699848.bard.

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Objectives: The overall goal of the project was to build an ultrastructural model of the Agrobacterium tumefaciens type IV secretion system (T4SS) based on electron microscopy, genetics, and immunolocalization of its components. There were four original aims: Aim 1: Define the contributions of contact-dependent and -independent plant signals to formation of novel morphological changes at the A. tumefaciens polar membrane. Aim 2: Genetic basis for morphological changes at the A. tumefaciens polar membrane. Aim 3: Immuno-localization of VirB proteins Aim 4: Structural definition of the substrate translocation route. There were no major revisions to the aims, and the work focused on the above questions. Background: Agrobacterium presents a unique example of inter-kingdom gene transfer. The process involves cell to cell transfer of both protein and DNA substrates via a contact-dependent mechanism akin to bacterial conjugation. Transfer is mediated by a T4SS. Intensive study of the Agrobacterium T4SS has made it an archetypal model for the genetics and biochemistry. The channel is assembled from eleven protein components encoded on the B operon in the virulence region of the tumor-inducing plasmid, plus an additional coupling protein, VirD4. During the course of our project two structural studies were published presenting X-ray crystallography and three-dimensional reconstruction from electron microscopy of a core complex of the channel assembled in vitro from homologous proteins of E. coli, representing VirB7, VirB9, and VirB10. Another study was published claiming that the secretion channels in Agrobacterium appear on helical arrays around the membrane perimeter and along the entire length of the bacterium. Helical arrangements in bacterial membranes have since fallen from favor however, and that finding was partially retracted in a second publication. Overall, the localization of the T4SS within the bacterial membranes remains enigmatic in the literature, and we believe that our results from this project make a significant advance. Summary of achievements : We found that polar inflations and other membrane disturbances relate to the activation conditions rather than to virulence protein expression. Activation requires low pH and nutrient-poor medium. These stress conditions are also reflected in DNA condensation to varying degrees. Nonetheless, they must be considered in modeling the T4SS as they represent the relevant conditions for its expression and activity. We identified the T4SS core component VirB7 at native expression levels using state of the art super-resolution light microscopy. This marker of the secretion system was found almost exclusively at the cell poles, and typically one pole. Immuno-electron microscopy identified the protein at the inner membrane, rather than at bridges across the inner and outer membranes. This suggests a rare or transient assembly of the secretion-competent channel, or alternatively a two-step secretion involving an intermediate step in the periplasmic space. We followed the expression of the major secreted effector, VirE2. This is a single-stranded DNA binding protein that forms a capsid around the transferred oligonucleotide, adapting the bacterial conjugation to the eukaryotic host. We found that over-expressed VirE2 forms filamentous complexes in the bacterial cytoplasm that could be observed both by conventional fluorescence microscopy and by correlative electron cryo-tomography. Using a non-retentive mutant we observed secretion of VirE2 from bacterial poles. We labeled the secreted substrates in vivo in order detect their secretion and appearance in the plant cells. However the low transfer efficiency and significant background signal have so far hampered this approach.
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Brayton, Kelly A., Varda Shkap, Guy H. Palmer, Wendy C. Brown, and Thea Molad. Control of Bovine Anaplasmosis: Protective Capacity of the MSP2 Allelic Repertoire. United States Department of Agriculture, January 2014. http://dx.doi.org/10.32747/2014.7699838.bard.

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Anaplasmosis is an arthropod-borne disease of cattle caused by the rickettsia Anaplasmamarginale and is an impediment to efficient production of healthy livestock in both Israel and the United States. Currently, the only effective vaccines are derived from the blood of infected cattle. The risk of widespread transmission of both known and newly emergent pathogens has prevented licensure of live blood-based vaccines in the U.S. and is a major concern for their continued use in Israel. Consequently, development of a safe, effective vaccine is a high priority. Despite its drawbacks as a live, blood-based vaccine, the Israel vaccine strain protects against disease upon challenge with wild-type A. marginale in extensive experimental trials and during 50 years of deployment in Israel. Field studies in Australia and Argentina indicate that this protection is broadly effective. Thus, to identify antigens for development of a safe and effective recombinant vaccine, we have used a comparative genomics approach by sequencing the Israel vaccine strain and searching for shared surface antigens with sequenced wild-type U.S. strains. We have focused on Msp2, the immune-dominant but antigenically variable surface protein, based on shared structure among strains and demonstration that antibody from cattle immunized with the Israel vaccine strain binds Msp2 from the genetically and geographically distinct U.S. St. Maries strain, consistent with the ability to protect against St. Maries challenge. Importantly, we have defined the full repertoire of Msp2 simple variants encoded by the vaccine strain and hypothesize that a recombinant vaccine encoding this full repertoire will induce protection equivalent to that induced by the live vaccine strain. Any escape from immunity by generation of complex Msp2 variants is predicted to carry a severe fitness cost that prevents high-level bacteremia and disease— consistent with the type of protection induced by the live vaccine strain. We tested the hypothesis that the Msp2 simple variant repertoires in wild-type A. marginale strains are recognized by antibody from cattle immunized with the Israel vaccine strain and that immunization with the vaccine strain Msp2 repertoire can recapitulate the protection provided by the vaccine strain upon challenge with Israel and U.S. strains of A. marginale. Our findings demonstrate that a set of conserved outer membrane proteins are recognized by immune serum from A. centrale vaccinated animals but that this set of proteins does not include Msp2. These findings suggest that “subdominant” immunogens are required for vaccine induced protection.
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6

Walian, P. J. Electron crystallography of PhoE porin, an outer membrane, channel- forming protein from E. coli. Office of Scientific and Technical Information (OSTI), November 1989. http://dx.doi.org/10.2172/6365889.

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7

Eldar, Avigdor, and Donald L. Evans. Streptococcus iniae Infections in Trout and Tilapia: Host-Pathogen Interactions, the Immune Response Toward the Pathogen and Vaccine Formulation. United States Department of Agriculture, December 2000. http://dx.doi.org/10.32747/2000.7575286.bard.

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In Israel and in the U.S., Streptococcus iniae is responsible for considerable losses in various fish species. Poor understanding of its virulence factors and limited know-how-to of vaccine formulation and administration are the main reasons for the limited efficacy of vaccines. Our strategy was that in order to Improve control measures, both aspects should be equally addressed. Our proposal included the following objectives: (i) construction of host-pathogen interaction models; (ii) characterization of virulence factors and immunodominant antigens, with assessment of their relative importance in terms of protection and (iii) genetic identification of virulence factors and genes, with evaluation of the protective effect of recombinant proteins. We have shown that two different serotypes are involved. Their capsular polysaccharides (CPS) were characterized, and proved to play an important role in immune evasion and in other consequences of the infection. This is an innovative finding in fish bacteriology and resembles what, in other fields, has become apparent in the recent years: S. iniae alters surface antigens. By so doing, the pathogen escapes immune destruction. Immunological assays (agar-gel immunodiffusion and antibody titers) confirmed that only limited cross recognition between the two types occurs and that capsular polysaccharides are immunodominant. Vaccination with purified CPS (as an acellular vaccine) results in protection. In vitro and ex-vivo models have allowed us to unravel additional insights of the host-pathogen interactions. S. iniae 173 (type II) produced DNA fragmentation of TMB-8 cells characteristic of cellular necrosis; the same isolate also prevented the development of apoptosis in NCC. This was determined by finding reduced expression of phosphotidylserine (PS) on the outer membrane leaflet of NCC. NCC treated with this isolate had very high levels of cellular necrosis compared to all other isolates. This cellular pathology was confirmed by observing reduced DNA laddering in these same treated cells. Transmission EM also showed characteristic necrotic cellular changes in treated cells. To determine if the (in vitro) PCD/apoptosis protective effects of #173 correlated with any in vivo activity, tilapia were injected IV with #173 and #164 (an Israeli type I strain). Following injection, purified NCC were tested (in vitro) for cytotoxicity against HL-60 target cells. Four significant observations were made : (i) fish injected with #173 had 100-400% increased cytotoxicity compared to #164 (ii) in vivo activation occurred within 5 minutes of injection; (iii) activation occurred only within the peripheral blood compartment; and (iv) the isolate that protected NCC from apoptosis in vitro caused in vivo activation of cytotoxicity. The levels of in vivo cytotoxicity responses are associated with certain pathogens (pathogen associated molecular patterns/PAMP) and with the tissue of origin of NCC. NCC from different tissue (i.e. PBL, anterior kidney, spleen) exist in different states of differentiation. Random amplified polymorphic DNA (RAPD) analysis revealed the "adaptation" of the bacterium to the vaccinated environment, suggesting a "Darwinian-like" evolution of any bacterium. Due to the selective pressure which has occurred in the vaccinated environment, type II strains, able to evade the protective response elicited by the vaccine, have evolved from type I strains. The increased virulence through the appropriation of a novel antigenic composition conforms with pathogenic mechanisms described for other streptococci. Vaccine efficacy was improved: water-in-oil formulations were found effective in inducing protection that lasted for a period of (at least) 6 months. Protection was evaluated by functional tests - the protective effect, and immunological parameters - elicitation of T- and B-cells proliferation. Vaccinated fish were found to be resistant to the disease for (at least) six months; protection was accompanied by activation of the cellular and the humoral branches.
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8

Splitter, Gary, and Menachem Banai. Microarray Analysis of Brucella melitensis Pathogenesis. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7709884.bard.

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Original Objectives 1. To determine the Brucella genes that lead to chronic macrophage infection. 2. To identify Brucella genes that contribute to infection. 3. To confirm the importance of Brucella genes in macrophages and placental cells by mutational analysis. Background Brucella spp. is a Gram-negative facultative intracellular bacterium that infects ruminants causing abortion or birth of severely debilitated animals. Brucellosis continues in Israel, caused by B. melitensis despite an intensive eradication campaign. Problems with the Rev1 vaccine emphasize the need for a greater understanding of Brucella pathogenesis that could improve vaccine designs. Virulent Brucella has developed a successful strategy for survival in its host and transmission to other hosts. To invade the host, virulent Brucella establishes an intracellular niche within macrophages avoiding macrophage killing, ensuring its long-term survival. Then, to exit the host, Brucella uses placenta where it replicates to high numbers resulting in abortion. Also, Brucella traffics to the mammary gland where it is secreted in milk. Missing from our understanding of brucellosis is the surprisingly lillie basic information detailing the mechanisms that permit bacterial persistence in infected macrophages (chronic infection) and dissemination to other animals from infected placental cells and milk (acute infection). Microarray analysis is a powerful approach to determine global gene expression in bacteria. The close genomic similarities of Brucella species and our recent comparative genomic studies of Brucella species using our B. melitensis microarray, suqqests that the data obtained from studying B. melitensis 16M would enable understanding the pathogenicity of other Brucella organisms, particularly the diverse B. melitensis variants that confound Brucella eradication in Israel. Conclusions Results from our BARD studies have identified previously unknown mechanisms of Brucella melitensis pathogenesis- i.e., response to blue light, quorum sensing, second messenger signaling by cyclic di-GMP, the importance of genomic island 2 for lipopolysaccharide in the outer bacterial membrane, and the role of a TIR domain containing protein that mimics a host intracellular signaling molecule. Each one of these pathogenic mechanisms offers major steps in our understanding of Brucella pathogenesis. Strikingly, our molecular results have correlated well to the pathognomonic profile of the disease. We have shown that infected cattle do not elicit antibodies to the organisms at the onset of infection, in correlation to the stealth pathogenesis shown by a molecular approach. Moreover, our field studies have shown that Brucella exploit this time frame to transmit in nature by synchronizing their life cycle to the gestation cycle of their host succumbing to abortion in the last trimester of pregnancy that spreads massive numbers of organisms in the environment. Knowing the bacterial mechanisms that contribute to the virulence of Brucella in its host has initiated the agricultural opportunities for developing new vaccines and diagnostic assays as well as improving control and eradication campaigns based on herd management and linking diagnosis to the pregnancy status of the animals. Scientific and Agricultural Implications Our BARD funded studies have revealed important Brucella virulence mechanisms of pathogenesis. Our publication in Science has identified a highly novel concept where Brucella utilizes blue light to increase its virulence similar to some plant bacterial pathogens. Further, our studies have revealed bacterial second messengers that regulate virulence, quorum sensing mechanisms permitting bacteria to evaluate their environment, and a genomic island that controls synthesis of its lipopolysaccharide surface. Discussions are ongoing with a vaccine company for application of this genomic island knowledge in a Brucella vaccine by the U.S. lab. Also, our new technology of bioengineering bioluminescent Brucella has resulted in a spin-off application for diagnosis of Brucella infected animals by the Israeli lab by prioritizing bacterial diagnosis over serological diagnosis.
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