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Relevant bibliographies by topics / Outer membrane protein

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Academic literature on the topic 'Outer membrane protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 March 2023

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Journal articles on the topic "Outer membrane protein"

1

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 d

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2

Ishikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh та Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly". Journal of Cell Biology 166, № 5 (23 серпня 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

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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

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4

Dhar, Rik, and Joanna SG Slusky. "Outer membrane protein evolution." Current Opinion in Structural Biology 68 (June 2021): 122–28. http://dx.doi.org/10.1016/j.sbi.2021.01.002.

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Slusky, Joanna SG. "Outer membrane protein design." Current Opinion in Structural Biology 45 (August 2017): 45–52. http://dx.doi.org/10.1016/j.sbi.2016.11.003.

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Murcha, Monika W., Dina Elhafez, A. Harvey Millar, and James Whelan. "The C-terminal Region of TIM17 Links the Outer and Inner Mitochondrial Membranes inArabidopsisand Is Essential for Protein Import." Journal of Biological Chemistry 280, no. 16 (February 18, 2005): 16476–83. http://dx.doi.org/10.1074/jbc.m413299200.

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The translocase of the inner membrane 17 (AtTIM17-2) protein fromArabidopsishas been shown to link the outer and inner mitochondrial membranes. This was demonstrated by several approaches: (i)In vitroorganelle import assays indicated the importedAtTIM17-2 protein remained protease accessible in the outer membrane when inserted into the inner membrane. (ii) N-terminal and C-terminal tagging indicated that it was the C-terminal region that was located in the outer membrane. (iii) Antibodies raised to the C-terminal 100 amino acids recognize a 31-kDa protein from purified mitochondria, but cross-

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Hoffmann, Juliane J., and Thomas Becker. "Crosstalk between Mitochondrial Protein Import and Lipids." International Journal of Molecular Sciences 23, no. 9 (May 9, 2022): 5274. http://dx.doi.org/10.3390/ijms23095274.

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Mitochondria import about 1000 precursor proteins from the cytosol. The translocase of the outer membrane (TOM complex) forms the major entry site for precursor proteins. Subsequently, membrane-bound protein translocases sort the precursor proteins into the outer and inner membrane, the intermembrane space, and the matrix. The phospholipid composition of mitochondrial membranes is critical for protein import. Structural and biochemical data revealed that phospholipids affect the stability and activity of mitochondrial protein translocases. Integration of proteins into the target membrane invol

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Court, Deborah A., Roland Lill, and Walter Neupert. "The protein import apparatus of the mitochondrial outer membrane." Canadian Journal of Botany 73, S1 (December 31, 1995): 193–97. http://dx.doi.org/10.1139/b95-245.

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The majority of proteins within mitochondria are synthesized on cytosolic ribosomes and imported into the organelles. Protein complexes in the mitochondrial outer membrane harbour both the receptors that recognize these preproteins, and a translocation pore. These "receptor complexes" are the entry points for most preproteins, which are subsequently targeted to their final submitochondrial locations. The outer membrane complexes cooperate with the import machinery of the inner membrane to target preproteins to the inner membrane itself, the matrix, or, in some cases, to the intermembrane space

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Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. "Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins." Journal of Cell Biology 109, no. 6 (December 1, 1989): 2603–16. http://dx.doi.org/10.1083/jcb.109.6.2603.

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To identify the membrane regions through which yeast mitochondria import proteins from the cytoplasm, we have tagged these regions with two different partly translocated precursor proteins. One of these was bound to the mitochondrial surface of ATP-depleted mitochondria and could subsequently be chased into mitochondria upon addition of ATP. The other intermediate was irreversibly stuck across both mitochondrial membranes at protein import sites. Upon subfraction of the mitochondria, both intermediates cofractionated with membrane vesicles whose buoyant density was between that of inner and ou

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Braun, Volkmar. "The Outer Membrane Took Center Stage." Annual Review of Microbiology 72, no. 1 (September 8, 2018): 1–24. http://dx.doi.org/10.1146/annurev-micro-090817-062156.

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My interest in membranes was piqued during a lecture series given by one of the founders of molecular biology, Max Delbrück, at Caltech, where I spent a postdoctoral year to learn more about protein chemistry. That general interest was further refined to my ultimate research focal point—the outer membrane of Escherichia coli—through the influence of the work of Wolfhard Weidel, who discovered the murein (peptidoglycan) layer and biochemically characterized the first phage receptors of this bacterium. The discovery of lipoprotein bound to murein was completely unexpected and demonstrated that t

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Dissertations / Theses on the topic "Outer membrane protein"

1

Barlow, Ann Katherine. "Neisseria meningitidis : the class 1 outer membrane protein." Thesis, University of Southampton, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.280415.

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McBride, Heidi May. "Protein import into and across the mitochondrial outer membrane." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40395.

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Protein import into the mitochondria is a result of a series of sequential binding interactions between a mitochondrial targeting signal and the translocation machinery of both mitochondrial membranes. The targeting signals contained within protein of the outer membrane are distinct from those which target proteins to other subcompartments. The transmembrane domain of the yeast outer membrane receptor protein yTom70 is capable of both targeting and inserting the protein into the outer membrane. The efficiency of this process is increased by the addition of a positively-charged region preceding

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See, Sarah Bihui. "Outer membrane protein immunity to Pasteurella pneumotropica and the interaction of allergy." University of Western Australia. School of Paediatrics and Child Health, 2010. http://theses.library.uwa.edu.au/adt-WU2010.0103.

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[Truncated abstract] Infectious and allergic diseases of the respiratory tract are major contributors to global mortality, morbidity and economic burden. Bacterial infections such as pneumonia and otitis media are important diseases, especially in children, while allergic diseases such as asthma and allergic rhinitis afflict up to 30% of the world's population. A confounding aspect of respiratory disease is the evidence of a complex relationship between respiratory allergy and respiratory infection, with infection suggested to both promote and prevent the pathogenesis of allergic disease. Addi

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Juodeikis, Rokas. "Engineering membranes in Escherichia coli : the magnetosome, LemA protein family and outer membrane vesicles." Thesis, University of Kent, 2016. https://kar.kent.ac.uk/61062/.

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Magnetosomes are membranous organelles found in magnetotactic bacteria (MTB). The organelle consist of ferromagnetic crystals housed within a lipid bilayer chained together by an actin-like filament and allows MTB to orient within magnetic fields. The genetic information required to produce these organelles has been linked to four different operons, encoding for 30 genes. These membranous organelles and the magnetic minerals housed within have various biotechnological applications, therefore enhanced recombinant production of such structures in a model organism holds significant potential. The

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Menon, Sailesh. "Characterization of a Fusobacterium necrophorum subspecies necrophorum outer membrane protein." Kansas State University, 2014. http://hdl.handle.net/2097/18128.

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Master of Science<br>Department of Biomedical Sciences<br>Sanjeev K. Narayanan<br>Fusobacterium necrophorum is an anaerobic Gram-negative non spore forming rod shaped bacteria that is a normal inhabitant of the alimentary tract of humans and animals. Two subspecies of F. necrophorum have been recognized- subspecies necrophorum and subspecies funduliforme. Subspecies necrophorum is an opportunistic pathogen in animals causing diseases such as bovine hepatic abscesses and sheep foot rot while as subspecies funduliforme is linked with human oral and hepatic infections such as sore throats, Lemier

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Shand, Geoffrey H. "Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginosa." Thesis, Aston University, 1985. http://publications.aston.ac.uk/12475/.

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Kaye, Elena Cortizas. "The Function of Outer Membrane Protein A (OmpA) in Yersinia pestis." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_theses/58.

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The outer membrane protein OmpA is one of the major outer membrane proteins in many species of bacteria, including the Yersiniae. Our goal was to explore the role of OmpA in Y. pestis. This encompasses the ability of Yersinia to infect and survive within macrophages, as well as to resist antimicrobial compounds. Our laboratory found that a delta ompA mutant is impaired in a macrophage-associated infectivity assay. We also found that OmpA might play a role in the ability of the bacteria to resist antimicrobial peptides, specifically polymyxin B. Aditionally, we assessed the differences in OmpA

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Ferris, Shirley. "Antibody responses to the major outer membrane protein of Chlamydia trachomatis." Thesis, University of Southampton, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295880.

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Schiffrin, Robert. "Roles of periplasmic chaperones and BamA in outer membrane protein folding." Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15952/.

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A defining feature of living things is that they have an inside and an outside, and in order for all living cells to survive, whether they are part of a blue whale or a unicellular microscopic organism, they must have mechanisms to mediate exchange with their environment. Food and energy enters the cell, and material must also leave, such as the waste products of metabolism, or virulence factors from pathogenic organisms. Lipid membranes define these boundaries, but it is membrane proteins that mediate the exchange. Although lipid bilayers can self-assemble in vitro, the assembly of complex bi

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Huysmans, Gerard Herman Marleen. "On the folding mechanism of the bacterial outer membrane protein PagP." Thesis, University of Leeds, 2008. http://etheses.whiterose.ac.uk/6752/.

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Membrane proteins represent an important class of macromolecules that play critical roles in many biological processes. The energetic principles underlying their stability, however, are not well understood. To address this deficiency, the kinetics and thermodynamics of the folding of the Escherichia coli outer membrane protein PagP were investigated by exploiting the ability of this polypeptide to refold into detergent micelles and into artificial lipid membranes. Investigations using the latter enabled the contributions to the folding process of both the protein sequence and of the bilayer li

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Books on the topic "Outer membrane protein"

1

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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2

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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3

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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4

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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5

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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6

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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7

Kania, Stephen Anthony. Isolation and characterization of a 78,000 dalton outer membrane protein of Haemophilus somnus. 1987.

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8

The 2.05 Å crystal structure of LptB, an essential protein in gram-negative bacterial outer membrane biogenesis. 2011.

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9

Structural and Functional Relationships in Prokaryotes. Springer, 2004.

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Barton, Larry L. Structural and Functional Relationships in Prokaryotes. Springer London, Limited, 2005.

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Book chapters on the topic "Outer membrane protein"

1

Poolman, J. "Outer Membrane Protein Vaccines." In Vaccines, 225–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59955-2_9.

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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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Poolman, Jan T. "Bacterial Outer Membrane Protein Vaccines." In Advances in Experimental Medicine and Biology, 73–77. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-1382-1_11.

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Cecil, Jessica D., Natalie Sirisaengtaksin, NEIL M. O'BRIEN-SIMPSON, and Anne Marie Krachler. "Outer Membrane Vesicle-Host Cell Interactions." In Protein Secretion in Bacteria, 201–14. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch17.

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Millar, D. G., and G. C. Shore. "Protein Insertion Into The Outer Mitochondrial Membrane." In Molecular Mechanisms of Membrane Traffic, 105–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_21.

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Grabowicz, Marcin. "Lipoproteins and Their Trafficking to the Outer Membrane." In Protein Secretion in Bacteria, 67–76. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch6.

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Tu, Shuh-Long, and Hsou-min Li. "Protein Targeting to the Chloroplast Outer Membrane." In Photosynthesis: Mechanisms and Effects, 3069–73. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_719.

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Heckels, J. E., M. Virji, K. Zak, and J. N. Fletcher. "Immunobiology of gonococcal outer membrane protein I." In Gonococci and Meningococci, 369–71. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1383-7_60.

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Ricci, Dante P., and Thomas J. Silhavy. "Outer Membrane Protein Insertion by the β-barrel Assembly Machine." In Protein Secretion in Bacteria, 91–101. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch8.

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Conference papers on the topic "Outer membrane protein"

1

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

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Harasztosi, Csaba, Emese Harasztosi, and Anthony W. Gummer. "Membrane recycling at the infranuclear pole of the outer hair cell." In MECHANICS OF HEARING: PROTEIN TO PERCEPTION: Proceedings of the 12th International Workshop on the Mechanics of Hearing. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4939332.

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Pires, Inês, and Miguel Machuqueiro. "pH-dependent permeability of outer membrane protein G: an in silico study." In MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/mol2net-04-06077.

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Voigt, W., W. Rabsch, and H. Tschäpe. "Differences in the outer membrane protein pattern of Salmonella typhimurium DT8, DT10 and DT104 strains." In Fourth International Symposium on the Epidemiology and Control of Salmonella and Other Food Borne Pathogens in Pork. Iowa State University, Digital Press, 2001. http://dx.doi.org/10.31274/safepork-180809-201.

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Shen, Dandan, Anchun Cheng, and Mingshu Wang. "Analysis of synonymous codon usage in the outer membrane efflux protein gene of Riemerella anatipestifer." In 2012 5th International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2012. http://dx.doi.org/10.1109/bmei.2012.6513098.

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Handayani, Tri, Dadang Priyoatmojo, and Afi Candra Trinugraha. "Outer Membrane Protein (OMP) Profiles of Brucella abortus Local Isolate by SDS-PAGE Procedure." In International Conference on Improving Tropical Animal Production for Food Security (ITAPS 2021). Paris, France: Atlantis Press, 2022. http://dx.doi.org/10.2991/absr.k.220309.006.

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Salamon, Zdzislaw, Gordon Tollin, Angus Macleod, and Ian C. Stevenson. "Spectroscopic studies of membrane protein-lipid bilayer systems deposited on multilayer thin film coatings." In Optical Interference Coatings. Washington, D.C.: Optica Publishing Group, 1997. http://dx.doi.org/10.1364/oic.1998.thd.1.

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Although thin film coatings have been used for many years in optical investigations of biological systems (especially as narrow band light filters), more recent applications of such films in two types of spectroscopic devices, surface plasmon resonance (SPR) and optical waveguides, have provided new biophysical tools for the study of protein-protein and protein-lipid membrane interactions [1]. Although both of these techniques are based on different physical phenomena, the thin film coatings have the same function, i.e. coupling devices in which incident light, under the appropriate optical co

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McBride, S., M. Ferguson, M. Kelly, K. Hawley, A. Luthra, H. Driscoll, J. Montezuma-Rusca, et al. "P401 Development and Utilization of Antibodies Specific for Extracellular Loops of the Treponema pallidum outer membrane protein BamA (TP0326)." 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.431.

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"Evaluation of 36 KDa Outer Membrane Protein (OMP’s) by Latex Dri-dot of Salmonella Enterica Serovar Typhi For The Diagnosis Of Typhoid Fever." In April 17-18, 2018 Kyoto (Japan). International Institute of Chemical, Biological and Environmental Engineering, 2018. http://dx.doi.org/10.17758/iicbe1.c0418154.

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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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Reports on the topic "Outer membrane protein"

1

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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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 follo

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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

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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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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, blo

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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 understand

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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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Abstract:

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

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