Dissertations / Theses on the topic 'Outer membrane protein'
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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.
Full textMcBride, 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.
Full textConsistent with this model, the signal-anchor sequence of the outer membrane protein yTom70 is also capable of importing into the inner membrane of mitochondria when the outer membrane is selectively removed. Import into the inner membrane requires the presence of an electrochemical potential across the lipid bilayer. Import proceeds in the absence of $ Delta Psi$ only when constructs are used which lack the positively-charged amino terminal region of the signal-anchor sequence. These results suggest that the positively-charged presequence leads the transmembrane domain into the import machinery and that $ Delta Psi$ is required to clear this region in order that the distal transmembrane region can enter the translocation pathway.
The charged N-terminal 10 residues of yTom70 are incapable of directing import into intact mammalian mitochondria, however, are able to efficiently direct import into the matrix of yeast mitochondria or mammalian mitoplasts. This potentially cryptic signal is excluded from intact mammalian mitochondria due to the presence of the receptor protein Tom20, since replacement of yeast Tom20 with mammalian Tom20 confers the mammalian phenotype onto yeast. These results suggest that receptor proteins may also have the ability to screen potentially cryptic signals from distal components of the outer and inner membrane translocation machinery.
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.
Full textJuodeikis, 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/.
Full textMenon, Sailesh. "Characterization of a Fusobacterium necrophorum subspecies necrophorum outer membrane protein." Kansas State University, 2014. http://hdl.handle.net/2097/18128.
Full textDepartment of Biomedical Sciences
Sanjeev K. Narayanan
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, Lemierre’s syndrome and hepatic abscesses. The pathogenic mechanisms of F. necrophorum are complex and are not well understood or defined. Several virulence factors such as leukotoxin, haemolysin, haemagglutinin and adhesin have been described. One of the most important factors in F. necrophorum bacterial pathogenesis is the adhesion of the bacteria to the host cell. The adhesion of the bacteria to the host cell helps it colonize the host tissue and this is followed by intracellular multiplication with dissemination to other tissues, which could ultimately lead to septicemia and death. Bacteria use adhesins which are proteins found in the outer membrane which help them bind with host receptors and this helps with the adhesion of the bacteria to the host cell. Not much is known about F. necrophorum adhesins. Here, we describe and characterize a novel adhesin.
Shand, Geoffrey H. "Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginosa." Thesis, Aston University, 1985. http://publications.aston.ac.uk/12475/.
Full textKaye, Elena Cortizas. "The Function of Outer Membrane Protein A (OmpA) in Yersinia pestis." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_theses/58.
Full textFerris, 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.
Full textSchiffrin, Robert. "Roles of periplasmic chaperones and BamA in outer membrane protein folding." Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15952/.
Full textHuysmans, 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/.
Full textMorgan, Cecilia A. "Treponema pallidum repeat protein K and heterologous protection against syphilis /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/9300.
Full textOliveira-Fry, Anna Maria, and s9911120@student rmit edu au. "Identification of Legionella outer membrane proteins for the development of a biosensor." RMIT University. Applied Sciences, 2007. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080513.140744.
Full textWebb, Dianne, and n/a. "Nontypeable Haemophilus influenzae outer membrane protein analysis, isolation, characterisation and vaccine potential." University of Canberra. Applied Science, 1998. http://erl.canberra.edu.au./public/adt-AUC20061110.105953.
Full textArbing, Mark A. "Electrophysiological properties of porin, the major outer membrane protein of Haemophilus influenzae." Thesis, McGill University, 2002. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=38146.
Full textTo study the properties of the porin (341 amino acids; Mr 37,782) of Haemophilus influenzae type b (Hib), purified porin was subjected to chemical modification. The covalent modification of lysine residues with succinic anhydride (SA; Mr 100.08) results in charge reversal. The addition of up to 12 succinate groups per porin molecule was identified using electrospray ionization mass spectrometry (MS). Tryptic digestion of the modified Hib porin followed by reverse phase chromatography and matrix assisted laser desorption ionization time-of-flight MS identified the sites of succinylation. The majority of modified lysines were positioned in surface-located loops, numbers 1 and 4 to 7. When the electrophysiological properties of SA-modified porin were analyzed in planar lipid bilayers (PLBs) and compared to Hib porin it was found that the single channel conductance was increased, while the threshold for voltage gating was decreased. The addition of extra negative charges increase the single channel conductance of Hib porin and function as voltage sensors.
Selected lysine residues that were found to be modified with SA were substituted with glutamic acid using site-directed mutagenesis. Single point mutations were made in a residue assigned to the barrel lumen and to three residues in each of loops 4 and 6. The mutant Hib porins had increased single channel conductances relative to wild-type Hib porin. Voltage gating of mutant Hib porins was altered by the introduction of negative charges into loops 4 and 6 and in the barrel lumen. Previous experiments had implicated surface-exposed loop 4 in voltage gating. This study ascribes a role for residues in loop 6 and a residue within the barrel lumen in the changes that accompany pore closure.
Hi strains causing infection in cystic fibrosis patients are capable of persistent infection despite prolonged antibiotic treatment with beta-lactam antibiotics. During the course of infection porin properties may be altered due to the changes in porin sequences that are attributed to antigenic drift. The electrophysiological properties of four porins from CF patient-derived Hi strains were characterized to examine changes in porin properties arising from persistent infection of the CF lung. The clinical Hi porins displayed altered channel properties that included increased voltage sensitivity and single channel conductances that were either greater or smaller than that of Hib porin. The decreased single channel conductance of one of the porins was associated with an increase in the minimal inhibitory concentration of the antibiotics novobiocin and streptomycin. These results demonstrate a porin-mediated decrease in OM permeability as an antibiotic resistance mechanism for Hi.
Carter, Michael William. "The major outer membrane protein gene of Chlamydia as a phylogenetic chronometer." Thesis, University of Southampton, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.336071.
Full textEneroth, Elina, and Astrid Karlsson. "A role of Aggregatibacter actinomycetemcomitans Outer Membrane Protein 100 in Serum Resistance?" Thesis, Umeå universitet, Institutionen för odontologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-128759.
Full textRios, Rosa Elvira. "Characterisation of the physiological, chemical and pathogenic changes arising from the adaptation of Campylobacter jejuni to aerotolerant growth." Thesis, Manchester Metropolitan University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243715.
Full textDahan, David. "Biophysics of porin, the major outer membrane protein of Haemophilus influenzae type b." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0025/NQ29916.pdf.
Full textSrikumar, Ramakrishnan. "Topology of porin, the major outer membrane protein of Haemophilus influenzae type b." Thesis, McGill University, 1995. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40261.
Full textBased on parameters of hydrophilicity and amphiphilicity a model for Hib porin was generated. The model proposed an organization of sixteen anti-parallel $ beta$-strands that traverse the outer membrane, eight long loops that connect the $ beta$-strands on one side and short turns on the other side.
By flow cytometry, six out of a panel of nine monoclonal antibodies against Hib porin recognized amino acid sequences at the cell surface. Hib porin was purified and subjected to chemical and enzymatic digestions. The fragments were immunoblotted; N-terminal sequencing identified boundaries of fragments. C-terminal deletions of Hib porin generated in the baculovirus expression system identified C-terminal boundaries of monoclonal antibody reactivities.
To map precisely the primary sequences to which these monoclonal antibodies bound, overlapping hexapeptides for the entire sequence of Hib porin were synthesized. These studies identified two surface-exposed regions in the mature sequence of Hib porin, amino acid residues 162-172 and 318-325. In the Hib porin model, these regions correspond to loops 4 and 8, respectively. Two regions between residues 112-126 (loop 3) and residues 148-153 were buried or inaccessible at the surface of the outer membrane.
Recombinant Hib porin was expressed in Bacillus subtilis. The biophysical and immunological properties of this lipooligosaccharide-free recombinant Hib porin were compared with those of native Hib porin.
In order to examine the role of loop 3, site-directed mutagenesis of the cloned Hib porin gene was undertaken. Six or twelve amino acid deletions in loop 3, expressed in a porin deletion strain, showed significant increase in sensitivities to several anti-microbial agents as compared to wild-type Hib porin. Deletion of twelve amino acids showed more pronounced phenotypes than deletion of six amino acids. Such mutagenesis experiments provided support to the notion that loop 3 in Hib porin folds back into the pore and produces a constriction of the channel.
Dahan, David. "Biophysics of porin : the major outer membrane protein of Haemophilus influenzae type b." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=42009.
Full textBased on predictions of porin secondary structure, a model of Hib porin was generated. The model proposed sixteen membrane spanning $ beta$-strands connected by eight long loops on one side and eight short $ beta$-turns on the other side. To refine further this model, the epitopes of nine monoclonal antibodies specific for Hib porin were mapped precisely. Surface-exposure of these epitopes was determined by flow cytometry of intact Hib cells. Our studies identified two surface-exposed regions of Hib porin: amino acids 162 to 172, and 318 to 325. These two regions correspond to loops 4 and 8 in the Hib porin model.
Three naturally occurring Hib porin variants were purified, reconstituted into planar bilayers, and analyzed for their voltage dependency. Substitutions at Arg166 residue, which is localized to loop 4, were associated with a lowered threshold potential for the voltage gating of Hib porin. This surface-exposed loop was therefore implicated in the conformational changes that are postulated to occur during voltage gating.
Lipooligosaccharide (LOS) binds tightly to Hib porin. To generate large amounts of Hib porin devoid of LOS, the ompP2 gene was cloned into an expression vector of Bacillus subtilis. Recombinant Hib porin was produced in large quantities and it aggregated into inclusion bodies. Under denaturing conditions, recombinant porin was purified to homogeneity and subsequently refolded. To assess the fidelity of refolding of recombinant porin, four criteria were used: spectroscopic properties, channel formation in planar bilayers, resistance to trypsin digestion and formation of the conformational epitope recognized by monoclonal antibody Hb-2. We conclude that in the absence of LOS, recombinant porin was refolded into a functional form, its structure closely resembling the native state.
McCallan, Lyanne Mary. "Differentiation of Campylobacter jejuni on the basis of outer membrane protein (OMP) patterns." Thesis, University of Ulster, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422191.
Full textWard, Stephen John. "Characterisation and immunogenicity of recombinant class 1 outer membrane protein of Neisseria meningitidis." Thesis, University of Southampton, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296140.
Full textHuang, Shouxiong. "Genetic and Antigenic Characterization of the Major Outer Membrane Protein of Campylobacter Jejuni." The Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=osu1046991783.
Full textWyllie, Susan. "Structural and functional characterisation of the major outer membrane protein of Chlamydia psittaci." Thesis, University of Edinburgh, 1999. http://hdl.handle.net/1842/22762.
Full textYe, Cui. "STABILITY STUDIES OF MEMBRANE PROTEINS." UKnowledge, 2014. http://uknowledge.uky.edu/chemistry_etds/33.
Full textMuhammad, Noor [Verfasser]. "Insertion of Cecropin A and reconstitution of bacterial outer membrane protein FhuA variants in polymeric membranes / Noor Muhammad." Aachen : Hochschulbibliothek der Rheinisch-Westfälischen Technischen Hochschule Aachen, 2011. http://d-nb.info/1018204458/34.
Full textau, T. La@murdoch edu, and Tom La. "Characterisation, Recombinant Expression and Immunogenicity of BHLP29.7, An Outer Membrane Lipoprotein of Brachyspira Hyodysenteriae." Murdoch University, 2006. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20070830.141953.
Full textMcGuinness, Brian Timothy. "Immunochemistry and structural variation of the class 1 outer membrane protein of Neisseria meningitidis." Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386663.
Full textHumes, Julia Rose. "The mechanism of the ATP-independent periplasmic chaperone SurA in outer membrane protein biogenesis." Thesis, University of Leeds, 2018. http://etheses.whiterose.ac.uk/22526/.
Full textMcMorran, Lindsay Madeline. "Mechanisms of outer membrane protein folding : effects of the lipid environment and periplasmic chaperones." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/5906/.
Full textFischer, Steven Harold. "Interactions of Neisseria gonorrhoeae with human neutrophils: Gonococcal outer membrane protein II modulates neutrophil responses." Diss., The University of Arizona, 1988. http://hdl.handle.net/10150/184364.
Full textEaston, Donna Meredith, and n/a. "Functional and Antigenic Characterisation of the Moraxella catarrhalis protein M35." University of Canberra. n/a, 2008. http://erl.canberra.edu.au./public/adt-AUC20081217.083105.
Full textSukumaran, Suja. "Spectroscopic investigation of stability, unfolding and refolding of outer membrane protein porin from Paracoccus denitrificans." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=974953849.
Full textBell, Angus. "Structure, function, and role in antibiotic resistance of outer membrane protein H1 in Pseudomonas aeruginosa." Thesis, University of British Columbia, 1989. http://hdl.handle.net/2429/29008.
Full textScience, Faculty of
Microbiology and Immunology, Department of
Graduate
Berry, Jody Douglas. "Antibody gene markers and their relationship to chlamydial major outer membrane protein (MOMP) immune response." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0006/NQ41602.pdf.
Full textButt, Neil James. "The complete nucleotide sequence and immunochemistry of the major outer membrane protein of Neisseria gonorrhoeae." Thesis, University of Southampton, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.316059.
Full textBulieris, Paula Vasilichia. "Kinetic Studies on the Folding and Insertion of Outer Membrane Protein A from Escherichia Coli." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-48784.
Full textUjwal, Rachma. "Structural and fuctional characterization of the outer mitochondrial membrane protein voltage-dependent anion channel 1/." Diss., Restricted to subscribing institutions, 2009. http://proquest.umi.com/pqdweb?did=1930281371&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.
Full textKöniger, Verena [Verfasser], and Rainer [Akademischer Betreuer] Haas. "CEACAMs as novel receptors for Helicobacter pylori outer membrane protein HopQ / Verena Königer ; Betreuer: Rainer Haas." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2016. http://d-nb.info/1119073731/34.
Full textKhursigara, Cezar M. "Interactions between the energy-transducing protein TonB and the outer membrane receptor FhuA from Escherichia coli." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=85563.
Full textSedimentation velocity analytical ultracentrifugation (AUC) experiments involving mixtures of recombinant TonB and FhuA were conducted to determine the oligomeric state of TonB-FhuA complexes. These experiments demonstrated that wild-type TonB-FhuA proteins form a 2:1 (TonB:FhuA) complex, and that this complex is more abundant when FhuA is pre-incubated with the siderophore Fc. Deletion of the N-terminal region of TonB also demonstrated a 2:1 complex stoichiometry with FhuA, but in much lower abundance. Deletion of a highly conserved proline-rich region within TonB resulted in the formation of a 1:1 complex, suggesting a novel role for this domain in the formation of a functional 2:1 complex.
Affinities of interaction between wild-type and mutant TonB and FhuA proteins were measured by surface plasmon resonance (SPR). SPR data revealed that wild-type TonB-FhuA interactions are comprised of multiple interaction sites, and undergo an intermediate rearrangement event prior to the formation of the 2:1 complex. Deletions of TonB domains do not disrupt this rearrangement, but do decrease affinity. FhuA cork domain deletions also identified novel sites important for stable interactions.
Information of TonB-FhuA interactions derived by AUC and SPR described herein has contributed greatly to the purification and crystallization of TonB-FhuA co-complexes. Overall, these complementary biophysical techniques have provided important mechanistic details into the protein-mediated transport of iron into Gram-negative bacteria, and will provide a conceptual framework of TonB-FhuA that will help in elucidating aspects of the high-resolution structure of the complex.
Malia, Thomas J. 1977. "NMR structural and functional studies of the mithochondrial outer membrane protein VDAC by Thomas J. Malia." Thesis, Massachusetts Institute of Technology, 2006. http://hdl.handle.net/1721.1/37889.
Full text"September 2006." Vita.
Includes bibliographical references.
Apoptosis is a mechanism of programmed cell death required by multicellular organisms during development and for tissue maintenance. Bcl-2 family proteins are central regulators of apoptosis and many of their primary roles are carried out in the outer mitochondrial membrane. Anti-apoptotic Bcl-xL has been found previously to interact with VDAC, an outer mitochondrial membrane protein responsible for metabolite trafficking. Here, the NMR-based investigation of VDAC and its interaction with Bcl-xL in detergent micelles is described. As an integral membrane protein VDAC presented a challenge for producing a folded form amenable to solution NMR studies. Methods developed for expression and purification of human VDAC for structural studies by NMR spectroscopy were developed. Optimal sample conditions were explored in a screen of various detergents and buffers. Suitable NMR sample conditions for VDAC were identified and allowed further characterization of VDAC and its interactions by NMR and other methods. Obtained through various means, evidence of a concentration dependent self-association of VDAC is also presented. Chemical cross-linking, analytical size exclusion chromatography, and NMR spectroscopic studies strongly support an equilibrium model for LDAO-purified VDAC between monomer and trimer.
(cont.) Methods that were necessary to carry out NMR structural studies of VDAC and results from those studies are described. In addition to various methods previously developed for solution NMR spectroscopy of very large proteins, extensive labeling approaches and unconventional experimental NMR methods were necessary to obtain a high level of chemical shift assignment for micelle-bound VDAC. Chemical shift assignment has allowed the preliminary characterization of ATP and Bcl-xL binding to VDAC. Binding of Bcl-xL, a central regulator of apoptosis, to VDAC is demonstrated here. Using NMR spectroscopy, the VDAC-binding region of Bcl-xL has been mapped to a putative helical hairpin motif, which also mediates insertion into membranes. The stoichiometry of the VDAC/Bcl-xL complex is shown to be a heterotrimer of two VDAC monomers and one Bcl-xL. The demonstration of VDAC/Bcl-xL complex formation supports the concept that components of apoptosis and metabolism are integrally connected, and that interplay between the two processes is required for regulation of cell survival and cell death.
Ph.D.
Dai, Xian-zhu. "Studies on the folding of an outer membrane protein from a psychrotrophic bacterium, Shewanella livingstonensis Ac10." Kyoto University, 2012. http://hdl.handle.net/2433/157718.
Full text0048
新制・課程博士
博士(農学)
甲第16927号
農博第1943号
新制||農||1001(附属図書館)
学位論文||H24||N4688(農学部図書室)
29602
京都大学大学院農学研究科応用生命科学専攻
(主査)教授 栗原 達夫, 教授 小川 順, 教授 阪井 康能
学位規則第4条第1項該当
Peddireddi, Lalitha. "Transcriptional analysis and promoter characterization of two differentially expressed outer membrane protein genes of Ehrlichia chaffeensis." Diss., Manhattan, Kan. : Kansas State University, 2009. http://hdl.handle.net/2097/1499.
Full textWhite, Paul. "Bacterial protein import mediated by an iron transporter." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:20298bb4-0998-4dad-9dfa-dd9e52854dec.
Full textRomero-Ruiz, Mercedes [Verfasser]. "Interactions of Polypeptides with the Protein Translocation Channel of the Outer Membrane of Mitochondria / Mercedes Romero-Ruiz." München : Verlag Dr. Hut, 2011. http://d-nb.info/1012431703/34.
Full textTaiarol, Natasha Sabrina Tamara. "The effect of environmental conditions on the antigenicity of the outer membrane 35K protein present in Salmonella." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0021/MQ53121.pdf.
Full textLai, Tzung-Huei. "Two-Component Regulatory Systems of Anaplasma phagocytophilum and Outer Membrane Protein P44 Expression Locus of Anaplasma platys." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1276709646.
Full textMohan, Kumar Dipu. "Insights into the Host Cell Entry of Ehrlichia chaffeensis: Roles of the Bacterial Outer Membrane Protein EtpE." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1397229647.
Full textSaul-McBeth, Jessica. "Characterization of SipA, A Protein Important for Stress Responses in Vibrio cholerae." University of Toledo Health Science Campus / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=mco1544540466901883.
Full textGaddy, Jennifer Angeline. "Acinetobacter baumannii Virulence Attributes: The Roles of Outer Membrane Protein A, Acinetobactin-mediated Iron Acquisition Functions, and Blue Light Sensing Protein A." Miami University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=miami1289178632.
Full text