Relevant bibliographies by topics / Autotransporters

Academic literature on the topic 'Autotransporters'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Autotransporters"

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Jain, Sumita, Peter van Ulsen, Inga Benz, M. Alexander Schmidt, Rachel Fernandez, Jan Tommassen, and Marcia B. Goldberg. "Polar Localization of the Autotransporter Family of Large Bacterial Virulence Proteins." Journal of Bacteriology 188, no. 13 (July 1, 2006): 4841–50. http://dx.doi.org/10.1128/jb.00326-06.

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ABSTRACT Autotransporters are an extensive family of large secreted virulence-associated proteins of gram-negative bacteria. Secretion of such large proteins poses unique challenges to bacteria. We demonstrate that autotransporters from a wide variety of rod-shaped pathogens, including IcsA and SepA of Shigella flexneri, AIDA-I of diffusely adherent Escherichia coli, and BrkA of Bordetella pertussis, are localized to the bacterial pole. The restriction of autotransporters to the pole is dependent on the presence of a complete lipopolysaccharide (LPS), consistent with known effects of LPS composition on membrane fluidity. Newly synthesized and secreted BrkA is polar even in the presence of truncated LPS, and all autotransporters examined are polar in the cytoplasm prior to secretion. Together, these findings are consistent with autotransporter secretion occurring at the poles of rod-shaped gram-negative organisms. Moreover, NalP, an autotransporter of spherically shaped Neisseria meningitidis contains the molecular information to localize to the pole of Escherichia coli. In N. meningitidis, NalP is secreted at distinct sites around the cell. These data are consistent with a model in which the secretion of large autotransporters occurs via specific conserved pathways located at the poles of rod-shaped bacteria, with profound implications for the underlying physiology of the bacterial cell and the nature of bacterial pathogen-host interactions.
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Jain, Sumita, and Marcia B. Goldberg. "Requirement for YaeT in the Outer Membrane Assembly of Autotransporter Proteins." Journal of Bacteriology 189, no. 14 (May 18, 2007): 5393–98. http://dx.doi.org/10.1128/jb.00228-07.

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ABSTRACT Autotransporters constitute the largest group of secreted proteins in gram-negative bacteria. Autotransporter secretion involves the insertion of a carboxy-terminal beta barrel into and the translocation of an amino-terminal domain across the outer membrane. Here, we demonstrate that secretion of autotransporters from several organisms requires the outer membrane assembly factor YaeT.
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Lane, M. Chelsea, Jonathan D. Lenz, and Virginia L. Miller. "Proteolytic processing of the Yersinia pestis YapG autotransporter by the omptin protease Pla and the contribution of YapG to murine plague pathogenesis." Journal of Medical Microbiology 62, no. 8 (August 1, 2013): 1124–34. http://dx.doi.org/10.1099/jmm.0.056275-0.

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Autotransporter protein secretion represents one of the simplest forms of secretion across Gram-negative bacterial membranes. Once secreted, autotransporter proteins either remain tethered to the bacterial surface or are released following proteolytic cleavage. Autotransporters possess a diverse array of virulence-associated functions such as motility, cytotoxicity, adherence and autoaggregation. To better understand the role of autotransporters in disease, our research focused on the autotransporters of Yersinia pestis, the aetiological agent of plague. Y. pestis strain CO92 has nine functional conventional autotransporters, referred to as Yaps for Yersinia autotransporter proteins. Three Yaps have been directly implicated in virulence using established mouse models of plague infection (YapE, YapJ and YapK). Whilst previous studies from our laboratory have shown that most of the CO92 Yaps are cell associated, YapE and YapG are processed and released by the omptin protease Pla. In this study, we identified the Pla cleavage sites in YapG that result in many released forms of YapG in Y. pestis, but not in the evolutionarily related gastrointestinal pathogen, Yersinia pseudotuberculosis, which lacks Pla. Furthermore, we showed that YapG does not contribute to Y. pestis virulence in established mouse models of bubonic and pneumonic infection. As Y. pestis has a complex life cycle involving a wide range of mammalian hosts and a flea vector for transmission, it remains to be elucidated whether YapG has a measurable role in any other stage of plague disease.
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Lenz, Jonathan D., Brenda R. S. Temple, and Virginia L. Miller. "Evolution and Virulence Contributions of the Autotransporter Proteins YapJ and YapK of Yersinia pestis CO92 and Their Homologs in Y. pseudotuberculosis IP32953." Infection and Immunity 80, no. 10 (July 16, 2012): 3693–705. http://dx.doi.org/10.1128/iai.00529-12.

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ABSTRACTYersinia pestis, the causative agent of plague, evolved from the gastrointestinal pathogenYersinia pseudotuberculosis. Both species have numerous type Va autotransporters, most of which appear to be highly conserved. InY. pestisCO92, the autotransporter genesyapKandyapJshare a high level of sequence identity. By comparingyapKandyapJto three homologous genes inY. pseudotuberculosisIP32953 (YPTB0365, YPTB3285, and YPTB3286), we show thatyapKis conserved inY. pseudotuberculosis, whileyapJis unique toY. pestis. All of these autotransporters exhibit >96% identity in the C terminus of the protein and identities ranging from 58 to 72% in their N termini. By extending this analysis to include homologous sequences from numerousY. pestisandY. pseudotuberculosisstrains, we determined that these autotransporters cluster into a YapK (YPTB3285) class and a YapJ (YPTB3286) class. The YPTB3286-like gene of mostY. pestisstrains appears to be inactivated, perhaps in favor of maintainingyapJ. Since autotransporters are important for virulence in many bacterial pathogens, includingY. pestis, any change in autotransporter content should be considered for its impact on virulence. Using established mouse models ofY. pestisinfection, we demonstrated that despite the high level of sequence identity,yapKis distinct fromyapJin its contribution to disseminatedY. pestisinfection. In addition, a mutant lacking both of these genes exhibits an additive attenuation, suggesting nonredundant roles foryapJandyapKin systemicY. pestisinfection. However, the deletion of the homologous genes inY. pseudotuberculosisdoes not seem to impact the virulence of this organism in orogastric or systemic infection models.
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Cotter, Shane E., Neeraj K. Surana, and Joseph W. St. Geme. "Trimeric autotransporters: a distinct subfamily of autotransporter proteins." Trends in Microbiology 13, no. 5 (May 2005): 199–205. http://dx.doi.org/10.1016/j.tim.2005.03.004.

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Sauri, Ana, Zora Soprova, David Wickström, Jan-Willem de Gier, Roel C. Van der Schors, August B. Smit, Wouter S. P. Jong, and Joen Luirink. "The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease." Microbiology 155, no. 12 (December 1, 2009): 3982–91. http://dx.doi.org/10.1099/mic.0.034991-0.

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Autotransporters are large virulence factors secreted by Gram-negative bacteria. They are synthesized with a C-terminal domain that forms a β-barrel pore in the outer membrane implicated in translocation of the upstream ‘passenger’ domain across the outer membrane. However, recent structural data suggest that the diameter of the β-barrel pore is not sufficient to allow the passage of partly folded structures observed for several autotransporters. Here, we have used a stalled translocation intermediate of the autotransporter Hbp to identify components involved in insertion and translocation of the protein across the outer membrane. At this intermediate stage the β-domain was not inserted and folded as an integral β-barrel in the outer membrane whereas part of the passenger was surface exposed. The intermediate was copurified with the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex that catalyse the insertion and assembly of outer-membrane proteins. The data suggest a critical role for this general machinery in the translocation of autotransporters across the outer membrane.
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Restieri, Concetta, Geneviève Garriss, Marie-Claude Locas, and Charles M. Dozois. "Autotransporter-Encoding Sequences Are Phylogenetically Distributed among Escherichia coli Clinical Isolates and Reference Strains." Applied and Environmental Microbiology 73, no. 5 (January 12, 2007): 1553–62. http://dx.doi.org/10.1128/aem.01542-06.

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ABSTRACT Autotransporters are secreted bacterial proteins exhibiting diverse virulence functions. Various autotransporters have been identified among Escherichia coli associated with intestinal or extraintestinal infections; however, the specific distribution of autotransporter sequences among a diversity of E. coli strains has not been investigated. We have validated the use of a multiplex PCR assay to screen for the presence of autotransporter sequences. Herein, we determined the presence of 13 autotransporter sequences and five allelic variants of antigen 43 (Ag43) among 491 E. coli isolates from human urinary tract infections, diarrheagenic E. coli, and avian pathogenic E. coli (APEC) and E. coli reference strains belonging to the ECOR collection. Clinical isolates were also classified into established phylogenetic groups. The results indicated that Ag43 alleles were significantly associated with clinical isolates (93%) compared to commensal isolates (56%) and that agn43K12 was the most common and widely distributed allele. agn43 allelic variants were also phylogenetically distributed. Sequences encoding espC, espP, and sepA and agn43 alleles EDL933 and RS218 were significantly associated with diarrheagenic E. coli strains compared to other groups. tsh was highly associated with APEC strains, whereas sat was absent from APEC. vat, sat, and pic were associated with urinary tract isolates and were identified predominantly in isolates belonging to either group B2 or D of the phylogenetic groups based on the ECOR strain collection. Overall, the results indicate that specific autotransporter sequences are associated with the source and/or phylogenetic background of strains and suggest that, in some cases, autotransporter gene profiles may be useful for comparative analysis of E. coli strains from clinical, food, and environmental sources.
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Van Ulsen, Peter, Loek Van Alphen, Jan Ten Hove, Floris Fransen, Peter Van Der Ley, and Jan Tommassen. "A Neisserial autotransporter NalP modulating the processing of other autotransporters." Molecular Microbiology 50, no. 3 (October 20, 2003): 1017–30. http://dx.doi.org/10.1046/j.1365-2958.2003.03773.x.

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Knudsen, Stine K., Allan Stensballe, Magnus Franzmann, Uffe B. Westergaard, and Daniel E. Otzen. "Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation." Biochemical Journal 412, no. 3 (May 28, 2008): 563–77. http://dx.doi.org/10.1042/bj20071497.

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Autotransporters constitute the biggest group of secreted proteins in Gram-negative bacteria and contain a membrane-bound β-domain and a passenger domain secreted to the extracellular environment via an unusually long N-terminal sequence. Several passenger domains are known to be glycosylated by cytosolic glycosyl transferases, promoting bacterial attachment to mammalian cells. In the present study we describe the effect of glycosylation on the extracellular passenger domain of the Escherichia coli autotransporter Ag43α, which induces frizzy colony morphology and cell settling. We identify 16 glycosylation sites and suggest two possible glycosylation motifs for serine and threonine residues. Glycosylation stabilizes against thermal and chemical denaturation and increases refolding kinetics. Unexpectedly, glycosylation also reduces the stabilizing effect of Ca2+ ions, removes the ability of Ca2+ to promote cell adhesion, reduces the ability of Ag43α-containing cells to form bacterial amyloid and increases the susceptibility of the resulting amyloid to proteolysis. In addition, our results indicate that Ag43α folds without a stable intermediate, unlike pertactin, indicating that autotransporters may arrive at the native state by a variety of different mechanisms despite a common overall structure. A small but significant fraction of Ag43α can survive intact in the periplasm if expressed without the β-domain, suggesting that it is able to adopt a protease-resistant structure prior to translocation across the membrane. The present study demonstrates that glycosylation may play significant roles in structural and functional properties of bacterial autotransporters at many different levels.
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Kostakioti, Maria, and Christos Stathopoulos. "Functional Analysis of the Tsh Autotransporter from an Avian Pathogenic Escherichia coli Strain." Infection and Immunity 72, no. 10 (October 2004): 5548–54. http://dx.doi.org/10.1128/iai.72.10.5548-5554.2004.

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ABSTRACT The temperature-sensitive hemagglutinin (Tsh) is an autotransporter protein secreted by avian-pathogenic Escherichia coli strains that colonize the respiratory tract and lead to airsacculitis, pericarditis, and colisepticemia. It is synthesized as a 140-kDa precursor protein, whose processing results in a 106-kDa passenger domain (Tshs) and a 33-kDa β-domain (Tshβ). The presence of a conserved 7-amino-acid serine protease motif within Tshs classifies the protein in a subfamily of autotransporters, known as serine protease autotransporters of the Enterobacteriaceae. In this study, we report that purified Tshs is capable of adhering to red blood cells, hemoglobin, and the extracellular matrix proteins fibronectin and collagen IV. We also demonstrate that Tshs exerts proteolytic activity against casein, and we provide experimental evidence demonstrating that serine 259 is essential for the protease function. However, this residue is not required for adherence to substrates, and its replacement by an alanine does not abolish binding activity. In summary, our results demonstrate that Tsh is a bifunctional protein with both adhesive and proteolytic properties.
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Dissertations / Theses on the topic "Autotransporters"

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Orner, Sherko A. "Functional characterisation of Neisseria meningitidis autotransporters MSPA and APP." Thesis, University of Nottingham, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.490049.

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Sims, Peter Vincent. "Biogenesis of BapF : a novel acylated Bordetella autotransporter." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/41811.

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Autotransporters are a superfamily of Gram-negative secreted proteins, composed of a Cterminal domain which forms a β-barrel in the outer membrane and plays a significant role in translocation of the N-terminal passenger domain to the cell surface. A subfamily of autotransporters is N-terminally acylated during their biogenesis, a post-translational modification demonstrated to be essential for their function. Considering the autotransporter passenger domain is secreted beyond the outer membrane, how translocation can occur in the presence of N-terminal acyl groups is undetermined. The work in this thesis describes the biogenesis of the Bordetella autotransporter F (BapF) from B. bronchiseptica RB50, which is Nterminally acylated during the initial stages of its secretion to the cell surface. The acyl groups attached to BapF at the Cys28 residue were shown to be subsequently removed by signal peptidase 1 cleavage between residues Ala34 and Ala35, indicating that BapF forms an acylated intermediate in its secretion pathway. Studying the secretion of BapF mutants in which Nterminal acylation was ablated revealed that the passenger domain was still capable of reaching the cell surface; the surface-expressed passenger domain mediated phenotypes of cellular aggregation and an increased rate of culture sedimentation, similar to that observed in E. coli cultures expressing the wild-type BapF protein. However, cells expressing these mutants appear to have damaged outer membranes, potentially due to the observed increase in fulllength protein accumulating in the periplasm. Alternatively, E. coli cells expressing a BapF mutant in which signal peptidase 1 cleavage is blocked do not exhibit obvious aggregation and sedimentation phenotypes. Yet, an independent passenger domain is clearly produced. Based on the results presented in this thesis, it can be hypothesized that sequential processing of the BapF signal peptide, producing an acylated intermediate in the secretion pathway, helps to regulate the passage of BapF through the periplasm ultimately permitting surface expression. In addition, bioinformatic and molecular analysis strongly suggest the BapF passenger domain folds into a β-propeller structure, and if proven to do so, BapF will be the first autotransporter reported with this conformation
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Bokhari, Syed Habib. "Characterisation and secretion mechanism of Bordetella pertussis autotransporter proteins." Thesis, University of Glasgow, 2002. http://theses.gla.ac.uk/1507/.

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The identification and characterisation of new virulence determinants of 5. pertussis is providing important information for understanding the colonisation and survival strategies of the microorganism. B. pertussis deploys a range of surface-associated components to enable its successful colonisation of the host. Bap-5 has been identified as a new member of the B. pertussis autotransporter family of proteins that includes PRN, BrkA, TCF and Vag-8, largely due to its homology at the C-terminus and some other similar regions such as the RGD (integrin-binding) and SGXG (glycosaminoglycan-binding) motifs. The bap-5 gene also exists in B. bronchiseptica and B. parapertussis. Characteristic upstream regulatory sequences such as a ribosome-binding site were not seen in bap-5, but a potential heptameric BvgA-binding motif was identified. The expression of Bap-5 was confirmed by RT-PCR and Western blotting and was shown to be bvg dependent. Although Bap-5 does not possess a typical signal sequence like pertactin (PRN), its surface localisation was confirmed by agglutination and immunofluorescence assays. A potential role for Bap-5 in infection was studied by generating Bap-5 deficient mutants in two strains of B. pertussis. An allelic exchange procedure with the suicide vector pSS1129 carrying the bap-5 gene disrupted with a kanamycin-resistance cassette was used. PCR and Southern blotting confirmed the replacement of the wild-type bap-5 gene with the mutated version. Moreover, SDS-PAGE and Western blotting of outer-membrane preparations of B. pertussis Taberman wild-type and its Bap-5-deficient mutant showed a clear difference in their outer-membrane profile at ~79.9kDa presumably representing the unprocessed form and bands at ~65 kDa and ~16 kDa may represent the processed forms of the protein. The Bap-5 characterisation studies showed that the Taberman Bap-5-deficient strain was less able than the parent strain to colonise the lower respiratory tract of mice and adhesion studies (in vitro) showed that the Taberman parent was better in adhering to certain cell types than the Bap-5-deficient mutant.
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Contreras, Morales Elis Rosella. "La planeación inadecuada del transporte público de Toluca. Caso de estudio la empresa Autotransportes Suburbanos de la ciudad de Toluca y Zona Industrial , S.A de C.V. ( ATSUZI )." Tesis de Licenciatura, Universidad Autónoma del Estado de México, 2013. http://hdl.handle.net/20.500.11799/49262.

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La Zona Metropolitana de Toluca durante las últimas décadas ha tenido un crecimiento demográfico y una expansión urbana importante, lo cual ha generado cambios en las estructura de la ciudad, así como en la prestación de servicios públicos; en este sentido, la oferta del servicio de transporte, se ha dado en forma deficiente, la capacidad de dotar infraestructura y de circulación ha sido desordenada, parcial, segmentada y la movilidad de las personas se ha visto obstruida, paralizando el tránsito en sectores de la ciudad en horas pico prolongadas. Esta investigación, surge ante la falta de referentes analíticos en la planeación de rutas del transporte público en la zona metropolitana y el rezago de documentación significativ a.
El objetivo de la presente investigación es analizar el transporte público urbano de la Zona Metrop oli tana de Toluca, en particular la empresa “Autotransportes Suburbanos de la Ciudad de Toluca y Zona Industrial, S.A. de C.V. (ATSUZI) en un contexto de movilidad urbana. La investigación se realizó con apoyo de información estadística, analizando la problemática del transporte público urbano existente en la ciudad y con ello realizar sugerencias de reordenamiento y de mov ilidad de la población de esta zona metropolitana.
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Dufailu, Osman Adamu. "Role of meningococcal Neisserial autotransporter lipoprotein (NalP) in host pathogenesis." Thesis, University of Nottingham, 2017. http://eprints.nottingham.ac.uk/41127/.

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Neisseria meningitidis (Nm) can cause life-threatening bacterial meningitis and septicaemia. The high mortality of meningitis is associated with meningococcal invasion of the central nervous system (CNS) by breaching of the blood-brain barrier (BBB). Nm elaborates several cell-surface and secreted virulence factors that promote host invasion and colonisation. One important class are the autotransporter proteins. Adhesion and penetration protein (App), meningococcal serine protease A (MspA), Immunoglobulin A1 protease (IgA1p) and Neisserial autotransporter lipoprotein (NalP) are serine protease autotransporters of Nm; all have previously been demonstrated to have roles in meningococcal virulence. For App and MspA, uptake by host cells, nuclear localisation, histone clipping and induction of apoptosis have been described in our laboratory. However, a time course for the efficient uptake and nuclear localisation of these proteins into human brain microvascular endothelial cells (HBMECs) and details regarding the mechanism for histone clipping remained unknown. To address these points, both App and MspA and proteolytically-inactive mutant derivatives were expressed using the pColdTF vector system and purified under native conditions. Using confocal scanning microscopy optimal uptake and nuclear localisation of recombinant fusion proteins containing the functional passenger domains of both App and MspA in HBMECs was shown to occur 8 h-post exposure. Furthermore, the requirement for the active site serine residue in both autotransporters for H3.1 clipping was demonstrated, and human coagulation factor V (FV) was shown to be an additional substrate for both proteins. NalP is a cell-surface maturation protease which processes App, MspA and other meningococcal surface proteins such as IgA1P, LbpB and NhbA, and thus modulates the cell surface and secretome of the organism. Previous studies aimed at functional characterisation of NalP have typically relied on the phenotypic comparison of wild-type and nalP-mutant derivatives. Here an active recombinant NalP was expressed and purified, and used to investigate the interaction of NalP with host cells in order to more comprehensively elucidate the role of NalP during meningococcal interaction with the host. A recombinant NalP (rNalP) passenger domain was purified under non-denaturing conditions using immobilized nickel chromatography. Although rNalP had apparent molecular weight 8-10 kDa less than that of NalP secreted by wild-type meningococci, it was functional as determined by its ability to process human complement 3 (C3). rNalP was shown to cleave human coagulation factor V (FV), a proteolytic event which is likely to contribute to bacterial pathogenesis. Binding and uptake of rNalP into human cells was demonstrated by flow cytometry and confocal microscopy. Interestingly, rNalP was differentially localised to different cellular compartments in different cell types. Treatment of HBMECs with rNalP resulted in increased levels of IL-6 and IL-8, and decreased levels of TNF-α in culture supernatants. rNalP was shown to clip histone 2B but not other histone proteins. Using a re-tagging approach a number of rNalP-interacting host proteins were identified. These included proteins of the candidate membrane, cytoplasm, cytoskeleton endoplasmic reticulum, mitochondrion, and nucleus. Some of these proteins are likely to be involved in trafficking of NalP and the cellular response to this protein. Overall, the findings of this study expand our knowledge on the contribution of three autotransporters to meningococci pathogenesis and provide a platform to further explore the host response to NalP uptake and the epigenetic changes associated with autotransporter host interactions, which may guide the development of future therapeutic interventions.
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Gagnon, Elizabeth. "The requirement of putative autochaperone motifs for autotransporter passenger domain folding." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/43502.

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Darch, Owen Matthew. "A study on the function of the Pseudomonas aeruainosa autotransporter PA0328." Thesis, University of Nottingham, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.523036.

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Noofeli, Mojtaba. "Genetic analysis and characterisation of the BapC autotransporter of bordetella pertussis." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/105/.

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The autotransporters are a family of extracellular proteins, found in various Gram-negative bacteria, that have many different functions but appear to have a similar mechanism of export. In B. pertussis, the virulence-regulated proteins Pertactin, BrkA, Tcf, and Vag8 have structural homology at their C-termini (30-kDa) and the N-terminal of the mature proteins share structural characteristics such as RGD and SGXG motifs. Recently, another member of the B. pertussis autotransporter family, Bap-5 (Blackburn, 2000) (GenBank accession number AF081494) or BapC (GenBank accession number AJ277634.1) was identified. The present work has suggested that BapC, like BrkA, is a serum-resistance factor. B. pertussis brkA, bapC double and bapC single mutants were created, and showed greater sensitivity to killing by normal human serum than their wild-type strains but they were not as sensitive as a bvg mutant strain. Competition assays also showed an important role for BapC, like BrkA, in virulence of B. pertussis strains after intranasal infection in the mouse. Moreover, the brkA, bapC double and bapC single mutants were found to be more sensitive to the antimicrobial peptide, cecropin P1, than the parent strain. Nucleotide and amino acid analyses of the bapC region spanning the poly(C) and poly(G) tracts of a number of B. pertussis strains showed minor nucleotide and amino acid polymorphisms in some strains but it appeared that all had an ORF that would be able to produce some form of BapC.
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Ait-Tahar, Kamel. "Identification and characterisation of AutA : an autotransporter protein of Neisseria meningitidis." Thesis, University of Nottingham, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394868.

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Yoo, Christopher Charles. "Investigating the Role of Trimeric Autotransporter Adhesins in Fusobacterium nucleatum Pathogenesis." Thesis, Virginia Tech, 2019. http://hdl.handle.net/10919/101683.

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Fusobacterium nucleatum is a Gram-negative bacterium that serves as a bridging organism in polymicrobial biofilms within the oral cavity. Although the bacterium is abundant in healthy gingival tissue, recent studies have found that F. nucleatum is associated with a wide-spectrum of human diseases which include periodontal disease, preterm birth, endocarditis, colorectal cancer, and pancreatic cancer. Previous studies of F. nucleatum virulence have uncovered two surface adhesins, Fap2 and FadA, that interact with the surface of human cells; however, the study of new virulence factors was previously limited as there was no gene deletion system available to functionally analyze F. nucleatum proteins. Interestingly, F. nucleatum has a diverse landscape of structurally unique surface adhesins called Type 5c secreted trimeric autotransporter adhesins (TAAs), which are a family of proteins that are historically known for their contributions to bacterial pathogenesis. This dissertation encompasses the use of recombinant protein expression systems and newly developed gene deletion technology to provide a foundational understanding of the contribution of Type 5c secreted proteins in F. nucleatum pathogenesis. Our results show that the presence of TAAs on the surface of F. nucleatum contribute to the bacterium's ability to bind and invade human cells, establishing the need to characterize other F. nucleatum surface proteins. Additionally, our studies analyzed the proinflammatory landscape induced by F. nucleatum through the identification of specific cytokines that are being secreted during in vitro infections of human cells. Cytokine signaling is a critical aspect of the host cell immune response as it promotes the recruitment of immune cells to the site of infection for efficient clearance of bacterial pathogens. While it has been well established that F. nucleatum modulates the secretion of IL-8, our studies identified that the bacterium also promotes the secretion of CXCL1, which is an important signaling protein that promotes tumor metastases. Overall, the work provided in this dissertation has delivered the initial characterization of TAAs in F. nucleatum virulence, a framework for future studies of Type 5c secreted proteins in Fusobacterium pathogenesis, and the role of Fap2 and FadA in promoting pro-inflammatory and pro-metastatic signaling from colorectal cancer cells.
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Books on the topic "Autotransporters"

1

La cara oculta de Ruta 100: La construcción subjetiva de la democracia, la representavidad y la legitimidad. México, D.F: Casa Abierta al Tiempo, 2002.

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Gutiérrez, Andrea. La (des) reglamentación del autotransporte metropolitano de pasajeros. Ciudad de Buenos Aires: Instituto de Geografía, Facultad de Filosofía y Letras, Universidad de Buenos Aires, 2003.

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González, Ovidio. Transporte en Querétaro en el siglo XX: Surgimiento y desarrollo del autotransporte, 1900-1965. [Mexico City]: Secretaría de Comunicaciones y Transportes, Instituto Mexicano del Transporte, 1992.

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Ruiz, José Enrique González. Ruta 100: La quiebra del estado de derecho. México: Grupo Editorial Planeta, 1996.

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Galeana, Oscar Armando Rico. La integración del autotransporte de carga en el marco del Tratado de Libre Comercio de América del Norte. [Mexico]: Secretaría de Comunicaciones y Transportes, 2001.

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Juridica, La Biblioteca. Ley de Caminos, Puentes y Autotransporte Federal (México) (Edición 2019). Independently Published, 2019.

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Payandeh, Jian Mehr-Dean. Production of the autotransporter IgA1 protease [beta]-domain from Neisseria gonorrhoeae for structural studies. 2004.

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Byrnes, Mike, and Mike Brynes &. Associates. Bumper to Bumper: La gua completa para operaciones de autotransporte de carga. Mike Byrnes & Associates, Inc., 1992.

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Eric, Moreno Quintero, and Instituto Mexicano del Transporte, eds. Características del autotransporte público y privado de carga en las carreteras mexicanas. Sanfandila, Qro: Secretaría de Comunicaciones y Transportes, Instituto Mexicano del Transporte, 2001.

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10

Mike Byrnes & Assoc.; Inc. Bumper to Bumper: LA Guia Completa Para Operaciones De Autotransporte De Carga. Mike Byrnes & Assoc., Inc., 2005.

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Book chapters on the topic "Autotransporters"

1

Otto, Ben R. "Autotransporters." In Protein Secretion Pathways in Bacteria, 191–205. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0095-6_10.

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van Ulsen, Peter. "Protein Folding in Bacterial Adhesion: Secretion and Folding of Classical Monomeric Autotransporters." In Advances in Experimental Medicine and Biology, 125–42. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0940-9_8.

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Łyskowski, Andrzej, Jack C. Leo, and Adrian Goldman. "Structure and Biology of Trimeric Autotransporter Adhesins." In Advances in Experimental Medicine and Biology, 143–58. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-0940-9_9.

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Yen, Yihfen T., and Christos Stathopoulos. "Identification of Autotransporter Proteins Secreted by Type V Secretion Systems in Gram-Negative Bacteria." In Protein Targeting Protocols, 33–46. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-466-7_3.

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Jaeger, Karl-Erich, and Harald Kolmar. "Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Cell Surface Display and Ultrahigh-Throughput Screening of Large Protein Libraries." In Springer Protocols Handbooks, 87–103. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8623_2015_125.

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Wilhelm, S., H. Kolmar, and F. Rosenau. "Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Ultra-High Throughput Cell-Surface Display and Screening of Large Protein Libraries." In Handbook of Hydrocarbon and Lipid Microbiology, 4587–600. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-77587-4_361.

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Navarro-García, Fernando. "Serine Protease Autotransporters of Enterobacteriaceae." In Handbook of Proteolytic Enzymes, 3092–98. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00683-9.

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"Structure and Function of the Translocator Domain of Bacterial Autotransporters." In RSC Biomolecular Sciences, edited by Reinhard Grisshamer and Susan K. Buchanan, 270–87. Cambridge: Royal Society of Chemistry, 2007. http://dx.doi.org/10.1039/9781847552563-00270.

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O.M. Al-Dahmoshi, Hussein, Noor S.K. Al-Khafaji, and Farah T. Al-Alaq. "Virulence and Antibiotic Resistance of Acinetobacter baumannii among Urinary Tract Infections." In Urinary Tract Infections - the Imbalance Between the Pathogen Virulence and the Host Defense [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94508.

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Abstract:
Acinetobacter baumannii is one of the opportunistic bacteria firstly related with the hospital acquired infection influencing primarily to weakening the patient in the ICU. It is sometimes transferred to the patient by transient colonization of hands of the workers of healthcare, and persistence on eco-surfaces. Acinetobacter baumannii inhalation aerosolized through endo-tracheal suctioning of the ventilated patient is widespread among ventilator-related pneumonia (VAP). It is infections mainly associated with ventilator-related pneumonia (VAP), community Acquired Pneumonia (CAP), invasive bacterial infections (IBIs) and UTI (urinary tract infection). It is one of the prominent uropathogens problematic with antibiotic resistance especially carbapenem resistant Acinetobacter baumannii (CRAB). Their colonization of urinary tract and establishment of infection may attributed mainly to set of virulence factors like: Acinetobactin-assisted iron acquisition system, Bap (biofilm-related protein), phospholipase D, Ata (Acinetobacter trimeric autotransporter), chaperone-usher type pilus (Csu), OmpA (outer membrane protein A), and Plasminogen-binding protein (CipA). The common drugs used for treatment Acinetobacter baumannii infections involve polymyxins, glycylcyclines, tetracyclines, mono-bactams, fluoroquinolones, aminoglycosides, antipseudomonal carbapenems, antipseudomonal cephalosporins, and sulbactam. The rates of MDR isolation or also comprehensively the resistant Acinetobacter baumannii are significantly increased and so the combination of two or more (colistin, tigecycline, or colistin-rifampicin combination therapy) drugs is sometimes used to treat infections of MDR-AB. As a conclusion the Acinetobacter baumannii engagement in urinary tract infections attributed mainly to their adhesins, invasins and intrinsic antibiotic resistance.
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Renn, Jonathan P., and Patricia L. Clark. "Disulfide Bond-Mediated Passenger Domain Stalling as a Structural Probe of Autotransporter Outer Membrane Secretion In Vivo." In Methods in Enzymology, 233–51. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-381268-1.00030-6.

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Conference papers on the topic "Autotransporters"

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"Properties of the C-terminal domain of HlyIICTD suggest that B. cereus HlyII is a representative potential member of trimeric autotransporter adhesins among gram-positive bacteria." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-384.

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