Relevant bibliographies by topics / Human Pathogen Helicobacter

Academic literature on the topic 'Human Pathogen Helicobacter'

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Published: 6 September 2023

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Journal articles on the topic "Human Pathogen Helicobacter"

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Forbes, GeoffreyM, BrendanJ Collins, Adam Harris, J. J. Misiewicz, Liam Murray, and Ian Harvey. "Helicobacter pylori: a human pathogen." Lancet 345, no. 8964 (June 1995): 1579–80. http://dx.doi.org/10.1016/s0140-6736(95)91132-4.

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Graham, J. R. "Helicobacter pylori: human pathogen or simply an opportunist?" Lancet 345, no. 8957 (April 1995): 1095–97. http://dx.doi.org/10.1016/s0140-6736(95)90824-2.

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Haley, Kathryn P., and Jennifer A. Gaddy. "Helicobacter pylori: Genomic Insight into the Host-Pathogen Interaction." International Journal of Genomics 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/386905.

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The advent of genomic analyses has revolutionized the study of human health. Infectious disease research in particular has experienced an explosion of bacterial genomic, transcriptomic, and proteomic data complementing the phenotypic methods employed in traditional bacteriology. Together, these techniques have revealed novel virulence determinants in numerous pathogens and have provided information for potential chemotherapeutics. The bacterial pathogen,Helicobacter pylori, has been recognized as a class 1 carcinogen and contributes to chronic inflammation within the gastric niche. Genomic analyses have uncovered remarkable coevolution between the human host andH. pylori. Perturbation of this coevolution results in dysregulation of the host-pathogen interaction, leading to oncogenic effects. This review discusses the relationship ofH. pyloriwith the human host and environment and the contribution of each of these factors to disease progression, with an emphasis on features that have been illuminated by genomic tools.
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Abd El-Ghany, Wafaa A. "Helicobacter pullorum: A potential hurdle emerging pathogen for public health." Journal of Infection in Developing Countries 14, no. 11 (November 30, 2020): 1225–30. http://dx.doi.org/10.3855/jidc.12843.

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Emerging zoonotic pathogens gain more attention due to the adverse effects on human and animal’s health and productivity. One of these zoonotic pathogens is Helicobacter pullorum (H. pullorum) which was firstly diagnosed in 1994. This bacterium is enterpathogenic in poultry and contaminates the carcasses meat during processing or improper handling. Human can get H. pullorum infection mainly through mishandling of contaminated carcasses or consumption of undercooked meat. Infection of H. pullorum in human is associated with gastroenteritis and hepatitis. Diagnosis of H. pullorum is very difficult as misdiagnosis with other enteric zoonotic pathogens like Campylobacter and other Helicobacter species is common. Unlike other types of Helicobacter, there are little information and few researches regarding prevalence, pathogenesis, diagnosis and control of H. pullorum infection either animals or human. Accordingly, this review article was prepared to give more details about H. pullorum sources of infection, pathogenicity, incidence in poultry and human as well as its treatment.
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Loman, N. J., L. A. S. Snyder, J. D. Linton, R. Langdon, A. J. Lawson, G. M. Weinstock, B. W. Wren, and M. J. Pallen. "Genome Sequence of the Emerging Pathogen Helicobacter canadensis." Journal of Bacteriology 191, no. 17 (June 19, 2009): 5566–67. http://dx.doi.org/10.1128/jb.00729-09.

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ABSTRACT We determined the genome sequence of the type strain of Helicobacter canadensis, an emerging human pathogen with diverse animal reservoirs. Potential virulence determinants carried by the genome include systems for N-linked glycosylation and capsular export. A protein-based phylogenetic analysis places H. canadensis close to Wolinella succinogenes.
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Prashar, Akriti, Mariana I. Capurro, and Nicola L. Jones. "Under the Radar: Strategies Used by Helicobacter pylori to Evade Host Responses." Annual Review of Physiology 84, no. 1 (February 10, 2022): 485–506. http://dx.doi.org/10.1146/annurev-physiol-061121-035930.

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The body depends on its physical barriers and innate and adaptive immune responses to defend against the constant assault of potentially harmful microbes. In turn, successful pathogens have evolved unique mechanisms to adapt to the host environment and manipulate host defenses. Helicobacter pylori ( Hp), a human gastric pathogen that is acquired in childhood and persists throughout life, is an example of a bacterium that is very successful at remodeling the host-pathogen interface to promote a long-term persistent infection. Using a combination of secreted virulence factors, immune subversion, and manipulation of cellular mechanisms, Hp can colonize and persist in the hostile environment of the human stomach. Here, we review the most recent and relevant information regarding how this successful pathogen overcomes gastric epithelial host defense responses to facilitate its own survival and establish a chronic infection.
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Krebes, Juliane, Richard D. Morgan, Boyke Bunk, Cathrin Spröer, Khai Luong, Raphael Parusel, Brian P. Anton, et al. "The complex methylome of the human gastric pathogen Helicobacter pylori." Nucleic Acids Research 42, no. 4 (December 2, 2013): 2415–32. http://dx.doi.org/10.1093/nar/gkt1201.

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Abstract The genome of Helicobacter pylori is remarkable for its large number of restriction-modification (R-M) systems, and strain-specific diversity in R-M systems has been suggested to limit natural transformation, the major driving force of genetic diversification in H. pylori. We have determined the comprehensive methylomes of two H. pylori strains at single base resolution, using Single Molecule Real-Time (SMRT®) sequencing. For strains 26695 and J99-R3, 17 and 22 methylated sequence motifs were identified, respectively. For most motifs, almost all sites occurring in the genome were detected as methylated. Twelve novel methylation patterns corresponding to nine recognition sequences were detected (26695, 3; J99-R3, 6). Functional inactivation, correction of frameshifts as well as cloning and expression of candidate methyltransferases (MTases) permitted not only the functional characterization of multiple, yet undescribed, MTases, but also revealed novel features of both Type I and Type II R-M systems, including frameshift-mediated changes of sequence specificity and the interaction of one MTase with two alternative specificity subunits resulting in different methylation patterns. The methylomes of these well-characterized H. pylori strains will provide a valuable resource for future studies investigating the role of H. pylori R-M systems in limiting transformation as well as in gene regulation and host interaction.
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Sharma, Cynthia M., Steve Hoffmann, Fabien Darfeuille, Jérémy Reignier, Sven Findeiß, Alexandra Sittka, Sandrine Chabas, et al. "The primary transcriptome of the major human pathogen Helicobacter pylori." Nature 464, no. 7286 (February 17, 2010): 250–55. http://dx.doi.org/10.1038/nature08756.

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Zanotti, Giuseppe, Francesca Vallese, and Nigam M. Mishra. "Function from structure: Lpp20 from the human pathogen Helicobacter pylori." Acta Crystallographica Section A Foundations and Advances 73, a2 (December 1, 2017): C240. http://dx.doi.org/10.1107/s2053273317093330.

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Pflock, Michael, Simone Kennard, Nadja Finsterer, and Dagmar Beier. "Acid-responsive gene regulation in the human pathogen Helicobacter pylori." Journal of Biotechnology 126, no. 1 (October 2006): 52–60. http://dx.doi.org/10.1016/j.jbiotec.2006.03.045.

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Dissertations / Theses on the topic "Human Pathogen Helicobacter"

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Baltrus, David Anthony. "Physiology and evolutionary effects of gene exchange in the human pathogen helicobacter pylori /." view abstract or download file of text, 2006. http://proquest.umi.com/pqdweb?did=1251837701&sid=1&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2006.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 97-108). Also available for download via the World Wide Web; free to University of Oregon users.
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Alderson, Jesse. "Studies on the aerobic respiratory chain of the human gastric pathogen Helicobacter pylori." Thesis, University of Sheffield, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324459.

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Pelliciari, Simone <1988&gt. "Biochemical and functional characterization of the HP1043 orphan response regulator of the human pathogen Helicobacter pylori." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2018. http://amsdottorato.unibo.it/8561/1/Simone%20Pelliciari_PhD%20thesis.pdf.

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In Helicobacter pylori, the hp1043 gene is one of the transcriptional regulator essential for cell viability. As such, this gene could not be deleted, supporting the hypothesis that HP1043 could be involved in the regulation of crucial cellular processes. The impossibility of generating a knock-out mutant for hp1043 gene, or even modulate the amount of HP1043 protein in the cell, has hampered the detailed characterization of its regulatory function. Using Chromatin Immunoprecipitation-sequencing (ChIP-seq), we were able to identify genome-wide at least 37 new HP1043 binding sites. Moreover, in vitro DNase I protection assays (footprints) enabled mapping of the HP1043 binding sites on a subset of the new targets, revealing the presence of a conserved nucleotide sequence motif consisting of a direct TTTAAG repeat. Furthermore, hydroxyl-radical probing allowed to further refine the positions of HP1043 binding, suggesting that the proposed direct repeats consensus motif is recognized by HP1043, likely through a major groove read-out mechanism. Intriguingly, a significant fraction of newly identified binding sites overlaps promoter regions of genes involved in translation. Accordingly, arrest of protein translation determined induction of almost all HP1043 target genes. These observations prompted us to propose HP1043 as key regulator in H. pylori, likely involved in sensing and in coordinating the response to environmental stress inducing an arrest of protein synthesis. DNase I and hydroxyl-radical footprinting experiments aimed to elucidate the role of each base of the consensus motif in the protein-DNA binding were performed. They showed a fundamental role of both hemisite, with major effect on the AAG out of TTTAAG for the first sequence and TTAA hexamer core for the second. Experiments aimed to elucidate the functional role of the protein were carried out by in vitro transcription assays, to evaluate the effect of HP1043 promoter binding on the activity on the RNA polymerase.
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Comtois, Spencer. "Enzymatic mechanisms that mediate resistance to oxidative and nitrosative stress in the human gastric pathogen Helicobacter pylori." Thesis, University of Sheffield, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.269273.

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Davids, Wagied. "Causes of Substitution Frequency Variation in Pathogenic Bacteria." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4838.

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Kumar, Amrendra. "Roles of Protein Acetylation in the Human Pathogen Helicobacter pylori." Thesis, 2021. https://etd.iisc.ac.in/handle/2005/5768.

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Helicobacter pylori is a gram-negative epsilon proteobacterium infecting half of the world population. H. pylori is a naturally competent bacterium with a huge repertoire of Restriction-Modification (RM) systems. The bacterium lacks a mismatch DNA repair system, lexA gene responsible for SOS response, and starvation/stress-responding alternative sigma factor. These factors make it essential to understand the physiology of bacteria to manage H. pylori-related diseases. In recent years, protein acetylation stands out as a vital regulatory system of cellular processes such as virulence, acid stress survival, transcription, motility, and metabolic pathways. In this study, Western blotting-based acetylome analysis of different strains of H. pylori suggest a prominent and significantly different acetylation profile in H. pylori, strain. Mass spectrometry-based acetylome analysis found 384 acetylation sites on 236. HP0935, a possible protein N-acetyltransferase belonging to GNAT superfamily was identified. Unlike most GNAT superfamily acetyltransferases HP0935 remains as a monomer in the solution. Biochemical analysis suggests that HP0935 acetylates the respective N-α amino group of lysine, arginine, methionine, and serine. In addition, HP0935 acetylates the N-ε amino group of lysine. Crystals of HP0935 were grown by the sitting drop vapor diffusion method, and the structure was solved to 1.93 Å resolution. The crystal structure of HP0935 showed a proper GNAT fold, which further validates that the protein belongs to the GNAT superfamily. The co-crystal structure of HP0935 and acetyl-CoA complex suggests that Glu77, His115, and Tyr127 and a conserved water molecule could play essential roles in the catalysis. In general, glutamate and histidine in most GNATs act as a general base that deprotonate the amino group of substrates. In other GNATs, conserved water molecules could perform a similar activity. Tyrosine in the structure acts as a general acid that protonates the leaving thiolate anion during catalysis. Point mutations of HP0935 E77Q, H115A, and Y127F were created by site-directed mutagenesis to understand the catalytic mechanism. Acetylation activity of these mutants against lysine showed that mutant E77Q and H115A have comparable activity to the wild type. In comparison, mutant Y127F completely lost its activity. These results suggest that HP0935 contains catalytic activity where a conserved water molecule probably performs the deprotonation of the amino group of substrates and Tyr127 acts as a general acid. In search of the protein substrates for HP0935, HPDprA, DNA processing protein A which plays an essential role in natural transformation found to be acetylated by HP0935. SPR analysis suggests that HPDprA interacts with HP0935. Enzymatically acetylated K133 residue and non-enzymatically acetylated K127 residue were found to play a regulatory role in the DNA binding activity of HPDprA. Next, acetylation of HPDprA inhibits its known stimulatory effects on the activity of HPyAVI DNA methyltransferase. Two other proteins, HPyAVI, an N6 adenine methyltransferase, and HPUvrD helicase were found to be substrates of HP0935. It was observed that enzymatic acetylation stimulates the DNA methyltransferase activity of HPyAVI. Biochemical analysis of acetylated HPUvrD suggests that both enzymatic and non-enzymatic acetylation stimulate its ATPase activity by ~30%. Acetylated HPUvrD also showed high helicase activity against 3’overhang DNA substrate in comparison to wild-type HPUvrD. These results demonstrate a role for acetylation in Natural Transformation and DNA repair pathways of H. pylori.
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Kumar, Sumith. "Exploring the Roles of Phase Variable HpyAII Restriction-modification System in the Human Pathogen Helicobacter pylori." Thesis, 2016. http://etd.iisc.ac.in/handle/2005/4069.

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Helicobacter pylori is a Gram-negative microaerophilic bacteria known to infect as much as 80% of some populations with an average morbidity range of around 50% of the world population. It has been recognized as a definitive carcinogen (Type I). H. pylori shows extraordinary genetic diversity and this property is critical to its success as a human pathogen. High genetic diversity and interstrain variations seen in H. pylori is attributed to its remarkable ability to take foreign DNA by natural transformation. Natural transformation in H. pylori is governed to some extent by the presence of Restriction-Modification systems (R-M systems). Three types of DNA methylation are associated with R-M systems in bacteria, N6-adenine (m6A), C5-cytosine (m5C) and N4-cytosine (m4C). Recent studies in pathogenic bacteria have shown the epigenetic roles of m6A in virulence, gene regulation and genetic evolution of the organism. This is in contrast to eukaryotes where m5C is known to be the epigenetic signal. In mammals and plants DNA cytosine methyltransferases epigenetically regulate the gene expression through the precise epigenetic modification of certain cytosine residues with a methyl group. Moreover, aberrant methylation patterns are embryonic lethal in mammals, and can also lead to diseases including cancer. In plant it can result in pleiotropic morphological defects. The role of cytosine methylation in bacteria is not very well known. A recent study has shown that the loss of m5C in H. pylori strains alters the expression of genes involved in motility, adhesion, and virulence. Another study in E. coli has shown the role of m5C in stationary phase stress regulation. However, no physiological role of the other form of cytosine methylation (m4C), aside restriction protection is known in bacteria. Genome sequences of various strains of H. pylori reveal an abundance of R-M systems. Typically 25-34 R-M systems are present in different H. pylori strains. Methylome analysis of H. pylori 26695 strain has revealed the presence of numerous m6A and m5C methyltransferases. H. pylori 26695 strain harbors a phase variable type IIS HpyAII R-M system. This R-M system is composed of two exocyclic methyltransferases, M1.HpyAII (m6A) and M2.HpyAII (m4C) and one type IIS phase variable endonuclease (HpyAII). HpyAII recognizes the sequence 5' GAAGA 3' / 3' CTTCT 5' and cleaves eight bp downstream on the top strand and seven bp downstream on the bottom strand. HpyAII is a novel phase-variable restriction endonuclease containing multiple repetitive stretches of adenine residues in the ORF. M1.HpyAII methylates the final adenine residue of GAAGA sequence, whereas M2.HpyAII methylates the first cytosine of the complementary TCTTC sequence. M2.HpyAII is the only N4-cytosine (m4C) MTase present in H. pylori strain 26695. The aim of the present study is to understand the potential epigenetic role of m4C modification by understanding the roles of HpyAII R-M system in virulence, gene expression and natural transformation of H. pylori. Understanding the biochemical properties of the novel phase variable HpyAII endonuclease can reveal critical information about the regulation of natural transformation in H. pylori. Bioinformatics analysis shows that HpyAII is an HNH catalytic motif containing endonuclease. The biochemical study on HpyAII indicates that the enzyme prefers two-site substrate over a one-site substrate for maximal activity. A strong preference for two-sites was observed with supercoiled plasmid and oligonucleotide duplex DNA. Cofactor analysis revealed the preference of R.HpyAII for transition metals (Ni2+, Cd2+, and Co2+) over alkaline earth metals (Mg2+, Ca2+) for maximal cleavage activity. Mutational analysis of the conserved residues of the HNH motif in HpyAII confirmed the presence of functional HNH motif. Interestingly, mutation of first His residue (general acid) of the HNH motif to Ala does not abolish the enzymatic activity but instead causes loss of fidelity compared to wild type HpyAII. The H328A mutant displayed promiscuous DNA cleavage activity on different DNA substrates. The novelty of this observation lies in the fact that mutation of first His residue (general acid) of the HNH motif in other known HNH motif containing enzymes has always abolished enzymatic activity. Mutation at a single amino acid residue leading to the loss of fidelity provides insights into the regulation of fidelity and evolution of restriction enzymes by point mutation.
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Prasad, Yedu. "Kinetic, Catalytic and Epigenetic Properties of HpyAXVII DNA Methyltransferase – a Phasevarion in the Human Pathogen Helicobacter pylori." Thesis, 2019. https://etd.iisc.ac.in/handle/2005/5097.

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Helicobacter pylori is the leading cause of gastric cancer in human beings. It is a helix-shaped, Gram-negative, motile bacteria that colonizes the gastric mucosa and eventually the gastric epithelium. It has an overabundance of Restriction-Modification (R-M) systems, a large majority of them being strain-specific. Several Type III DNA MTases have been identified as phasevarions (phase variable regulons) that can reversibly switch ON or OFF depending on the repeat length at a phase variable locus within the gene. This study is a comprehensive approach to understand the biochemical and enzyme kinetic nature of M.HpyAXVII, a phase variable N6-adenine DNA MTase from H. pylori 26695. Initial velocity, product inhibition and substrate inhibition analyses revealed that M.HpyAXVII binds to AdoMet first followed by DNA to form a ternary complex in an ordered Bi Bi reaction. Comparison of M.HpyAXVII amino acid sequence with its homologues from H. pylori strains, for which full sequence data is available, showed that the protein is highly conserved except for the TRD domain. The high homology at the region flanking the TRD means that this region is amenable for domain swapping. Combined with phase variable switching between ON and OFF states, H. pylori has evolved a powerful way to switch between genome methylation status, or methylomes, thereby increasing fitness. Comparison of hpyaxvii DNA sequences of homologs across strains revealed that the poly-G repeat length is variable. In almost half the strains the poly-G is maintained in the OFF position, i.e., a full-length fusion protein is not expressed. However, addition or deletion of a single guanosine can result in the expression of a potentially functional M.HpyAXVII in these strains. In a small subset of strains, the status of the phase variable locus is in the phase variably ON position. Interestingly, there are a few strains where the locus is always ON, i.e., there is no poly-G tract at all. Thus, the ontogeny of hpyaxvii phase variation in different strains provides a snapshot into the phylogeny of hpyaxvii phase evolution across different H. pylori strains. To investigate the effects of the total absence of M.HpyAXVII from H. pylori 26695, as in, constitutively OFF genotype, a deletion mutant was generated, designated Δhpyaxvii. Comparison of total mRNA levels between H. pylori 26695 Δhpyaxvii and WT revealed several genes that were differentially expressed. Several proteins that have been associated with acid-stress and iron-starvation stress were downregulated in Δhpyaxvii cells. This study provides a holistic understanding of M.HpyAXVII, a phasevarion from H. pylori 26695. The phase variable switching from a truncated, inactive DNA MTase to a functional, full-length DNA MTase has been shown before in Haemophilus influenzae strain Rd (ModA) and Helicobacter pylori strain P12 (ModH5). However, this is the first study where the biochemical and enzyme kinetic properties of such a phase variable DNA MTase have been elucidated.
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Lane, Michael. "Biochemical and molecular characterisation of FliI and FliH from Helicobacter pylori : a thesis presented in partial fulfilment of Doctor of Philosophy in Microbiology at the Institute of Molecular BioSciences, Massey University, Palmerston North, New Zealand." 2006. http://hdl.handle.net/10179/1579.

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The bacterium Helicobacter pylori is a human pathogen that infects a large proportion of the world's population and is associated with serious diseases such as gastric ulcers and adenocarcinoma. The motility of this organism, by virtue of sheathed polar flagella is essential to colonisation and persistence in the human host. The sequencing of the H. pylori genome in 1996 identified homologues of the majority of the flagellar genes found in S. enterica serovai typhimurium. These included genes encoding the flagellum ATPase, FliI and FliH a presumptive inhibitor, the primary focus of this study. Sequencing did not originally identify an H. pylori homologue of the flagellar chaperone FliJ, and this is also considered in this study. Bioinformatic analysis and modeling suggests a structural and functional relationship between FliI and homologues such as F1-ATPase α- and β-subunit. In particular, residues 2-91 of FliI resemble the N-terminal domain of the F1-ATPase α- and β-subunits. Biochemical analyses reported in this thesis showed that a truncated FliI-(2- 91) protein was folded, although the N-terminal 18 residues were likely unstructured. Furthermore, deletion mutagenesis showed that this disordered segment of the protein mediates interaction with FliH and very likely forms an amphipathic α-helix upon forming of the FliI-FliH complex. The scanning mutagenesis of this interaction segment of FliI identified a cluster of conserved hydrophobic residues that was critical for the interaction with FliH. Thus, the interaction between FliI and FliH has similarities to the interaction between the N-terminal α-helix of the α-subunit and the globular domain of the δ-subunit of the F1-ATPase. This similarity suggests that FliH, by analogy with the δ-subunit of the F1-ATPase, may function as a molecular stator of the flagellum. The findings presented above have been published (96). The function of a putative H. pylori FliJ homologue, HP0256, was also investigated by knock-out mutagenesis. Disruption of this gene does not abolish flagellar assembly, however further research continued beyond this thesis showed that the knock-out mutant results in impaired motility.
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Book chapters on the topic "Human Pathogen Helicobacter"

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Ahmed, Niyaz, Singamaneni Haritha Devi, Shivendra Tenguria, Mohammad Majid, Syed Asad Rahman, and Seyed E. Hasnain. "Genomic Fluidity of the Human Gastric Pathogen Helicobacter pylori." In Genome Plasticity and Infectious Diseases, 27–43. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555817213.ch3.

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Fischer, Wolfgang, Sandra Prassl, and Rainer Haas. "Virulence Mechanisms and Persistence Strategies of the Human Gastric Pathogen Helicobacter pylori." In Current Topics in Microbiology and Immunology, 129–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-01846-6_5.

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Roncarati, Davide, and Vincenzo Scarlato. "Roles and Regulation of the Heat Shock Proteins of the Major Human Pathogen Helicobacter pylori." In Regulation of Heat Shock Protein Responses, 411–27. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-74715-6_17.

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Challa, Surekha, and Nageswara Rao Reddy Neelapu. "Association Between Horizontal Gene Transfer and Adaptation of Gastric Human Pathogen Helicobacter pylori to the Host." In Horizontal Gene Transfer, 257–67. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-21862-1_10.

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Fox, J. G. "Hepatobiliary Helicobacters: recognized animal pathogens with suspected pathogenic potential in humans." In Helicobacter pylori, 83–104. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-011-3927-4_10.

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Fox, James G. "Helicobacter Species other than Helicobacter pylori: Emerging Pathogens in Humans and Animals." In Emerging Infections 4, 121–35. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555816971.ch9.

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Kelly, David J. "The Physiology and Metabolism of the Human Gastric Pathogen Helicobacter pylori." In Advances in Microbial Physiology, 137–89. Elsevier, 1998. http://dx.doi.org/10.1016/s0065-2911(08)60131-9.

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Syahniar, Rike, Dayu Swasti Kharisma, and Rayhana. "Helicobacter pylori Challenge Vaccine for Humans." In Vaccine Development. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.101157.

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Helicobacter pylori infect during childhood and are typically present for life, despite a vigorous host immune response, which includes the invading pathogen being coated with antibodies. This bacterial longevity indicates the development, on the part of the pathogen, of a range of processes for evading effective host immunity. Since its discovery 25 years ago, significant progress has been made in understanding the virulence factors and several aspects of the pathogenesis of H. pylori gastric diseases. The prevalence of antimicrobial drug resistance is so high that all patients infected with H. pylori should be considered resistant infections. The most severe consequence of H. pylori infection, and the key reason a vaccine is required, is gastric cancer, globally the third leading cause of death due to cancer. Patients typically present with gastric cancer without knowing they are infected; eradication likely has little effect by this time. Vaccine against H. pylori that reduces the incidence of gastric cancer will probably be cost effective in developed countries. Several vaccines were successfully tested in different experimental animal models, but translation into an efficacious human vaccine has been unsuccessful.
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Jain, Sunil K., Kuldeep Rajpoot, K. Kesavan, Awesh Yadav, Umesh Gupta, and Prem N. Gupta. "Targeting Potential of Nanocarriers for Efficient Treatment of H. Pylori Infection." In Nanoparticles and Nanocarriers-Based Pharmaceutical Formulations, 157–74. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815049787122010008.

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Helicobacter pylori (H. pylori), a prevalent human-specific pathogen, plays a key role in the development of peptic ulcer disease, gastric carcinoma, and gastric mucosa associated lymphoid tissue lymphoma. Once infected, those bacteria reside below the gastric mucosa adherent to the gastric epithelium, and entry of drugs to this target site is very difficult. The bacteria can also acquire resistance to commonly used antimicrobial drugs. Thus, an effective antimicrobial concentration cannot be achieved in the gastric mucous layer or on the epithelial cell surfaces where H. pylori exist and caused inefficient treatment. Such challenges have encouraged researchers into developing some therapies based on nanotechnology.
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Makristathis, Athanasios, and Alexander Hirschl. "Helicobacter." In Molecular Detection of Human Bacterial Pathogens, 1141–51. CRC Press, 2011. http://dx.doi.org/10.1201/b10848-105.

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Conference papers on the topic "Human Pathogen Helicobacter"

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Gao, Yali, Philip M. Sherman, Yu Sun, and Dongqing Li. "Multiplexed High-Throughput Electrokinetically-Controlled Immunoassay on a Chip for the Detection of Specific Bacterial Antibodies in Human Serum." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42512.

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This work presents a multiplexed electrokinetically-controlled heterogeneous immunoassay that can process ten samples in parallel. The immunoassay microchip was soft-lithographically fabricated using poly(dimethylsiloxane) and glass. Controlling parameters of the electrokinetically-driven flow in the microfluidic network was determined by numerically simulating transport processes. Multiple passively adsorbed antigens captured antibodies present in samples, which then bound with TRITC-labeled detection antibodies to generate fluorescent signals. Antibodies against Escherichia coli O157:H7 and Helicobacter pylori were studied as model analytes. After conditions for antigen-coating were optimized, a 24-minute assay detected E. coli O157:H7 antibody in the concentration range of 0.02–10 μg/mL, and H. pylori antibody in the range of 0.1–50 μg/mL. In testing human serum samples, non-specific binding of serum components was effectively suppressed by using 10% (w/v) bovine serum albumin. An accuracy of 100% was achieved in detecting either E. coli O157:H7 antibody or H. pylori antibody from human serum samples. Simultaneous screening of both antibodies was also successfully demonstrated. The immunoassay chip shows an excellent potential for efficiently detecting multiple pathogenic infections in clinical environments.
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