scholarly journals Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695

2004 ◽  
Vol 186 (4) ◽  
pp. 949-955 ◽  
Author(s):  
Seung-Chul Baik ◽  
Kyung-Mi Kim ◽  
Su-Min Song ◽  
Do-Su Kim ◽  
Jin-Su Jun ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Proteins ◽  
Immunoblot Analysis ◽  
Outer Membrane Fraction ◽  
Flight Mass Spectrometry ◽  
Molecular Masses ◽  
H Pylori

ABSTRACT Helicobacter pylori causes gastroduodenal disease, which is mediated in part by its outer membrane proteins (OMPs). To identify OMPs of H. pylori strain 26695, we performed a proteomic analysis. A sarcosine-insoluble outer membrane fraction was resolved by two-dimensional electrophoresis with immobilized pH gradient strips. Most of the protein spots, with molecular masses of 10 to 100 kDa, were visible on the gel in the alkaline pI regions (6.0 to 10.0). The proteome of the OMPs was analyzed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Of the 80 protein spots processed, 62 spots were identified; they represented 35 genes, including 16 kinds of OMP. Moreover, we identified 9 immunoreactive proteins by immunoblot analysis. This study contributes to the characterization of the H. pylori strain 26695 proteome and may help to further elucidate the biological function of H. pylori OMPs and the pathogenesis of H. pylori infection.

scholarly journals Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695

2005 ◽  
Vol 187 (4) ◽  
pp. 1541-1541
Author(s):  
Seung-Chul Baik ◽  
Kyung-Mi Kim ◽  
Su-Min Song ◽  
Do-Su Kim ◽  
Jin-Su Jun ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

Proteomic analysis of the sarcosine-insoluble outer membrane fraction of the bacterial pathogenBartonella henselae

2007 ◽  
pp. 203-224
Author(s):  
Thomas A. Rhomberg ◽  
Olof Karlberg ◽  
Thierry Mini ◽  
Ursula Zimny-Arndt ◽  
Ulrika Wickenberg ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction

scholarly journals Genome-wide mutation analysis of Helicobacter pylori after inoculation to Mongolian gerbils

Gut Pathogens ◽  
2019 ◽  
Vol 11 (1) ◽  
Author(s):  
Rumiko Suzuki ◽  
Kazuhito Satou ◽  
Akino Shiroma ◽  
Makiko Shimoji ◽  
Kuniko Teruya ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Human Stomach ◽  
Next Generation Sequencing Data ◽  
Mongolian Gerbils ◽  
New Host ◽  
Model Animal ◽  
H Pylori

Abstract Background Helicobacter pylori is a pathogenic bacterium that causes various gastrointestinal diseases in the human stomach. H. pylori is well adapted to the human stomach but does not easily infect other animals. As a model animal, Mongolian gerbils are often used, however, the genome of the inoculated H. pylori may accumulate mutations to adapt to the new host. To investigate mutations occurring in H. pylori after infection in Mongolian gerbils, we compared the whole genome sequence of TN2 wild type strain (TN2wt) and next generation sequencing data of retrieved strains from the animals after different lengths of infection. Results We identified mutations in 21 loci of 17 genes of the post-inoculation strains. Of the 17 genes, five were outer membrane proteins that potentially influence on the colonization and inflammation. Missense and nonsense mutations were observed in 15 and 6 loci, respectively. Multiple mutations were observed in three genes. Mutated genes included babA, tlpB, and gltS, which are known to be associated with adaptation to murine. Other mutations were involved with chemoreceptor, pH regulator, and outer membrane proteins, which also have potential to influence on the adaptation to the new host. Conclusions We confirmed mutations in genes previously reported to be associated with adaptation to Mongolian gerbils. We also listed up genes that mutated during the infection to the gerbils, though it needs experiments to prove the influence on adaptation.

scholarly journals Role of the Helicobacter pylori outer-membrane proteins AlpA and AlpB in colonization of the guinea pig stomach

2004 ◽  
Vol 53 (5) ◽  
pp. 375-379 ◽  
Author(s):  
Ramon de Jonge ◽  
Zarmina Durrani ◽  
Sjoerd G. Rijpkema ◽  
Ernst J. Kuipers ◽  
Arnoud H.M. van Vliet ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Membrane Proteins ◽  
Guinea Pig ◽  
Outer Membrane ◽  
Type Strain ◽  
Wild Type Strain ◽  
Outer Membrane Proteins ◽  
Wild Type ◽  
H Pylori

The human gastric pathogen Helicobacter pylori expresses several putative outer-membrane proteins (OMPs), but the role of individual OMPs in colonization of the stomach by H. pylori is still poorly understood. The role of four such OMPs (AlpA, AlpB, OipA and HopZ) in a guinea pig model of H. pylori infection has been investigated. Single alpA, alpB, hopZ and oipA isogenic mutants were constructed in the guinea pig-adapted, wild-type H. pylori strain GP15. Guinea pigs were inoculated intragastrically with the wild-type strain, single mutants or a mixture of the wild-type and a single mutant in a 1 : 1 ratio. Three weeks after infection, H. pylori could be isolated from stomach sections of all animals that were infected with the wild-type, the hopZ mutant or the oipA mutant, but from only five of nine (P = 0.18) and one of seven (P = 0.02) animals that were infected with the alpA or alpB mutants, respectively. The hopZ and oipA mutants colonized the majority of animals that were inoculated with the strain mixture, whereas alpA and alpB mutants could not be isolated from animals that were infected with the strain mixture (P < 0.01). Specific IgG antibody responses were observed in all animals that were infected with either the wild-type or a mutant, but IgG levels were lower in animals that were infected with either the alpA or the alpB mutants, compared to the wild-type strain (P < 0.05). In conclusion, absence of AlpA or AlpB is a serious disadvantage for colonization of the stomach by H. pylori.

scholarly journals Comparative Genomics of Helicobacter pylori: Analysis of the Outer Membrane Protein Families

2000 ◽  
Vol 68 (7) ◽  
pp. 4155-4168 ◽  
Author(s):  
Richard A. Alm ◽  
James Bina ◽  
Beth M. Andrews ◽  
Peter Doig ◽  
Robert E. W. Hancock ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Gene Families ◽  
Ancestral Gene ◽  
Related Function ◽  
Paralogous Family ◽  
H Pylori ◽  
Complete Genomic

ABSTRACT The two complete genomic sequences of Helicobacter pylori J99 and 26695 were used to compare the paralogous families (related genes within one genome, likely to have related function) of genes predicted to encode outer membrane proteins which were present in each strain. We identified five paralogous gene families ranging in size from 3 to 33 members; two of these families contained members specific for either H. pylori J99 or H. pylori26695. Most orthologous protein pairs (equivalent genes between two genomes, same function) shared considerable identity between the two strains. The unusual set of outer membrane proteins and the specialized outer membrane may be a reflection of the adaptation of H. pylori to the unique gastric environment where it is found. One subfamily of proteins, which contains both channel-forming and adhesin molecules, is extremely highly related at the sequence level and has likely arisen due to ancestral gene duplication. In addition, the largest paralogous family contained two essentially identical pairs of genes in both strains. The presence and genomic organization of these two pairs of duplicated genes were analyzed in a panel of independentH. pylori isolates. While one pair was present in every strain examined, one allele of the other pair appeared partially deleted in several isolates.

scholarly journals Outer Membrane Protein Expression Profile in Helicobacter pylori Clinical Isolates

2009 ◽  
Vol 77 (9) ◽  
pp. 3782-3790 ◽  
Author(s):  
Stefan Odenbreit ◽  
Kirstin Swoboda ◽  
Iris Barwig ◽  
Stefan Ruhl ◽  
Thomas Borén ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Outer Membrane ◽  
Expression Profiles ◽  
Outer Membrane Proteins ◽  
Infection Process ◽  
Clinical Isolates ◽  
Large Set ◽  
Associated Proteins ◽  
H Pylori ◽  
The Individual

ABSTRACT The gram-negative gastric pathogen Helicobacter pylori is equipped with an extraordinarily large set of outer membrane proteins (OMPs), whose role in the infection process is not well understood. The Hop (Helicobacter outer membrane porins) and Hor (Hop-related proteins) groups constitute a large paralogous family consisting of 33 members. The OMPs AlpA, AlpB, BabA, SabA, and HopZ have been identified as adhesins or adherence-associated proteins. To better understand the relevance of these and other OMPs during infection, we analyzed the expression of eight different omp genes (alpA, alpB, babA, babB, babC, sabA, hopM, and oipA) in a set of 200 patient isolates, mostly from symptomatic children or young adults. Virtually all clinical isolates produced the AlpA and AlpB proteins, supporting their essential function. All other OMPs were produced at extremely variable rates, ranging from 35% to 73%, indicating a function in close adaptation to the individual host or gastric niche. In 11% of the isolates, BabA was produced, and SabA was produced in 5% of the isolates, but the strains failed to bind their cognate substrates. Interleukin-8 (IL-8) expression in gastric cells was strictly dependent on the presence of the cag pathogenicity island, whereas the presence of OipA clearly enhanced IL-8 production. The presence of the translocated effector protein CagA correlated well with BabA and OipA production. In conclusion, we found unexpectedly diverse omp expression profiles in individual H. pylori strains and hypothesize that this reflects the selective pressure for adhesion, which may differ across different hosts as well as within an individual over time.

scholarly journals Antigenic Properties of HpaA and Omp18, Two Outer Membrane Proteins of Helicobacter pylori

2003 ◽  
Vol 71 (7) ◽  
pp. 3837-3843 ◽  
Author(s):  
Petra Voland ◽  
Nadia Hafsi ◽  
Marco Zeitner ◽  
Stephanie Laforsch ◽  
Hermann Wagner ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Dendritic Cells ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Mononuclear Cells ◽  
Human Peripheral Blood ◽  
Outer Membrane Proteins ◽  
Interleukin 12 ◽  
Antigenic Properties ◽  
H Pylori

ABSTRACT Outer membrane proteins (OMPs) are incorporated into the outer plasma membrane of Helicobacter pylori and are important for, e.g., ion transport, adherence, structural and osmotic stability, and bacterial virulence but may also be antigenic due to their surface exposure. Previous proteome-based approaches with H. pylori lysates determined a strong serological reaction towards two H. pylori OMPs, HpaA (TIGR HP0797) and Omp18 (TIGR HP1125). PCR was used to detect DNA encoding the two proteins, and a positive signal was found in all H. pylori strains tested. Proteins were cloned and expressed in the human kidney cell line HK293 with the QiaExpressionist system with a C-terminal His tag. Only sera from infected persons showed a positive reaction with the recombinant proteins. Recombinant HpaA (rHpaA) and rOmp18 were incubated with human peripheral blood mononuclear cells and induced secretion of interleukin-12 (IL-12) and IL-10 from these cells. To determine the effect on antigen-presenting cells, human blood monocytic and dendritic cells (DCs) were isolated by magnetic cell separation. rOmp18 and rHpaA strongly stimulated major histocompatibility class II and CD83 expression 7- to 10-fold on isolated DCs. rHpaA and rOmp18 failed to stimulate IL-8 secretion from monocytes but increased secretion of IL-12 and IL-10 from DCs significantly. In summary, HpaA and Omp18 are recognized by human dendritic cells and induce their maturation as well as antigen presentation. HpaA and Omp18 of H. pylori thereby appear to have a specific antigenic potential in humans.

Proteomic analysis of the sarcosine-insoluble outer membrane fraction of the bacterial pathogenBartonella henselae

PROTEOMICS ◽  
2004 ◽  
Vol 4 (10) ◽  
pp. 3021-3033 ◽  
Author(s):  
Thomas A. Rhomberg ◽  
Olof Karlberg ◽  
Thierry Mini ◽  
Ursula Zimny-Arndt ◽  
Ulrika Wickenberg ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Proteomic Analysis ◽  
Membrane Fraction ◽  
Outer Membrane Fraction
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