Crystal structure of HP0721, a novel secreted protein from Helicobacter pylori

2011 ◽  
Vol 79 (5) ◽  
pp. 1678-1681 ◽  
Author(s):  
Gianluca Cioci ◽  
Laurent Terradot ◽  
Cyril Dian ◽  
Christoph Mueller-Dieckmann ◽  
Gordon Leonard
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Secreted Protein

scholarly journals Serological Assays for Identification of Human Gastric Colonization by Helicobacter pylori Strains Expressing VacA m1 or m2

2007 ◽  
Vol 14 (4) ◽  
pp. 442-450 ◽  
Author(s):  
Chandrabali Ghose ◽  
Guillermo I. Perez-Perez ◽  
Victor J. Torres ◽  
Marialuisa Crosatti ◽  
Abraham Nomura ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Asian American ◽  
Specific Antigen ◽  
Secreted Protein ◽  
Gastric Epithelial Cells ◽  
Allele Specific ◽  
Risk Of Disease ◽  
Specific Antigens ◽  
H Pylori ◽  
Development Of Gastric Cancer

ABSTRACT The Helicobacter pylori vacA gene encodes a secreted protein (VacA) that alters the function of gastric epithelial cells and T lymphocytes. H. pylori strains containing particular vacA alleles are associated with differential risk of disease. Because the VacA midregion may exist as one of two major types, m1 or m2, serologic responses may potentially be used to differentiate between patients colonized with vacA m1- or vacA m2-positive H. pylori strains. In this study, we examined the utility of specific antigens from the m regions of VacA as allele-specific diagnostic antigens. We report that serological responses to P44M1, an H. pylori m1-specific antigen, are observed predominantly in patients colonized with m1-positive strains, whereas responses to VacA m2 antigens, P48M2 and P55M2, are observed in patients colonized with either m1- or m2-positive strains. In an Asian-American population, serologic responses to VacA m region-specific antigens were not able to predict the risk of development of gastric cancer.

scholarly journals Structural Analysis of Variability and Interaction of the N-terminal of the Oncogenic Effector CagA of Helicobacter pylori with Phosphatidylserine

2018 ◽  
Vol 19 (10) ◽  
pp. 3273 ◽  
Author(s):  
Cindy Ulloa-Guerrero ◽  
Maria Delgado ◽  
Carlos Jaramillo
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Conservation Score ◽  
Intermolecular Forces ◽  
P Value ◽  
Cytotoxin Associated Gene A ◽  
Molecular Forces ◽  
Severe Pathology ◽  
Risk Of Cancer ◽  
Bulk Effect

Helicobacter pylori cytotoxin-associated gene A protein (CagA) has been associated with the increase in virulence and risk of cancer. It has been demonstrated that CagA’s translocation is dependent on its interaction with phosphatidylserine. We evaluated the variability of the N-terminal CagA in 127 sequences reported in NCBI, by referring to molecular interaction forces with the phosphatidylserine and the docking of three mutations chosen from variations in specific positions. The major sites of conservation of the residues involved in CagA–Phosphatidylserine interaction were 617, 621 and 626 which had no amino acid variation. Position 636 had the lowest conservation score; mutations in this position were evaluated to observe the differences in intermolecular forces for the CagA–Phosphatidylserine complex. We evaluated the docking of three mutations: K636A, K636R and K636N. The crystal and mutation models presented a ΔG of −8.919907, −8.665261, −8.701923, −8.515097 Kcal/mol, respectively, while mutations K636A, K636R, K636N and the crystal structure presented 0, 3, 4 and 1 H-bonds, respectively. Likewise, the bulk effect of the ΔG and amount of H-bonds was estimated in all of the docking models. The type of mutation affected both the ΔG ( χ 2 ( 1 ) = 93.82 , p-value < 2.2 × 10 − 16 ) and the H-bonds ( χ 2 ( 1 ) = 91.93 , p-value < 2.2 × 10 − 16 ). Overall, 76.9% of the strains that exhibit the K636N mutation produced a severe pathology. The average H-bond count diminished when comparing the mutations with the crystal structure of all the docking models, which means that other molecular forces are involved in the CagA–Phosphatidylserine complex interaction.

scholarly journals Crystal structure of JHP933 from Helicobacter pylori J99

2014 ◽  
Vol 70 (a1) ◽  
pp. C823-C823
Author(s):  
Sang Jae Lee ◽  
Ji Young Yoon ◽  
Bong-Jin Lee ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Peptic Ulcer ◽  
Functional Characterization ◽  
Domain Architecture ◽  
Structural Similarity ◽  
Terminal Domain ◽  
Plasticity Region ◽  
H Pylori ◽  
And Function

Helicobacter pylori infection is the main cause of chronic gastritis, gastric mucosal atrophy, peptic ulcer, and some forms of gastric cancer. There has been considerable interest in strain-specific genes found outside of the cag pathogenicity island, especially genes in the plasticity regions of H. pylori. In H. pylori strain J99, the plasticity region contains 48 genes ranging from jhp0914 to jhp0961. Because little is known about many of these genes in the plasticity region, further studies are necessary to elucidate their roles in H. pylori-associated pathogenesis. The JHP933 protein, encoded by the jhp0933 gene in the plasticity region of H. pylori J99, is one of the prevalently expressed proteins in some gastritis and peptic ulcer patients. However, its structure and function remain unknown. Here, we have determined the crystal structure of JHP933, revealing the first two-domain architecture of DUF1814 family. The N-terminal domain has the nucleotidyltransferase fold and the C-terminal domain is a helix bundle. Structural similarity of JHP933 to known nucleotidyltransferases is very remote, suggesting that it may function as a novel nucleotidyltransferase. It is expected that this study will facilitate functional characterization of JHP933 to obtain an insight into its role in pathogenesis by the H. pylori plasticity region.

Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori

2016 ◽  
Vol 194 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Ivana Pulić ◽  
Laura Cendron ◽  
Marco Salamina ◽  
Patrizia Polverino de Laureto ◽  
Dubravka Matković-Čalogović ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Human Pathogen

The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension

2008 ◽  
Vol 1784 (11) ◽  
pp. 1601-1606 ◽  
Author(s):  
Luciana Esposito ◽  
Anke Seydel ◽  
Rosa Aiello ◽  
Giosué Sorrentino ◽  
Laura Cendron ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Superoxide Dismutase ◽  
Helicobacter Pylori

scholarly journals Crystal structure of toxin HP0892 from Helicobacter pylori with two Zn(II) at 1.8 Å resolution

2014 ◽  
Vol 23 (6) ◽  
pp. 819-832 ◽  
Author(s):  
Hookang Im ◽  
Sun-Bok Jang ◽  
Chinar Pathak ◽  
Yeon-Jin Yang ◽  
Hye-Jin Yoon ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori

scholarly journals Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori

2003 ◽  
Vol 51 (4) ◽  
pp. 616-617 ◽  
Author(s):  
Byung Il Lee ◽  
Je Eun Kwak ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Type Ii
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