scholarly journals Age-Specific Immune Response to HspA in Helicobacter pylori-Positive Persons in Mexico

2004 ◽  
Vol 11 (5) ◽  
pp. 983-985 ◽  
Author(s):  
Peter P. Eamranond ◽  
Javier Torres ◽  
Onofre Muñoz ◽  
Guillermo I. Pérez-Pérez
Keyword(s):  
Immune Response ◽  
Developing Countries ◽  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A ◽  
Developed Countries ◽  
Enzyme Linked Immunosorbent Assay ◽  
Specific Enzyme ◽  
Or In Developing Countries

ABSTRACT The immune response to heat shock protein A (HspA) in Helicobacter pylori-positive adults increases with age in developed countries. This response has not been studied with children or in developing countries (G. I. Pérez-Pérez, J. M. Thiberge, A. Labigne, and M. J. Blaser, J. Infect. Dis. 174:1046-1050, 1996). As determined by using a specific enzyme-linked immunosorbent assay, HspA seropositivity among 592 individuals in Mexico was <10% in children and increased to >40% in adults.

scholarly journals Immune Response against a Cross-Reactive Epitope on the Heat Shock Protein 60 Homologue of Helicobacter pylori

2000 ◽  
Vol 68 (6) ◽  
pp. 3448-3454 ◽  
Author(s):  
Hiroyuki Yamaguchi ◽  
Takako Osaki ◽  
Masanori Kai ◽  
Haruhiko Taguchi ◽  
Shigeru Kamiya
Keyword(s):  
Escherichia Coli ◽  
Immune Response ◽  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Heat Shock Protein 60 ◽  
Epitope Region ◽  
H Pylori ◽  
Human Hsp60

ABSTRACT We previously established a monoclonal antibody (MAb), designated H9, which reacts with the heat shock protein 60 (HSP60) homologue ofHelicobacter pylori as well as with other bacterial and human HSP60s. To determine the importance of a cross-reactive epitope on H. pylori HSP60 in H. pyloriimmunopathogenesis, we performed (i) mapping of an epitope on H. pylori HSP60 recognized by the H9 MAb, (ii) analysis of immunoglobulin G responses of patients with or without H. pylori infection to its epitope region, and (iii) studies of the protective effect of immunization with its epitope region onH. pylori infection in mice. The epitope recognized by the H9 MAb was mapped to the sequence of amino acids 189 to 203 (VEGMQFDRGYLSPYF) on the H. pylori HSP60 molecule. It was confirmed that the synthesized peptide designated pH9 was recognized by the H9 MAb. Enzyme-linked immunosorbent assay analysis showed that patients with H. pylori infection (n = 349) had significantly lower titers of pH9 antibody than did uninfected patients (n = 200) (P < 0.001), but this was not the case with purified H. pylori HSP60 recombinant Escherichia coli GroEL, or recombinant human HSP60. In C57BL/6 mice immunized with the pH9 peptide with Freund's complete adjuvant (FCA), the number of H. pylori organisms colonizing the stomach was significantly lower than that in mice immunized with pCont plus FCA (P < 0.0001) or FCA only (P < 0.005). The results suggest that the immune response to the cross-reactive epitope (pH9 region) on H. pylori HSP60 is unique and might be associated with protection against H. pylori infection.

scholarly journals Immune response to heat shock protein of Helicobacter pylori -a candidate as a vaccine component

2002 ◽  
Vol 51 (supplement2) ◽  
pp. 24-25 ◽  
Author(s):  
Shigeru Kamiya ◽  
Takako Osaki ◽  
Haruhiko Taguchi ◽  
Hiroyuki Yamaguchi
Keyword(s):  
Immune Response ◽  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Vaccine Component

scholarly journals Immunization with Heat Shock Protein A and γ-Glutamyl Transpeptidase Induces Reduction on the Helicobacter pylori Colonization in Mice

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0130391 ◽  
Author(s):  
Xiaoli Zhang ◽  
Jinyong Zhang ◽  
Feng Yang ◽  
Weiru Wu ◽  
Heqiang Sun ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A ◽  
Glutamyl Transpeptidase

scholarly journals Cloning, expression and antigenic analysis of heat shock protein A gene of human Helicobacter pylori

2003 ◽  
Vol 11 (10) ◽  
pp. 1480-1484
Author(s):  
Zheng Jiang ◽  
Dan Pu ◽  
Ai-Long Huang ◽  
Xiao-Hong Tao ◽  
Pi-Long Wang
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A ◽  
Antigenic Analysis

scholarly journals Live Attenuated Measles Virus Vaccine Expressing Helicobacter pylori Heat Shock Protein A

2020 ◽  
Vol 19 ◽  
pp. 136-148
Author(s):  
Ianko D. Iankov ◽  
Cheyne Kurokawa ◽  
Kimberly Viker ◽  
Steven I. Robinson ◽  
Arun Ammayappan ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Virus Vaccine ◽  
Measles Virus ◽  
Protein A

scholarly journals Helicobacter pylori Heat Shock Protein A: Serologic Responses and Genetic Diversity

1999 ◽  
Vol 6 (3) ◽  
pp. 377-382 ◽  
Author(s):  
Enders K. W. Ng ◽  
Stuart A. Thompson ◽  
Guillermo I. Pérez-Pérez ◽  
Imad Kansau ◽  
Arie van der Ende ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Helicobacter Pylori ◽  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Sequence Variation ◽  
Protein A ◽  
Nucleotide Sequences ◽  
Serological Response ◽  
H Pylori

ABSTRACT Helicobacter pylori synthesizes an unusual GroES homolog, heat shock protein A (HspA). The present study was aimed at an assessment of the serological response to HspA in a group of Chinese patients with defined gastroduodenal pathologies and determination of whether diversity is present in the nucleotide sequences encoding HspA in isolates from these patients. Serum samples collected from 154 patients who had an upper gastrointestinal pathology and the presence of H. pylori defined by biopsy were tested for an immunoglobulin G (IgG) serologic response to H. pylori HspA by an enzyme linked immunosorbant assay. HspA-encoding nucleotide sequences in H. pylori isolates from 14 patients (7 seropositive and 7 seronegative for HspA) were analyzed by PCR and direct sequencing of the PCR products. The sequencing results were compared to those of 48 isolates from other parts of the world. Of the 154 known H. pylori-positive patients, 54 (35.1%) were seropositive for HspA. The A domain (GroES homology) of HspA was highly conserved in the 14 isolates tested. Although the B domain (metal-binding site unique to H. pylori) resembled that in the known major variant, particular amino acid substitutions allowed definition of an HspA variant associated with isolates from East Asia. There were no associations between patient characteristics and HspA seropositivity or amino acid sequences. We confirmed in this study that the clinical outcomes of H. pylori infection are not related to HspA antigenicity or to sequence variation. However, B-domain sequence variation may be a marker for the study of the genetic diversity of H. pylori strains of different geographic origins.

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