TITLE

Human peripheral and gastric lymphocyte responses to Helicobacter pylori NapA and AphC differ in infected and uninfected individuals

AUTHOR(S)
Windle, H. J.; Ang, Y. S.; Morales, V. A.; McManus, R.; Kelleher, D.
PUB. DATE
January 2005
SOURCE
Gut;Jan2005, Vol. 54 Issue 1, p25
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Background: In this study, we identify the nature of the immunological response of human peripheral blood mononuclear cells (PBMC) and lamina propria gastric lymphocytes (IPI) to two Helicobacter pylon antigens, the neutrophil activating protein (NapA) and alkyl hydroperoxide reductase (AphC). These antigens were identified and selected for study based on the observation that serological recognition of these proteins was associated with H pylori negative status in humans. Aims: The aim was to study the serological, proliferative, and cytokine responses of PBMC and LPL obtained from H pylon infected and uninfected individuals, to these antigens. Methods: Patient serum, PBMC, and LPL were used to determine antibody isotype, and proliferative and cytokine responses to recombinant forms of NapA and AphC using western blotting and ELISA. Results: Western blotting revealed antibody reactivity to recombinant NapA and AphC among the H pylon negative population studied. Both the proliferative and interferon y responses of PBMC and LPL to NapA and AphC were significantly higher in H pylon negative compared with H pylon positive subjects. Analysis of the lgG subclass profiles to both antigens revealed a T helper 1 associated IgG3 antibody response in uninfected individuals. However, interleukin 10 production was greater in H pylon positive individuals in response to these antigens. Conclusions: Taken together these data are consistent with an immune response to these antigens skewed towards a T helper 1 response in the uninfected cohort.
ACCESSION #
16163221

 

Related Articles

  • The protein-protein interaction map of Helicobacter pylori. Rain, Jean-Christopher; Selig, Luc; De Reuse, Hilde; Battaglia, Veronique; Reverdy, Celine; Simon, Stephane; Lenzen, Gerlinde; Petel, Fabien; Wojcik, Jerome; Schachter, Vincent; Chemama, Y.; Labigne, Agnes; Legrain, Pierre // Nature;1/11/2001, Vol. 409 Issue 6817, p211 

    Reports on the construction of a large-scale protein-protein interaction map of the human gastric pathogen Helicobacter pylori. Importance of developing reliable proteome-wide approaches for a better understanding of protein function; Description of the map, which provides the assignment of...

  • Helicobacter pylori vaccines and mechanisms of effective immunity: Is mucus the key? Sutton, P; Sutton, Philip // Immunology & Cell Biology;Feb2001, Vol. 79 Issue 1, p67 

    Summary In this theoretical article, the hypothesis is proposed that immunization against gastric helicobacter infection is mediated by CD4+ T-cell induced changes in mucus production. Vaccine development for the gastric pathogen Helicobacter pylori has encountered several problems. Resolving...

  • Persistent Helicobacter pylori Specific Th17 Responses in Patients with Past H. pylori Infection Are Associated with Elevated Gastric Mucosal IL-1β. Victoria Serelli-Lee; Khoon Lin Ling; Cassandra Ho; Lai Han Yeong; Gek Keow Lim; Bow Ho; Soon Boon Justin Wong // PLoS ONE;Jun2012, Vol. 7 Issue 6, p1 

    Background: Ongoing Helicobacter pylori (HP) infection triggers a chronic active gastritis. Eradicating HP reduces gastric inflammation, but does not eliminate it. We sought to characterize this persistent gastritis, and demonstrate the persistence of HP-specific Th17 responses in individuals...

  • The zinc-ribbon domain of Helicobacter pylori HP0958: requirement for RpoN accumulation and possible roles of homologs in other bacteria.  // Microbial Informatics & Experimentation;2011, Vol. 1 Issue 1, p8 

    The article discusses a study which suggests the importance of the zinc-ribbon domain of FlgZ in protecting Helicobacter pylori HP0958 protein RpoN from turnover. The study concluded that DUF164 proteins are widespread among bacteria, but the functions of these proteins are virtually unknown. It...

  • Concurrent Proinflammatory and Apoptotic Activity of a Helicobacter pylori Protein (HP986) Points to Its Role in Chronic Persistence. Alvi, Ayesha; Ansari, Suhail A.; Ehtesham, Nasreen Z.; Rizwan, Mohammed; Devi, Savita; Sechi, Leonardo A.; Qureshi, Insaf A.; Hasnain, Seyed E.; Ahmed, Niyaz // PLoS ONE;2011, Vol. 6 Issue 7, p1 

    Helicobacter pylori induces cytokine mediated changes in gastroduodenal pathophysiology, wherein, the activated macrophages at the sub-mucosal space play a central role in mounting innate immune response against the antigens. The bacterium gains niche through persistent inflammation and local...

  • Oral immunization against Helicobacter pylori--a future concept. Michetti, Pierre // Journal of Gastroenterology;1998 Supplement 10, Vol. 33, p66 

    The demonstration that oral immunization with lysates of Helicobacter or with Helicobacter pylori urease can protect mice against H. felis infection opened the field of vaccine development against Helicobacter infections. More recently, the same antigen preparations were used successfully as a...

  • The Immune Response to Helicobacter pylori. Ihan, Alojz; Gubina, Marija // Food Technology & Biotechnology;Apr-Jun2014, Vol. 52 Issue 2, p204 

    The immune response to Helicobacter pylori involves different mechanisms that are both protective and damaging to the host. The innate and the adaptive immune responses lead to inflammatory as well as anti-inflammatory responses, allowing for persistence of many infections. Thus, developing new...

  • NMR Solution Structure of HP0827 (O25501_HELPY) from Helicobacter pylori: Model of the Possible RNA-binding Site. Sun-Bok Jang; Chao Ma; Ji-Yoon Lee; Ji-Hun Kim; Park, Sung Jean; Ae-Ran Kwon; Bong-Jin Lee // Journal of Biochemistry;Nov2009, Vol. 146 Issue 5, p667 

    The HP0827 protein is an 82-residue protein identified as a putative ss-DNA-binding protein 12RNP2 Precursor from Helicobacter pylori. Here, we have determined 3D structure of HP0827 using Nuclear Magnetic Resonance. It has a ferredoxin-like fold,...

  • Signalling pathways and molecular interactions of NOD1 and NOD2. Strober, Warren; Murray, Peter J.; Kitani, Atsushi; Watanabe, Tomohiro // Nature Reviews Immunology;Jan2006, Vol. 6 Issue 1, p9 

    The NOD (nucleotide-binding oligomerization domain) proteins NOD1 and NOD2 have important roles in innate immunity as sensors of microbial components derived from bacterial peptidoglycan. The importance of these molecules is underscored by the fact that mutations in the gene that encodes NOD2...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sign out of this library

Other Topics