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A comparison of Helicobacter pylori and non-Helicobacter pylori Helicobacter spp. Binding to Canine Gastric Mucosa with Defined Gastric Glycophenotype
- Source :
- Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP
- Publication Year :
- 2014
- Publisher :
- Wiley, 2014.
-
Abstract
- Background: The gastric mucosa of dogs is often colonized by non-Helicobacter pylori helicobacters (NHPH), while H. pylori is the predominant gastric Helicobacter species in humans. The colonization of the human gastric mucosa by H. pylori is highly dependent on the recognition of host glycan receptors. Our goal was to define the canine gastric mucosa glycophenotype and to evaluate the capacity of different gastric Helicobacter species to adhere to the canine gastric mucosa. Materials and Methods: The glycosylation profile in body and antral compartments of the canine gastric mucosa, with focus on the expression of histo-blood group antigens was evaluated. The in vitro binding capacity of FITC-labeled H. pylori and NHPH to the canine gastric mucosa was assessed in cases representative of the canine glycosylation pattern. Results: The canine gastric mucosa lacks expression of type 1 Lewis antigens and presents a broad expression of type 2 structures and A antigen, both in the surface and glandular epithelium. Regarding the canine antral mucosa, H. heilmannii s.s. presented the highest adhesion score whereas in the body region the SabA-positive H. pylori strain was the strain that adhered more. Conclusions: The canine gastric mucosa showed a glycosylation profile different from the human gastric mucosa suggesting that alternative glycan receptors may be involved in Helicobacter spp. binding. Helicobacter pylori and NHPH strains differ in their ability to adhere to canine gastric mucosa. Among the NHPH, H. heilmannii s.s. presented the highest adhesion capacity in agreement with its reported colonization of the canine stomach. We kindly thank Prof. Thomas Boren from the Department of Medical Biochemistry and Biophysics, Umea University, Sweden for providing the 17875/Leb and 17875babA1A2H. pylori strains. The authors thank Dr. Fernando Rodrigues, Dr. Ana Laura Saraiva, and Cristina Bacelar who kindly provided technical support. I. Amorim (SFRH/BD/76237/2011) and A. Magalhães (SFRH/BPD/75871/2011) acknowledge FCT for financial support. This study was partially funded by the Portuguese Foundation for Science and Technology (PTDC/CTM-BPC/121149/2010; PTDC/CVT/117610/2010; PTDC/BBB-EBI/0786/2012). The Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP) is an Associate Laboratory of the Portuguese Ministry of Science, Technology and Higher Education and is partially supported by FCT.
- Subjects :
- Glycosylation
040301 veterinary sciences
Histocompatibility Antigens/chemistry
Bacterial Adhesion
Microbiology
0403 veterinary science
03 medical and health sciences
Dogs
Antigen
Polysaccharides
Helicobacter
Histocompatibility Antigens
medicine
Gastric mucosa
Polysaccharides/analysis
Animals
Receptor
Antrum
030304 developmental biology
0303 health sciences
biology
Gastric Mucosa/chemistry
Stomach
digestive, oral, and skin physiology
Gastroenterology
04 agricultural and veterinary sciences
General Medicine
Helicobacter pylori
biology.organism_classification
Gastric Mucosa/microbiology
Helicobacter/physiology
digestive system diseases
3. Good health
Infectious Diseases
medicine.anatomical_structure
Gastric Mucosa
Body region
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP
- Accession number :
- edsair.doi.dedup.....7d7ebe084ee4626ea8c6ad275474325d