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Adherence properties of Helicobacter pylori: Impact on pathogenesis and adaptation to the host
The adherence of the human gastric pathogen Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the lar...
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Published in: | International journal of medical microbiology 2005-09, Vol.295 (5), p.317-324 |
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container_title | International journal of medical microbiology |
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description | The adherence of the human gastric pathogen
Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the large outer membrane protein (OMP) family of
H. pylori. Among these, the BabA protein was shown to recognize the Le
b antigen, which is presented as a dominant surface structure in the gastric mucosa. The SabA adhesin binds to sialylated antigens, which are up-regulated in inflamed gastric tissue. Other OMPs, such as AlpAB or HopZ were also shown to be involved in binding to gastric epithelial cells, but the corresponding receptors are unknown. The aim of this review is to summarize recent data giving new insights in binding specificities of
H. pylori adhesins and their role in pathogenesis and adaptation to the host. |
doi_str_mv | 10.1016/j.ijmm.2005.06.003 |
format | article |
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Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the large outer membrane protein (OMP) family of
H. pylori. Among these, the BabA protein was shown to recognize the Le
b antigen, which is presented as a dominant surface structure in the gastric mucosa. The SabA adhesin binds to sialylated antigens, which are up-regulated in inflamed gastric tissue. Other OMPs, such as AlpAB or HopZ were also shown to be involved in binding to gastric epithelial cells, but the corresponding receptors are unknown. The aim of this review is to summarize recent data giving new insights in binding specificities of
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Helicobacter pylori to the gastric mucosa is widely assumed to play a substantial role in initial colonization and long-term persistence in the human stomach. In the past, a couple of putative adhesins were identified, most of which were members of the large outer membrane protein (OMP) family of
H. pylori. Among these, the BabA protein was shown to recognize the Le
b antigen, which is presented as a dominant surface structure in the gastric mucosa. The SabA adhesin binds to sialylated antigens, which are up-regulated in inflamed gastric tissue. Other OMPs, such as AlpAB or HopZ were also shown to be involved in binding to gastric epithelial cells, but the corresponding receptors are unknown. The aim of this review is to summarize recent data giving new insights in binding specificities of
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H. pylori. Among these, the BabA protein was shown to recognize the Le
b antigen, which is presented as a dominant surface structure in the gastric mucosa. The SabA adhesin binds to sialylated antigens, which are up-regulated in inflamed gastric tissue. Other OMPs, such as AlpAB or HopZ were also shown to be involved in binding to gastric epithelial cells, but the corresponding receptors are unknown. The aim of this review is to summarize recent data giving new insights in binding specificities of
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source | ScienceDirect Journals |
subjects | Adaptation, Physiological Adherence Adhesins, Bacterial - physiology Animals Bacterial Adhesion - physiology Bacterial Outer Membrane Proteins - physiology Colonization Gastric Mucosa - microbiology Helicobacter Infections - microbiology Helicobacter pylori Helicobacter pylori - pathogenicity Helicobacter pylori - physiology Helicobacter pylori - ultrastructure Humans Lewis blood group antigens Outer membrane proteins |
title | Adherence properties of Helicobacter pylori: Impact on pathogenesis and adaptation to the host |
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