Тип публикации: статья из журнала
Год издания: 2016
Идентификатор DOI: 10.1016/j.micpath.2016.01.005
Ключевые слова: Adenocarcinoma, cagPAI, T4SS, EPIYA, Crystal structure, Integrin alpha 5 beta 1, Phosphatidylserine, Integrin ?5?1, bacterial protein, cytotoxin associated gene A, unclassified drug, bacterial virulence, cancer growth, carcinogenesis, disease association, epithelium cell, Helicobacter infection, Helicobacter pylori, human, nonhuman, pathogenesis, pathogenicity island, priority journal, protein function, protein interaction, protein localization, protein targeting, Review, stomach cancer, structure activity relation, structure analysis, type IV secretion system
Аннотация: Helicobacter pylori has been described as the main etiologic agent of gastric cancer, causing a considerable rate of mortality and morbidity in human population across the world. Although the infection mainly begins asymptomatically, but simply develops to peptic ulcer, chronic gastritis, lymphoma of the gastric mucosa and eventualПоказать полностьюly adenocarcinoma. The major pathological feature of H. pylori infection is due to the activity of the cytotoxin-associated gene A (CagA), a 125-140 kDa protein encoded by the cag pathogenicity island (cagPAI). CagA is also known as the first bacterial onco-protein, ranking the H. pylori-mediated adenocarcinoma as the second most deadly cancer type worldwide. Upon cytoplasmic translocation CagA undergoes interacting with numerous proteins in phosphorylation dependant and independent manners within the gastric epithelial cells. The profound effect of CagA on multiple intracellular pathways causes major consequences such as perturbation of intracellular actin trafficking, stimulation of inflammatory responses and disruption of cellular tight junctions. Such activities of CagA further participate in development of the hummingbird phenotype and gastric cancer. This review is sought to provide a structural and functional analysis of the CagA protein with focus on demonstrating the molecular basis of the mechanism of CagA intracellular translocation and its interaction with intracellular targets. (C) 2016 Elsevier Ltd. All rights reserved.
Журнал: MICROBIAL PATHOGENESIS
Выпуск журнала: Vol. 93
Номера страниц: 44-55
ISSN журнала: 08824010
Место издания: LONDON
Издатель: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD