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PMID: 8577751 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Helicobacter pylori attachment to gastric cells induces cytoskeletal rearrangements and tyrosine phosphorylation of host cell proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 3 ·1996-02-06 ·Pages 1259-64

Segal ED, Falkow S, Tompkins LS

Abstract

The consequences of Helicobacter pylori attachment to human gastric cells were examined by transmission electron microscopy and immunofluorescence microscopy. H. pylori attachment resulted in (i) effacement of microvilli at the site of attachment, (ii) cytoskeletal rearrangement directly beneath the bacterium, and (iii) cup/pedestal formation at the site of attachment. Double-immunofluorescence studies revealed that the cytoskeletal components actin, alpha-actinin, and talin are involved in the process. Immunoblot analysis showed that binding of H. pylori to AGS cells induced tyrosine phosphorylation of two host cell proteins of 145 and 105 kDa. These results indicate that attachment of H. pylori to gastric epithelial cells resembles that of enteropathogenic Escherichia coli. Coccoid H. pylori, which are thought to be terminally differentiated bacterial forms, are capable of binding and inducing cellular changes of the same sort as spiral H. pylori, including tyrosine phosphorylation of host proteins.

MeSH Terms
Adenocarcinoma Bacterial Adhesion Cell Line Cytoskeletal Proteins/metabolism Cytoskeleton/microbiology,ultrastructure Escherichia coli/pathogenicity Fluorescent Antibody Technique Helicobacter pylori/pathogenicity,physiology,ultrastructure Humans Microscopy, Confocal Microscopy, Electron Microscopy, Immunoelectron Microvilli/microbiology,ultrastructure Phosphoproteins/analysis,metabolism Phosphorylation Phosphotyrosine/analysis Stomach Neoplasms Tumor Cells, Cultured Tyrosine/metabolism
Chemicals
Cytoskeletal Proteins Phosphoproteins Phosphotyrosine Tyrosine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Segal E D
Department of Microbiology and Immunology, Stanford University School of Medicine, CA 94305, USA.
Falkow S
Tompkins L S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.3.1259
Published
1996-02-06
Pages
1259-64
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC40067
Subset
IM
Grants
NIAID NIH HHS · AI23796 · United States
NIDDK NIH HHS · DK 38707 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.3.1259 PMC Full Text View journal details
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