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Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli
T J Baldwin1, S F Brooks, S Knutton
1Department of Genetics, University of Leicester, United Kingdom.
Abstract:
Infection of HEp-2 monolayers with enteropathogenic Escherichia coli 2036-80 (O119) stimulated phosphorylation of several target cell proteins, the most prominent of which had apparent molecular weights of 21,000 and 29,000. Proteins of the same size were phosphorylated in response to known activators of the calcium-phospholipid-dependent protein kinase C. Screening of clinical isolates of various O serogroups revealed that all strains able to form the characteristic attaching and effacing lesion of enteropathogenic E. coli showed elevated phosphorylation of 21,000- and 29,000-dalton protein species.
Insights
Enteropathogenic Escherichia coli infection triggers specific protein phosphorylation in host cells. This cellular response involves 21,000 and 29,000-dalton proteins, crucial for forming attaching and effacing lesions.
Area of Science:
- Microbiology
- Cell Biology
- Molecular Biology
Background:
- Enteropathogenic Escherichia coli (EPEC) is a significant cause of diarrheal disease.
- EPEC infection involves the formation of attaching and effacing (A/E) lesions on host intestinal cells.
- Host cell signaling pathways are activated during bacterial infection.
Purpose of the Study:
- To investigate host cell protein phosphorylation changes induced by EPEC infection.
- To identify specific host proteins targeted by EPEC.
- To correlate protein phosphorylation with the formation of A/E lesions.
Main Methods:
- Infection of HEp-2 cell monolayers with EPEC strain 2036-80 (O119).
- Analysis of protein phosphorylation using techniques to determine molecular weights.
- Screening of clinical EPEC isolates for phosphorylation patterns.
Main Results:
- EPEC infection stimulated the phosphorylation of host cell proteins, notably those with molecular weights of 21,000 and 29,000.
- Phosphorylation of these proteins mimicked responses to activators of protein kinase C.
- All EPEC strains capable of forming A/E lesions exhibited elevated phosphorylation of the 21,000- and 29,000-dalton proteins.
Conclusions:
- EPEC infection induces specific host cell protein phosphorylation events.
- The phosphorylation of 21,000- and 29,000-dalton proteins is associated with EPEC's ability to form A/E lesions.
- Protein kinase C pathways may be involved in the host response to EPEC infection.