Protein Phosphorylation by Protein Kinase C in HEp-2 Cells Infected with Enteropathogenic Escherichia Coli

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 1990 Mar 1

PMID 2407656

Citations 35

Authors

T J Baldwin

S F Brooks

S Knutton

H A Manjarrez Hernandez

A Aitken

P H Williams

Affiliations

Soon will be listed here.

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.

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