Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli

作者：Thomas J. Baldwin, Susan F. Brooks, Stuart Knutton, H. Hernández, A. Aitken, PETER H. WILLIAMS · 发表于：Infection and Immunity · 年份：1990 · DOI：10.1128/iai.58.3.761-765.1990 · 被引用次数：69 · 研究领域：Glycosylation and Glycoproteins Research、Escherichia coli research studies、RNA and protein synthesis mechanisms

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.