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Updated: Sep 27, 2026

A Fluorescence-based Method to Study Bacterial Gene Regulation in Infected Tissues
Published on: February 19, 2019
Modulation of EGF receptor autophosphorylation by alpha-hemolysin of Staphylococcus aureus via protein tyrosine
Sharma Vandana1, Sangha Navneet, Kaur Surinder
1National Center for Cell Science, Ganeshkind Road, Pune 411 007, India.
Abstract:
In the presence of assembled alpha-hemolysin (alpha-HL) of Staphylococcus aureus, the epidermal growth factor receptor (EGFr) is rapidly dephosphorylated. Several obvious possibilities that otherwise would have contributed to the dephosphorylation were ruled out. Instead, an elevation in the activity of a protein tyrosine phosphatase appears to be responsible for the observed loss of phosphorylation signal of EGFr. For this dephosphorylation, the assembly of alpha-HL is necessary while lytic pore formation is not required. In summary, the EGFr is unable to retain its phosphorylation signal in the presence of alpha-HL and the process is irreversible.
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