Format

Send to

Choose Destination
See comment in PubMed Commons below
PLoS Pathog. 2013;9(4):e1003325. doi: 10.1371/journal.ppat.1003325. Epub 2013 Apr 25.

The Chlamydia pneumoniae invasin protein Pmp21 recruits the EGF receptor for host cell entry.

Author information

1
Funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine Universität, Düsseldorf, Germany.

Abstract

Infection of mammalian cells by the strictly intracellular pathogens Chlamydiae requires adhesion and internalization of the infectious Elementary Bodies (EBs). The components of the latter step were unknown. Here, we identify Chlamydia pneumoniae Pmp21 as an invasin and EGFR as its receptor. Modulation of EGFR surface expression evokes correlated changes in EB adhesion, internalization and infectivity. Ectopic expression of EGFR in EGFR-negative hamster cells leads to binding of Pmp21 beads and EBs, thus boosting the infection. EB/Pmp21 binding and invasion of epithelial cells results in activation of EGFR, recruitment of adaptors Grb2 and c-Cbl and activation of ERK1/2, while inhibition of EGFR or MEK kinase activity abrogates EB entry, but not attachment. Binding of Grb2 and c-Cbl by EGFR is essential for infection. This is the first report of an invasin-receptor interaction involved in host-cell invasion by any chlamydial species.

PMID:
23633955
PMCID:
PMC3635982
DOI:
10.1371/journal.ppat.1003325
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Public Library of Science Icon for PubMed Central
    Loading ...
    Support Center