Chlamydia trachomatis highjacks host MYO1C for actin cage recruitment at the bacterial inclusion
Abstract
Chlamydia trachomatis (Ct), a Gram-negative obligate intracellular pathogen, manipulates host actin dynamics to facilitate its entry, development, and exit. It assembles a dynamic actin cage around its intracellular niche, known as the ‘inclusion’, which provides structural stability for bacterial growth, and is crucial for exit via the non-cell-lytic extrusion process. We found that Ct recruits Myosin 1 C (MYO1C), a ubiquitous actin dependent motor protein, to the inclusion throughout its life cycle. Consequently, loss of MYO1C activity reduced Ct infection and the production of bacterial progenies. Mechanistically, MYO1C functions as a dynamic tether that assembles an actin cage around the inclusion membrane, as depletion of MYO1C or its inhibition by pentachloropseudilin (PClP) leads to the loss of the actin network surrounding the inclusion. In vitro reconstitution assays revealed that the presence of purified MYO1C was necessary and sufficient to build an actin cage around giant membranous vesicles. In summary, our findings identified MYO1C as a novel host target of Ct and provided mechanistic evidence for its role as a dynamic tether to recruit the essential actin cage around the bacterial inclusion.
Related
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BibTeX
@article{cuervo2026chlamydia,
title = {{Chlamydia trachomatis highjacks host MYO1C for actin cage recruitment at the bacterial inclusion}},
author = {María Emilia Cuervo and Diego del Balzo and María Natalia Zanetti and Mariela Beatriz Nolly and Hugo Lachuer and Rostislav Petkov and Nour Ismail and John Manzi and Rubén Walter Caron and Christophe Le Clainche and Maria Teresa Damiani and Julien Pernier and Kristine Schauer and Anahi Capmany},
journal = {Microbiological Research},
year = {2026},
month = sep,
doi = {10.1016/j.micres.2025.128395},
url = {https://hal.inrae.fr/hal-05399774v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - Chlamydia trachomatis highjacks host MYO1C for actin cage recruitment at the bacterial inclusion
AU - María Emilia Cuervo
AU - Diego del Balzo
AU - María Natalia Zanetti
AU - Mariela Beatriz Nolly
AU - Hugo Lachuer
AU - Rostislav Petkov
AU - Nour Ismail
AU - John Manzi
AU - Rubén Walter Caron
AU - Christophe Le Clainche
AU - Maria Teresa Damiani
AU - Julien Pernier
AU - Kristine Schauer
AU - Anahi Capmany
PY - 2026
DA - 2026/09/28
JO - Microbiological Research
DO - 10.1016/j.micres.2025.128395
UR - https://hal.inrae.fr/hal-05399774v1
AB - Chlamydia trachomatis (Ct), a Gram-negative obligate intracellular pathogen, manipulates host actin dynamics to facilitate its entry, development, and exit. It assembles a dynamic actin cage around its intracellular niche, known as the ‘inclusion’, which provides structural stability for bacterial growth, and is crucial for exit via the non-cell-lytic extrusion process. We found that Ct recruits Myosin 1 C (MYO1C), a ubiquitous actin dependent motor protein, to the inclusion throughout its life cycle. Consequently, loss of MYO1C activity reduced Ct infection and the production of bacterial progenies. Mechanistically, MYO1C functions as a dynamic tether that assembles an actin cage around the inclusion membrane, as depletion of MYO1C or its inhibition by pentachloropseudilin (PClP) leads to the loss of the actin network surrounding the inclusion. In vitro reconstitution assays revealed that the presence of purified MYO1C was necessary and sufficient to build an actin cage around giant membranous vesicles. In summary, our findings identified MYO1C as a novel host target of Ct and provided mechanistic evidence for its role as a dynamic tether to recruit the essential actin cage around the bacterial inclusion.
SN - 0944-5013
ER -