Related Experiment Video

Updated: Dec 5, 2025

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis
10:32

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

Published on: June 10, 2020

4.4K

The Chlamydia effector CT622/TaiP targets a nonautophagy related function of ATG16L1

Daniel Hamaoui1, Mathilde M Cossé1,2, Jagan Mohan3

  • 1Unité de Biologie cellulaire de l'infection microbienne, Institut Pasteur, UMR3691 CNRS, F-75015, Paris, France.

Proceedings of the National Academy of Sciences of the United States of America
|October 15, 2020
PubMed

Insights

The bacteria Chlamydia trachomatis uses the effector protein TaiP to block the host protein ATG16L1, which normally restricts bacterial growth. This allows the bacteria to multiply within host cells.

Area of Science:

  • Microbiology
  • Cell Biology
  • Infectious Diseases

Background:

  • Chlamydia trachomatis is an obligate intracellular bacterium causing trachoma and STDs.
  • Bacteria reside in a vacuolar compartment called the inclusion, secreting effector proteins to manipulate host cells.
  • Host autophagy-related protein 16-1 (ATG16L1) is known for its role in LC3 lipidation during autophagy and LC3-associated phagocytosis.

Purpose of the Study:

  • To investigate the role of ATG16L1 in restricting Chlamydia trachomatis inclusion growth.
  • To identify the bacterial effector responsible for counteracting ATG16L1's function.
  • To elucidate the mechanism by which the bacterial effector interferes with ATG16L1.

Main Methods:

  • Investigated the interaction between ATG16L1 and Chlamydia trachomatis.
  • Identified and characterized the bacterial effector CT622/TaiP.
  • Utilized techniques to study protein-protein interactions and cellular trafficking pathways.

Main Results:

  • ATG16L1 restricts the growth of Chlamydia trachomatis inclusions.
  • The bacterial effector CT622/TaiP counteracts ATG16L1's inhibitory effect.
  • TaiP binds to ATG16L1's WD40 domain via a mimic of an eukaryotic binding motif, preventing interaction with TMEM59.
  • This interaction disrupts ATG16L1's role in intracellular traffic, promoting inclusion growth.

Conclusions:

  • The bacterial effector TaiP targets ATG16L1's function in intracellular trafficking, not LC3 lipidation.
  • This highlights a previously underappreciated role of ATG16L1 in regulating intracellular traffic.
  • Understanding this interaction is crucial for developing strategies against Chlamydia trachomatis infections.
Keywords:
ATG16L1Chlamydia trachomatisautophagyhost-pathogen interactionsintracellular traffic

More Related Videos

Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens07:40

Identification of Host Pathways Targeted by Bacterial Effector Proteins using Yeast Toxicity and Suppressor Screens

Published on: October 25, 2019

6.3K
Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis10:35

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis

Published on: January 30, 2020

7.0K

Related Concept Videos

Bacterial Phylum Chlamydiae01:29

Bacterial Phylum Chlamydiae

The phylum Chlamydiae or Chlamydiota is composed of a single order, Chlamydiales. This phylum consists entirely of obligate intracellular parasites that infect eukaryotic hosts. While human pathogens within this group have been studied extensively, the phylum encompasses many species capable of interacting with various eukaryotic organisms. Members of Chlamydiae are typically small cocci, approximately 0.5 μm in diameter, and exhibit a distinctive developmental cycle. As is characteristic...
309
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.5K
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.3K