Analysis of the atypical tryptophan biosynthetic operon of Chlamydia trachomatis revealed the simultaneous regulation of transcriptional initiation and termination by an iron-dependent repressor, expanding known regulatory mechanisms of this pathway.

The bacterium Chlamydia trachomatis, a human pathogen, hijacks its host’s energy supplies by using the parasitophorous vacuole as a glycogen synthesis and storage compartment.

The central immune modulator interferon-gamma downregulates the proto-oncogene c-Myc to shut down host cell metabolism and interfere with infection of epithelial cells by obligate intracellular pathogenic Chlamydia trachomatis.

Chlamydia hijacks membrane trafficking proteins of the human host via the cytoplasmic domain of a secreted transmembrane protein.

Obligate intracellular Chlamydia secrete a deubiquitinating enzyme (Cdu1) into the membrane of the Chlamydia-containing vacuole to deubiquitinate selected host proteins and support the survival of the bacteria during genital infection.

To establish membrane contacts between its vacuole and the endoplasmic reticulum, the obligate intracellular bacterial pathogen Chlamydia trachomatis has evolved complex molecular strategies to mimic emerging regulatory processes that control contact-dependent organelle–organelle communication.

Structure of a pathogen effector complexed to Sorting Nexin 5 reveals an evolutionarily conserved interface that is required for retromer-dependent host restriction.

Genetic and biochemical analyses show that Chlamydia protects secreted effectors necessary for its exit from infected cells, preventing them from undergoing ubiquitination and degradation.

The in vivo modification of the canonical intermediate filament protein vimentin with O-linked beta-N-acetylglucosamine affects its function in filament assembly, cell migration and host-pathogen interactions.