Structure of a pathogen effector complexed to Sorting Nexin 5 reveals an evolutionarily conserved interface that is required for retromer-dependent host restriction.
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.
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 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.
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.
A protein modification called O-linked glycosylation regulates the interactions between vimentin molecules under normal conditions, and the ability of Chlamydia bacteria to replicate after they infect cells.
Isolation of a gokushovirus capable of lysogenizing enterobacteria challenges previous notions about the biology of the most prolific phages within the Microviridae and facilitates experimental study in a model organism.
