title: Disassembly of a Medial Transenvelope Structure by Antibiotics during Intracellular Division.
abstract: Chlamydiales possess a minimal but functional peptidoglycan precursor biosynthetic and remodeling pathway involved in the assembly of the division septum by an atypical cytokinetic machine and cryptic or modified peptidoglycan-like structure (PGLS). How this reduced cytokinetic machine collectively coordinates the invagination of the envelope has not yet been explored in Chlamydiales. In other Gram-negative bacteria, peptidoglycan provides anchor points that connect the outer membrane to the peptidoglycan during constriction using the Pal-Tol complex. Purifying PGLS and associated proteins from the chlamydial pathogen Waddlia chondrophila, we unearthed the Pal protein as a peptidoglycan-binding protein that localizes to the chlamydial division septum along with other components of the Pal-Tol complex. Together, our PGLS characterization and peptidoglycan-binding assays support the notion that diaminopimelic acid is an important determinant recruiting Pal to the division plane to coordinate the invagination of all envelope layers with the conserved Pal-Tol complex, even during osmotically protected intracellular growth.
authors.affiliation: Department of Laboratories, Institute of Microbiology, University Hospital Center and University of Lausanne, Lausanne 1011, Switzerland.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Jacquier
authors.affiliation: Department of Microbiology & Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva, Geneva 1211, Switzerland.
authors.forename: Antonio
authors.initials: A
authors.lastname: Frandi
authors.affiliation: Department of Microbiology & Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva, Geneva 1211, Switzerland. Electronic address: patrick.viollier@unige.ch.
authors.forename: Patrick H
authors.initials: PH
authors.lastname: Viollier
authors.affiliation: Department of Laboratories, Institute of Microbiology, University Hospital Center and University of Lausanne, Lausanne 1011, Switzerland. Electronic address: gilbert.greub@chuv.ch.
authors.forename: Gilbert
authors.initials: G
authors.lastname: Greub
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D002473:Cell Wall / Q000187:drug effects / Q000378:metabolism; D002695:Chlamydiales / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism*; D017124:Conserved Sequence; D003960:Diaminopimelic Acid / Q000378:metabolism; D008074:Lipoproteins / Q000378:metabolism; D010457:Peptidoglycan / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D008074:Lipoproteins; D010457:Peptidoglycan; D003960:Diaminopimelic Acid
keywords: Waddlia chondrophila; cell division; cell wall; chlamydia-related bacteria; contractile ring; peptidoglycan; peptidoglycan associated lipoprotein