The type II secretion system: biogenesis, molecular architecture and mechanism.
TLDR
Recent structural and biochemical information is reviewed to describe the current knowledge of the biogenesis and architecture of the T2SS and its mechanism of action.Abstract:
Many Gram-negative bacteria use type II secretion systems (T2SSs) to translocate a range of proteins across the outer membrane from the periplasm. In this Review, Hol and colleagues describe how recent structural and biochemical studies have provided insights into the biogenesis and architecture of T2SSs and the mechanism by which they function.read more
Citations
More filters
Journal ArticleDOI
Secretion systems in Gram-negative bacteria: structural and mechanistic insights
Tiago R. D. Costa,Catarina Felisberto-Rodrigues,Amit Meir,Marie S. Prevost,Adam Redzej,Martina Trokter,Gabriel Waksman +6 more
TL;DR: The structural and mechanistic relationships between these single- and double-membrane-embedded systems are explored, and how this knowledge can be exploited for the development of new antimicrobial strategies are discussed.
Journal ArticleDOI
Bacterial Secretion Systems – An overview
Erin R. Green,Joan Mecsas +1 more
TL;DR: This chapter reviews the canonical features of several common bacterial protein secretion systems, as well as their roles in promoting the virulence of bacterial pathogens, and addresses recent findings that indicate that the innate immune system of the host can detect and respond to the presence ofprotein secretion systems during mammalian infection.
Journal ArticleDOI
Biology of Acinetobacter baumannii: Pathogenesis, Antibiotic Resistance Mechanisms, and Prospective Treatment Options.
Chang-Ro Lee,Jung Hun Lee,Moonhee Park,Kwang Seung Park,Il Kwon Bae,Young Bae Kim,Chang-Jun Cha,Byeong Chul Jeong,Sang Hee Lee +8 more
TL;DR: Current studies on the virulence factors that contribute to A. baumannii pathogenesis are summarized and Mechanisms of antibiotic resistance of this organism, including acquirement of β-lactamases, up-regulation of multidrug efflux pumps, modification of aminoglycosides, permeability defects, and alteration of target sites are discussed.
Journal ArticleDOI
Type IV Pilin Proteins: Versatile Molecular Modules
TL;DR: Recent advances in this research area are considered, from structural revelations to insights into diversity, posttranslational modifications, regulation, and function, which suggest both a common evolutionary origin and a highly adaptable functional plan.
Journal ArticleDOI
Architecture of the type IVa pilus machine.
Yi-Wei Chang,Yi-Wei Chang,Lee A. Rettberg,Anke Treuner-Lange,Janet Iwasa,Lotte Søgaard-Andersen,Grant J. Jensen,Grant J. Jensen +7 more
TL;DR: Putting the known structures of the individual proteins in place like pieces of a three-dimensional puzzle revealed insights into how the T4PM machine works, including evidence that ATP hydrolysis by cytoplasmic motors rotates a membrane-embedded adaptor that slips pilin subunits back and forth from the membrane onto the pilus.
References
More filters
Journal ArticleDOI
The complete general secretory pathway in gram-negative bacteria
TL;DR: The unifying feature of all proteins that are transported out of the cytoplasm of gram-negative bacteria by the general secretory pathway is the presence of a long stretch of predominantly hydrophobic amino acids, the signal sequence.
Journal ArticleDOI
Pilus retraction powers bacterial twitching motility.
TL;DR: The experiments establish that Tfp filaments retract, generate substantial force and directly mediate cell movement, which is required for twitching and social gliding.
Journal ArticleDOI
Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
TL;DR: Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes, and Omp85 is likely to play a role in outer membrane protein assembly.
Journal ArticleDOI
Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin
Petr G. Leiman,Petr G. Leiman,Marek Basler,Udupi A. Ramagopal,Jeffrey B. Bonanno,J. Michael Sauder,Stefan Pukatzki,Stephen K. Burley,Steven C. Almo,John J. Mekalanos +9 more
TL;DR: It is proposed that T6SS is a multicomponent structure whose extracellular part resembles both structurally and functionally a bacteriophage tail, an efficient machine that translocates proteins and DNA across lipid membranes into cells.
Journal ArticleDOI
Biology of type II secretion.
TL;DR: Recent findings on the organization of the secretion apparatus and the role of its various components in secretion are discussed, as are the possible properties that determine whether a protein is recognized and secreted by the type II pathway.