PilF Is an Outer Membrane Lipoprotein Required for Multimerization and Localization of the Pseudomonas aeruginosa Type IV Pilus Secretin
J Koo, S Tammam, SY Ku, LM Sampaleanu… - Journal of …, 2008 - Am Soc Microbiol
ABSTRACT Type IV pili (T4P) are retractile appendages that contribute to the virulence of
bacterial pathogens. PilF is a Pseudomonas aeruginosa lipoprotein that is essential for T4P …
bacterial pathogens. PilF is a Pseudomonas aeruginosa lipoprotein that is essential for T4P …
Effects of tcpB Mutations on Biogenesis and Function of the Toxin-Coregulated Pilus, the Type IVb Pilus of Vibrio cholerae
Y Gao, CA Hauke, JM Marles, RK Taylor - Journal of Bacteriology, 2016 - Am Soc Microbiol
Vibrio cholerae is the etiological agent of the acute intestinal disorder cholera. The toxin-
coregulated pilus (TCP), a type IVb pilus, is an essential virulence factor of V. cholerae …
coregulated pilus (TCP), a type IVb pilus, is an essential virulence factor of V. cholerae …
Functional Mapping of PilF and PilQ in the Pseudomonas aeruginosa Type IV Pilus System
Pseudomonas aeruginosa uses type IV pili (T4P) to interact with the environment and as key
virulence factors when acting as an opportunistic pathogen. Assembly of the outer …
virulence factors when acting as an opportunistic pathogen. Assembly of the outer …
Genetic Characterization of a New Type IV-A Pilus Gene Cluster Found in Both Classical and El Tor Biotypes ofVibrio cholerae
KJ Fullner, JJ Mekalanos - Infection and immunity, 1999 - Am Soc Microbiol
The Vibrio cholerae genome contains a 5.4-kb pil gene cluster that resembles the
Aeromonas hydrophila tap gene cluster and other type IV-A pilus assembly operons. The …
Aeromonas hydrophila tap gene cluster and other type IV-A pilus assembly operons. The …
Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis
DG Thanassi, C Stathopoulos, K Dodson… - Journal of …, 2002 - Am Soc Microbiol
Biogenesis of a superfamily of surface structures by gram-negative bacteria requires the
chaperone/usher pathway, a terminal branch of the general secretory pathway. In this …
chaperone/usher pathway, a terminal branch of the general secretory pathway. In this …
Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae
KV Korotkov, B Krumm, M Bagdasarian… - Journal of molecular …, 2006 - Elsevier
The type 2 secretion system (T2SS) occurring in Gram-negative bacteria is composed of 12–
15 different proteins which form large assemblies spanning two membranes and secreting …
15 different proteins which form large assemblies spanning two membranes and secreting …
Type IV-like pili formed by the type II secreton: specificity, composition, bundling, polar localization, and surface presentation of peptides
G Vignon, R Köhler, E Larquet, S Giroux… - Journal of …, 2003 - Am Soc Microbiol
The secreton or type II secretion machinery of gram-negative bacteria includes several type
IV pilin-like proteins (the pseudopilins) that are absolutely required for secretion. We …
IV pilin-like proteins (the pseudopilins) that are absolutely required for secretion. We …
Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity
M Patrick, KV Korotkov, WGJ Hol… - Journal of Biological …, 2011 - ASBMB
EpsE is an ATPase that powers transport of cholera toxin and hydrolytic enzymes through
the Type II secretion (T2S) apparatus in the Gram-negative bacterium, Vibrio cholerae. On …
the Type II secretion (T2S) apparatus in the Gram-negative bacterium, Vibrio cholerae. On …
The Vibrio cholerae Minor Pilin TcpB Initiates Assembly and Retraction of the Toxin-Coregulated Pilus
D Ng, T Harn, T Altindal, S Kolappan, JM Marles… - PLoS …, 2016 - journals.plos.org
Type IV pilus (T4P) systems are complex molecular machines that polymerize major pilin
proteins into thin filaments displayed on bacterial surfaces. Pilus functions require rapid …
proteins into thin filaments displayed on bacterial surfaces. Pilus functions require rapid …
The chaperone/usher pathway: a major terminal branch of the general secretory pathway
DG Thanassi, ET Saulino, SJ Hultgren - Current opinion in microbiology, 1998 - Elsevier
Gram-negative bacteria assemble a variety of adhesive organelles on their surface,
including the thread-like structures known as pili. Recent studies on pilus assembly by the …
including the thread-like structures known as pili. Recent studies on pilus assembly by the …