Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.

Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.

Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of beta-barrel pore-forming toxins (beta-PFTs). By contrast, other beta-PFTs form homo-oligomeric pores; for example, the staphyl...

Descrizione completa

Dettagli Bibliografici
Autori principali:	Miles, G, Movileanu, L, Bayley, J
Natura:	Journal article
Lingua:	English
Pubblicazione:	2002

Documenti analoghi

Staphylococcal Bicomponent Pore-Forming Toxins: Targets for Prophylaxis and Immunotherapy
di: M. Javad Aman, et al.
Pubblicazione: (2014-03-01)

Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
di: Gouaux, J, et al.
Pubblicazione: (1994)

Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells.
di: Valeva, A, et al.
Pubblicazione: (1997)

Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.
di: Valeva, A, et al.
Pubblicazione: (1996)

Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin.
di: Krishnasastry, M, et al.
Pubblicazione: (1994)

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.
di: Song, L, et al.
Pubblicazione: (1996)

Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore
di: Noriko TOMITA, et al.
Pubblicazione: (2011-10-01)

Studying Staphylococcal Leukocidins: A Challenging Endeavor
di: Angelino T. Tromp, et al.
Pubblicazione: (2020-04-01)

Imaging the assembly of the Staphylococcal pore-forming toxin alpha-Hemolysin
di: Thompson, J, et al.
Pubblicazione: (2009)

Staphylococcus aureus isolates from Eurasian Beavers (Castor fiber) carry a novel phage-borne bicomponent leukocidin related to the Panton-Valentine leukocidin
di: Stefan Monecke, et al.
Pubblicazione: (2021-12-01)

Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules.
di: Movileanu, L, et al.
Pubblicazione: (2001)

Engineered transmembrane pores.
di: Ayub, M, et al.
Pubblicazione: (2016)

Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore.
di: Movileanu, L, et al.
Pubblicazione: (2000)

Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
di: Miles, G, et al.
Pubblicazione: (2002)

Human Monocyte-Derived Osteoclasts Are Targeted by Staphylococcal Pore-Forming Toxins and Superantigens.
di: Sacha Flammier, et al.
Pubblicazione: (2016-01-01)

Host–Receptor Post-Translational Modifications Refine Staphylococcal Leukocidin Cytotoxicity
di: Angelino T. Tromp, et al.
Pubblicazione: (2020-02-01)

An octameric carbopeptoid; Secondary structure in octameric and tetrameric 5-aminomethyl-tetrahydrofuran-2-carboxylates
di: Claridge, T, et al.
Pubblicazione: (1999)

Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.
di: Walker, B, et al.
Pubblicazione: (1992)

The staphylococcal alpha-toxin pore has a flexible conformation.
di: Vécsey-Semjén, B, et al.
Pubblicazione: (1999)

Crystal structure of a two-subunit TrkA octameric gating ring assembly.
di: Marc C Deller, et al.
Pubblicazione: (2015-01-01)

Redirecting pore assembly of staphylococcal α-hemolysin by protein engineering
di: Koo, S, et al.
Pubblicazione: (2019)

Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel.
di: Cheley, S, et al.
Pubblicazione: (1997)

Separately or combined, LukG/LukH is functionally unique compared to other staphylococcal bicomponent leukotoxins.
di: Machi Yanai, et al.
Pubblicazione: (2014-01-01)

Deciphering the Pathological Role of Staphylococcal α-Toxin and Panton–Valentine Leukocidin Using a Novel Ex Vivo Human Skin Model
di: Reuben Olayinka Olaniyi, et al.
Pubblicazione: (2018-05-01)

Redirecting Pore Assembly of Staphylococcal α‑Hemolysin by Protein Engineering
di: Sunwoo Koo, et al.
Pubblicazione: (2019-03-01)

Temperature-responsive protein pores.
di: Jung, Y, et al.
Pubblicazione: (2006)

Vibrio pore-forming leukocidin activates pyroptotic cell death via the NLRP3 inflammasome
di: Hadar Cohen, et al.
Pubblicazione: (2020-01-01)

Pore-forming toxins
di: Gilbert, R
Pubblicazione: (2002)

Pore-forming toxins.
di: Gilbert, R
Pubblicazione: (2002)

Single DNA rotaxanes of a transmembrane pore protein.
di: Sánchez-Quesada, J, et al.
Pubblicazione: (2004)

Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore.
di: Gu, L, et al.
Pubblicazione: (2003)

A functional protein pore with a "retro" transmembrane domain.
di: Cheley, S, et al.
Pubblicazione: (1999)

Partitioning of individual flexible polymers into a nanoscopic protein pore.
di: Movileanu, L, et al.
Pubblicazione: (2003)

Tumor protease-activated, pore-forming toxins from a combinatorial library.
di: Panchal, R, et al.
Pubblicazione: (1996)

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin
di: Sarah J Piper, et al.
Pubblicazione: (2019-04-01)

Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.
di: Walker, B, et al.
Pubblicazione: (1995)

Non-conventional octameric structure of C-phycocyanin
di: Takuo Minato, et al.
Pubblicazione: (2021-10-01)

Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism.
di: Alexander F Kintzer, et al.
Pubblicazione: (2010-11-01)

Staphylococcal Protein A, Panton-Valentine Leukocidin and Coagulase Aggravate the Bone Loss and Bone Destruction in Osteomyelitis
di: Tao Jin, et al.
Pubblicazione: (2013-08-01)

Interactions of peptides with a protein pore.
di: Movileanu, L, et al.
Pubblicazione: (2005)