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Mechanistic and structural insights into the type VI secretion system tail of" vibrio cholerae"

Cell. 2015;

Mikhail Kudryashev,, Ray Yu-Ruei Wang,, Maximilian Brackmann, Sebastian Scherer, Timm Maier, David Baker, Frank DiMaio, Henning Stahlberg, Edward H. Egelman,,* and Marek Basler,*

Products/Services Used	Details	Operation
Peptide Synthesis	Antigen-purified rabbit polyclonal antibodies raised against VipB peptide QENPPADVRSRRPL were obtained commercially (GenScript, USA).Membrane was blocked with 5% milk in Tris-buffered saline (pH 7.4) containing Tween 0.1% (TBST), incubated with primary peptide antibody against Hcp (“QSGQPSGQRVHKPF”, Genscript, Piscataway, New Jersey, USA [1]), or peptide antibody against VipB (“QENPPADVRSRRPL”, Genscript, Piscataway, New Jersey, USA [27]) for 16 h at 4°C or 1 h at room temperature, washed with TBST, incubated for 1 h with horseradish peroxidaselabeled anti-rabbit antibody (Jackson ImmunoResearch Inc., USA), and washed with the recommended buffer, and peroxidase was detected by LumiGLO Chemiluminescent Substrate (KPL, Inc., Gaithersburg, Maryland, USA).	Get A Quote

摘要

Secretion systems are essential for bacteria to survive and manipulate their environment. The bacterial type VI secretion system (T6SS) generates the force needed for protein translocation by the contraction of a long polymer called sheath. The sheath is a sixstart helical assembly of interconnected VipA/VipB subunits. The mechanism of T6SS sheath contraction is unknown. Here, we show that elongating the N-terminal VipA linker or eliminating charge of a specific VipB residue abolishes sheath contraction and delivery of effectors into target cells. Mass spectrometry analysis identified the inner tube protein Hcp, spike protein VgrG, and other components of the T6SS baseplate significantly enriched in samples of ... More