| Products/Services Used | Details | Operation |
|---|---|---|
| Peptide Synthesis | 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, USA [1]), or peptide antibody against VipB, (“QENPPADVRSRRPL”, Genscript, USA [22]) for 16 hr at 4°C or 1 hr at room temperature, washed with TBST, incubated for 1 hr with horseradish peroxidase-labeled 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 |
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, which is composed of interconnected VipA/VipB subunits forming a six-start helix. The mechanism of T6SS sheath contraction and the structure of its extended state are unknown. Here we show that elongating the N-terminal VipA linker or eliminating charge of a specific VipB residue abolished sheath contraction and delivery of effectors into target cells. The assembly of the non-contractile sheaths was dependent on the baseplate component TssE and mass-spectrometry analysis ide... More
