ArticleJournal of bacteriology2019
Role and Recruitment of the TagL Peptidoglycan-Binding Protein during Type VI Secretion System Biogenesis.
Article in Journal of bacteriology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- Neisseria subflava Type 6 Secretion System competition with bacterial and fungal species.Applied microbiology and biotechnology · 2026Article
- Assembly of a unique membrane complex in type VI secretion systems of Bacteroidota.Nature communications · 2024Article
- Bacterial One- and Two-Hybrid Assays to Monitor Transmembrane Helix Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- The accessory protein TagV is required for full Type VI secretion system activity in Serratia marcescens.Molecular microbiology · 2023Article
- Structure and Activity of the Type VI Secretion System.Microbiology spectrum · 2019Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VI secretion system (T6SS) is an injection apparatus that uses a springlike mechanism for effector delivery. The contractile tail is composed of a needle tipped by a sharpened spike and wrapped by the sheath that polymerizes in an extended conformation on the assembly platform, or baseplate. Contraction of the sheath propels the needle and effectors associated with it into target cells. The passage of the needle through the cell envelope of the attacker is ensured by a dedicated trans-envelope channel complex. This membrane complex (MC) comprises the TssJ lipoprotein and the TssL and TssM inner membrane proteins. MC assembly is a hierarchized mechanism in which the different subunits are recruited in a specific order: TssJ, TssM, and then TssL. Once assembled, the MC serves as a docking station for the baseplate. In enteroaggregative
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