ArticlePloS one2021
Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Crystal structures of Campylobacter jejuni CadF reveal a potential role for the arginine residue R268 in peptidoglycan recognition and pocket formation.Scientific reports · 2025Article
- Genomic profiling and experimental validation of type VI secretion system-associated proteins in Klebsiella.PLoS genetics · 2025Article
- Microscopic and metatranscriptomic analyses revealed unique cross-domain parasitism between phylummBio · 2024Article
- Diversity of the type VI secretion systems in theMicrobial genomics · 2023Article
- The accessory protein TagV is required for full Type VI secretion system activity in Serratia marcescens.Molecular microbiology · 2023Article
- Identification and Comparative Genomic Analysis of Type VI Secretion Systems and Effectors inFrontiers in microbiology · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.
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