ArticlePLoS pathogens2018
C-terminal processing of GlyGly-CTERM containing proteins by rhombosortase in Vibrio cholerae.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 21 citations in OpenAlex.
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inJournal of bacteriology · 2026Article
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inbioRxiv : the preprint server for biology · 2026Article
- Article
- Enrichment isolation and metabolic characteristics ofApplied and environmental microbiology · 2025Article
- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
- Article
- Myxosortase: an intramembrane protease that sorts MYXO-CTERM proteins to the cell surface.mBio · 2025Article
- Article
- The type II secretion system as an underappreciated and understudied mediator of interbacterial antagonism.Infection and immunity · 2024Review
- Article
- Coevolution between marine Aeromonas and phages reveals temporal trade-off patterns of phage resistance and host population fitness.The ISME journal · 2023Article
- Review
- Article
- MYXO-CTERM sorting tag directs proteins to the cell surface via the type II secretion system.Molecular microbiology · 2020Article
- Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Vibrio cholerae and a subset of other Gram-negative bacteria, including Acinetobacter baumannii, express proteins with a C-terminal tripartite domain called GlyGly-CTERM, which consists of a motif rich in glycines and serines, followed by a hydrophobic region and positively charged residues. Here we show that VesB, a V. cholerae serine protease, requires the GlyGly-CTERM domain, the intramembrane rhomboid-like protease rhombosortase, and the type II secretion system (T2SS) for localization at the cell surface. VesB is cleaved by rhombosortase to expose the second glycine residue of the GlyGly-CTERM motif, which is then conjugated to a glycerophosphoethanolamine-containing moiety prior to engagement with the T2SS and outer membrane translocation. In support of this, VesB accumulates intracellularly in the absence of the T2SS, and surface-associated VesB activity is no longer detected when the rhombosortase gene is inactivated. In turn, when VesB is expressed without an intact GlyGly-CTERM domain, VesB is released to the extracellular milieu by the T2SS and does not accumulate on the cell surface. Collectively, our findings suggest that the posttranslational modification of the GlyGly-CTERM domain is essential for cell surface localization of VesB and other proteins expressed with this tripartite extension.
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