ArticleJournal of bacteriology2008
SciN is an outer membrane lipoprotein required for type VI secretion in enteroaggregative Escherichia coli.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.
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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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Who cites it
125 citing papers in PubMed, 204 citations in OpenAlex.
- A T4SS effector directly disarms competing antibacterial T6SSs by hijacking their conserved spike component.Science China. Life sciences · 2026Article
- The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026Article
- T6SS in plant pathogens: unique mechanisms in complex hosts.Infection and immunity · 2024Review
- The role of the type VI secretion system in the stress resistance of plant-associated bacteria.Stress biology · 2024Review
- The role of type VI secretion system genes in antibiotic resistance and virulence inFrontiers in cellular and infection microbiology · 2024Article
- No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregativeJournal of bacteriology · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Identification and immunological characterization of cuproptosis-related molecular clusters in ulcerative colitis.BMC gastroenterology · 2023Article
- Type III Secretion System Repressor RhpR Induces GrlP, a Glycine-Rich Outer Membrane Lipoprotein with Functions in Regulating the Periplasmic Space and Pleiotropic Responses.Applied and environmental microbiology · 2023Article
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Protein Interactome Analysis of the Type IX Secretion System Identifies PorW as the Missing Link between the PorK/N Ring Complex and the Sov Translocon.Microbiology spectrum · 2022Article
- Prevalence and diversity of type VI secretion systems in a model beneficial symbiosis.Frontiers in microbiology · 2022Article
- A Shaving Proteomic Approach to Unveil Surface Proteins Modulation of Multi-Drug ResistantFrontiers in medicine · 2022Article
- Identification of Type VI Secretion Systems Effector Proteins That Contribute to Interbacterial Competition inFrontiers in microbiology · 2022Article
- Genome Analysis of theCurrent issues in molecular biology · 2021Article
- Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.PloS one · 2021Article
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Xenorhabdus bovienii strain jolietti uses a type 6 secretion system to kill closely related Xenorhabdus strains.FEMS microbiology ecology · 2020Article
- Article
65 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enteroaggregative Escherichia coli (EAEC) is a pathogen implicated in several infant diarrhea or diarrheal outbreaks in areas of endemicity. Although multiple genes involved in EAEC pathogenesis have been identified, the overall mechanism of virulence is not well understood. Recently, a novel secretion system, called type VI secretion (T6S) system (T6SS), has been identified in EAEC and most animal or plant gram-negative pathogens. T6SSs are multicomponent cell envelope machines responsible for the secretion of at least two putative substrates, Hcp and VgrG. In EAEC, two copies of T6S gene clusters, called sci-1 and sci-2, are present on the pheU pathogenicity island. In this study, we focused our work on the sci-1 gene cluster. The Sci-1 apparatus is probably composed of all, or a subset of, the 21 gene products encoded on the cluster. Among these subunits, some are shared by all T6SSs identified to date, including a ClpV-type AAA(+) ATPase (SciG) and an IcmF (SciS) and an IcmH (SciP) homologue, as well as a putative lipoprotein (SciN). In this study, we demonstrate that sciN is a critical gene necessary for T6S-dependent secretion of the Hcp-like SciD protein and for biofilm formation. We further show that SciN is a lipoprotein, as shown by the inhibition of its processing by globomycin and in vivo labeling with [(3)H]palmitic acid. SciN is tethered to the outer membrane and exposed in the periplasm. Sequestration of SciN at the inner membrane by targeting the +2 residue responsible for lipoprotein localization (Gly2Asp) fails to complement an sciN mutant for SciD secretion and biofilm formation. Together, these results support a model in which SciN is an outer membrane lipoprotein exposed in the periplasm and essential for the Sci-1 apparatus function.
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