ArticlePLoS genetics2017
Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.
Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- OFrontiers in cellular and infection microbiology · 2025Article
- Protein-Protein Interaction: Tandem Affinity Purification in Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Recent insights into type-3 secretion system injectisome structure and mechanism of human enteric pathogens.Current opinion in microbiology · 2023Review
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- Calcium regulates the mycophagous ability of Burkholderia gladioli strain NGJ1 in a type III secretion system-dependent manner.BMC microbiology · 2020Article
- Role of CsrA in stress responses and metabolism important for Salmonella virulence revealed by integrated transcriptomics.PloS one · 2019Article
- Acyl Carrier Protein 3 Is Involved in Oxidative Stress Response inFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial pathogens often deliver effectors into host cells using type 3 secretion systems (T3SS), the extremity of which forms a translocon that perforates the host plasma membrane. The T3SS encoded by Salmonella pathogenicity island 1 (SPI-1) is genetically associated with an acyl carrier protein, IacP, whose role has remained enigmatic. In this study, using tandem affinity purification, we identify a direct protein-protein interaction between IacP and the translocon protein SipB. We show, by mass spectrometry and radiolabelling, that SipB is acylated, which provides evidence for a modification of the translocon that has not been described before. A unique and conserved cysteine residue of SipB is identified as crucial for this modification. Although acylation of SipB was not essential to virulence, we show that this posttranslational modification promoted SipB insertion into host-cell membranes and pore-forming activity linked to the SPI-1 T3SS. Cooccurrence of acyl carrier and translocon proteins in several γ- and β-proteobacteria suggests that acylation of the translocon is conserved in these other pathogenic bacteria. These results also indicate that acyl carrier proteins, known for their involvement in metabolic pathways, have also evolved as cofactors of new bacterial protein lipidation pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.