ReviewInternational journal of molecular sciences2012
Förster resonance energy transfer (FRET) as a tool for dissecting the molecular mechanisms for maturation of the Shigella type III secretion needle tip complex.
Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Structural and Biophysical Characterization of the Yersinia Type Three Secretion System ATPase YscN.Proteins · 2026Article
- Novel Noncompetitive Type Three Secretion System ATPase Inhibitors Shut DownBiochemistry · 2020Article
- Dominant negative effects by inactive Spa47 mutants inhibit T3SS function and Shigella virulence.PloS one · 2020Article
- Interfacial amino acids support Spa47 oligomerization and shigella type three secretion system activation.Proteins · 2019Article
- Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD.Biochemistry · 2017Article
- Structural and Biochemical Characterization of Spa47 Provides Mechanistic Insight into Type III Secretion System ATPase Activation and Shigella Virulence Regulation.The Journal of biological chemistry · 2016Article
- N-terminus of IpaB provides a potential anchor to the Shigella type III secretion system tip complex protein IpaD.Biochemistry · 2013Article
- Fluorescent biphenyl derivatives of phenylalanine suitable for protein modification.Biochemistry · 2013Article
- Detection of dihydrofolate reductase conformational change by FRET using two fluorescent amino acids.Journal of the American Chemical Society · 2013Article
- Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.Protein science : a publication of the Protein Society · 2013Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Förster resonance energy transfer (FRET) provides a powerful tool for monitoring intermolecular interactions and a sensitive technique for studying Å-level protein conformational changes. One system that has particularly benefited from the sensitivity and diversity of FRET measurements is the maturation of the Shigella type III secretion apparatus (T3SA) needle tip complex. The Shigella T3SA delivers effector proteins into intestinal cells to promote bacterial invasion and spread. The T3SA is comprised of a basal body that spans the bacterial envelope and a needle with an exposed tip complex that matures in response to environmental stimuli. FRET measurements demonstrated bile salt binding by the nascent needle tip protein IpaD and also mapped resulting structural changes which led to the recruitment of the translocator IpaB. At the needle tip IpaB acts as a sensor for host cell contact but prior to secretion, it is stored as a heterodimeric complex with the chaperone IpgC. FRET analyses showed that chaperone binding to IpaB's N-terminal domain causes a conformational change in the latter. These FRET analyses, with other biophysical methods, have been central to understanding T3SA maturation and will be highlighted, focusing on the details of the FRET measurements and the relevance to this particular system.
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