Disulfide Bonding within Components of the Chlamydia Type III Secretion Apparatus Correlates with Development

Betts-Hampikian, H. J.; Fields, Kenneth A.

doi:10.1128/jb.05163-11

Cited by 23 publications

(26 citation statements)

References 47 publications

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“…Unlike orthologs in other T3SSs, the chlamydial needle subunit protein CdsF contains Cys residues [12]. Intermolecular disulfide bonds among CdsF subunits are apparent in EBs but not RBs [11], raising the possibility that disulfide bonding has evolved in Chlamydia to couple T3S activity with one of the hallmarks of the chlamydial developmental cycle. Based on modeling of other T3S needle proteins [25], the N-terminally located Cys residues of CdsF could be oriented in the lumen of the needle channel.…”

Section: Attachmentmentioning

confidence: 99%

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A working model for the type III secretion mechanism in Chlamydia

Ferrell

Fields

2016

Microbes and Infection

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Section: Attachmentmentioning

confidence: 99%

“…CdsE and CdsG form a heterodimer capable of interacting with CdsF [61, 12]. CdsF-containing projections are apparent on EBs [12], and nearly all of EB-localized CdsF contains intermolecular disulfide bonds [11]. This suggests that secretion of CdsF is not required during the invasion process.…”

Section: Intracellular Developmentmentioning

confidence: 99%

A working model for the type III secretion mechanism in Chlamydia

Ferrell

Fields

2016

Microbes and Infection

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“…It has been described that T3SS proteins tend to oligomerize via disulfide bonding and that the occurrence of SS‐bridges is related to the developmental cycle of the bacteria . The full length CdsD sequence has altogether four cysteines (Cys92, Cys669, Cys781, and Cys813), from which the Cys669 is conserved when comparing sequences within Chlamydia spp . Cys669 is the only cysteine that is present in both constructs studied here and it is well ordered in each of the two crystal structures.…”

Section: Resultsmentioning

confidence: 83%

The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis

2016

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The type III secretion system (T3SS) is required for the virulence of many gram-negative bacterial human pathogens. It is composed of several structural proteins, forming the secretion needle and its basis, the basal body. In Chlamydia spp., the T3SS inner membrane ring (IM-ring) of the basal body is formed by the periplasmic part of CdsD (outer ring) and CdsJ (inner ring). Here we describe the crystal structure of the C-terminal, periplasmic part of CdsD, not including the last 60 residues. Two crystal forms were obtained, grown in three different crystallization conditions. In both crystal forms there is one molecule per asymmetric unit adopting a similar extended structure. The structures consist of three periplasmic domains (PDs) of similar abbab topology as seen also in the structures of the homologous PrgH (Salmonella typhimurium) and YscD (Yersinia enterocolitica). Only in the C2 crystal form, there is a C-terminal additional helix after the PD3 domain. The relative orientation of the three subsequent CdsD PD domains with respect to each other is more extended than in PrgH but less extended than in YscD. Small-angle X-ray scattering data show that also in solution this CdsD construct adopts the same elongated shape. In both crystal forms the CdsD molecules are packed in a parallel fashion, using translational crystallographic symmetry. The most extensive crystal contacts are preserved in both crystal forms, suggesting a possible mode of assembly of the CdsD periplasmic part into a 24-mer complex forming the outer ring of the IM-ring of the T3SS.

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“…The structural conservation of T3SA across broad species boundaries ranging from Chlamydiae [56,57] to the more genetically complex Burkhoderia spp [58]. to the Gram-negative bacterial flagellar systems [59] has provided a strong argument for the evolutionary importance of the T3SA and this secretion system in general.…”

Section: Förster Resonance Energy Transfermentioning

confidence: 99%

Förster Resonance Energy Transfer (FRET) as a Tool for Dissecting the Molecular Mechanisms for Maturation of the Shigella Type III Secretion Needle Tip Complex

Dickenson

Picking

2012

IJMS

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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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Disulfide Bonding within Components of the Chlamydia Type III Secretion Apparatus Correlates with Development

Cited by 23 publications

References 47 publications

A working model for the type III secretion mechanism in Chlamydia

A working model for the type III secretion mechanism in Chlamydia

The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis

Förster Resonance Energy Transfer (FRET) as a Tool for Dissecting the Molecular Mechanisms for Maturation of the Shigella Type III Secretion Needle Tip Complex

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