Yersinia pestis Yop secretion protein F: Purification, characterization, and protective efficacy against bubonic plague

Świętnicki, Wiesław; Powell, Bradford S.; Goodin, Jeremy L.

doi:10.1016/j.pep.2005.02.016

Cited by 37 publications

(25 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The T3SS needle is known to exist as a preformed structure on the cell surface and is essential for T3SS activity in other systems. Indeed, hyperimmunization with Yersinia YscF has been shown to protect mice from Y. pestis infection (35,54). Furthermore, CdsF is highly conserved in Chlamydia with Ͼ95% sequence identity between all strains, raising the possibility that a CdsF-based vaccine may provide a wide range of protection against all medically significant strains of Chlamydia.…”

Section: Vol 190 2008mentioning

confidence: 99%

“…Numerous studies have demonstrated that deletion or mutation of the gene encoding the needle results in significant attenuation of virulence (31,53,55,56). Experiments using a subcutaneous murine infection model have shown that the Yersinia pestis needle protein YscF can serve as a protective antigen, indicating that the needle may have potential in vaccine development (8,35,45,54,55). In addition to its role as an injectisome component, evidence suggests that the needle is also important in host cell detection and thus regulation of T3S (12,30,60).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Bioinformatic and Biochemical Evidence for the Identification of the Type III Secretion System Needle Protein ofChlamydia trachomatis

et al. 2008

View full text Add to dashboard Cite

Chlamydia spp. express a functional type III secretion system (T3SS) necessary for pathogenesis and intracellular growth. However, certain essential components of the secretion apparatus have diverged to such a degree as to preclude their identification by standard homology searches of primary protein sequences. One example is the needle subunit protein. Electron micrographs indicate that chlamydiae possess needle filaments, and yet database searches fail to identify a SctF homologue. We used a bioinformatics approach to identify a likely needle subunit protein for Chlamydia. Experimental evidence indicates that this protein, designated CdsF, has properties consistent with it being the major needle subunit protein. CdsF is concentrated in the outer membrane of elementary bodies and is surface exposed as a component of an extracellular needle-like projection. During infection CdsF is detectible by indirect immunofluorescence in the inclusion membrane with a punctuate distribution adjacent to membrane-associated reticulate bodies. Biochemical cross-linking studies revealed that, like other SctF proteins, CdsF is able to polymerize into multisubunit complexes. Furthermore, we identified two chaperones for CdsF, termed CdsE and CdsG, which have many characteristics of the Pseudomonas spp. needle chaperones PscE and PscG, respectively. In aggregate, our data are consistent with CdsF representing at least one component of the extended Chlamydia T3SS injectisome. The identification of this secretion system component is essential for studies involving ectopic reconstitution of the Chlamydia T3SS. Moreover, we anticipate that CdsF could serve as an efficacious target for anti-Chlamydia neutralizing antibodies.

show abstract

Section: Vol 190 2008mentioning

confidence: 99%

mentioning

confidence: 99%

Bioinformatic and Biochemical Evidence for the Identification of the Type III Secretion System Needle Protein ofChlamydia trachomatis

et al. 2008

View full text Add to dashboard Cite

show abstract

“…The needle proteins from different species share only between 20 and 30% sequence identity but are all small (7 to 10 kDa), are neutral in charge, and are mostly alpha helical in structure (11,69,76). Using a combination of X-ray fiber diffraction and electron microscopy, the first three-dimensional structure of a needle filament was solved to ϳ16 Å by using purified needles from Shigella (9).…”

mentioning

confidence: 99%

Mutations in the Yersinia pseudotuberculosis Type III Secretion System Needle Protein, YscF, That Specifically Abrogate Effector Translocation into Host Cells

Davis

Mecsas

2007

J Bacteriol

View full text Add to dashboard Cite

The trafficking of effectors, termed Yops, from Yersinia spp. into host cells is a multistep process that requires the type III secretion system (TTSS). The TTSS has three main structural parts: a base, a needle, and a translocon, which work together to ensure the polarized movement of Yops directly from the bacterial cytosol into the host cell cytosol. To understand the interactions that take place at the interface between the tip of the TTSS needle and the translocon, we developed a screen to identify mutations in the needle protein YscF that separated its function in secretion from its role in translocation. We identified 25 translocation-defective (TD) yscF mutants, which fall into five phenotypic classes. Some classes exhibit aberrant needle structure and/or reduced levels of Yop secretion, consistent with known functions for YscF. Strikingly, two yscF TD classes formed needles and secreted Yops normally but displayed distinct translocation defects. Class I yscF TD mutants showed diminished pore formation, suggesting incomplete pore insertion and/or assembly. Class II yscF TD mutants formed pores but showed nonpolar translocation, suggesting unstable needle-translocon interactions. These results indicate that YscF functions in Yop secretion and translocation can be genetically separated. Furthermore, the identification of YscF residues that are required for the assembly of the translocon and/or productive interactions with the translocon has allowed us to initiate the mapping of the needle-translocon interface.

show abstract

“…Immunization of mice with YscF resulted in a high anti-YscF titer and provided partial protection against intravenous (i.v.) challenge with Y. pestis (Matson et al, 2005;Swietnicki et al, 2005).…”

Section: Subunit Vaccines Based On the F1 Lcrv And Yscf Proteinsmentioning

confidence: 99%

Recent Advancement in the Development of Vaccines Against Y. pestis - A Potential Agent of Bioterrorism

Ali¹,

Rao²

2012

Bioterrorism

View full text Add to dashboard Cite

Yersinia pestis Yop secretion protein F: Purification, characterization, and protective efficacy against bubonic plague

Cited by 37 publications

References 21 publications

Bioinformatic and Biochemical Evidence for the Identification of the Type III Secretion System Needle Protein ofChlamydia trachomatis

Bioinformatic and Biochemical Evidence for the Identification of the Type III Secretion System Needle Protein ofChlamydia trachomatis

Mutations in the Yersinia pseudotuberculosis Type III Secretion System Needle Protein, YscF, That Specifically Abrogate Effector Translocation into Host Cells

Recent Advancement in the Development of Vaccines Against Y. pestis - A Potential Agent of Bioterrorism

Contact Info

Product

Resources

About