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Costa, Tiago
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Publications (10 of 11) Show all publications
Costa, T., Francis, M. K., Farag, S., Edgren, T. & Francis, M. S. (2019). Measurement of Yersinia translocon pore formation in erythrocytes. In: Viveka Vadyvaloo and Matthew B. Lawrenz (Ed.), Pathogenic Yersinia: methods and protocols (pp. 211-229). New York, NY, U.S.A.: Humana Press
Open this publication in new window or tab >>Measurement of Yersinia translocon pore formation in erythrocytes
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2019 (English)In: Pathogenic Yersinia: methods and protocols / [ed] Viveka Vadyvaloo and Matthew B. Lawrenz, New York, NY, U.S.A.: Humana Press, 2019, p. 211-229Chapter in book (Refereed)
Abstract [en]

Many Gram-negative pathogens produce a type III secretion system capable of intoxicating eukaryotic cells with immune-modulating effector proteins. Fundamental to this injection process is the prior secretion of two translocator proteins destined for injectisome translocon pore assembly within the host cell plasma membrane. It is through this pore that effectors are believed to travel to gain access to the host cell interior. Yersinia species especially pathogenic to humans and animals assemble this translocon pore utilizing two hydrophobic translocator proteins-YopB and YopD. Although a full molecular understanding of the biogenesis, function and regulation of this translocon pore and subsequent effector delivery into host cells remains elusive, some of what we know about these processes can be attributed to studies of bacterial infections of erythrocytes. Herein we describe the methodology of erythrocyte infections by Yersinia, and how analysis of the resultant contact-dependent hemolysis can serve as a relative measurement of YopB- and YopD-dependent translocon pore formation.

Place, publisher, year, edition, pages
New York, NY, U.S.A.: Humana Press, 2019
Series
Methods in Molecular Biology, ISSN 1064-3745, E-ISSN 1940-6029 ; 2010
Keywords
Biogenesis, Contact-dependent hemolysis, Effector recognition and intracellular delivery, Function and regulation, Host immune response, Membrane integration, Type III translocon pore complex
National Category
Microbiology in the medical area Microbiology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-161385 (URN)10.1007/978-1-4939-9541-7_15 (DOI)31177441 (PubMedID)978-1-4939-9540-0 (ISBN)
Funder
Swedish Research Council, 2014-2105Swedish Research Council, 2009-5628
Available from: 2019-07-03 Created: 2019-07-03 Last updated: 2019-07-03Bibliographically approved
Gurung, J. M., Amer, A., Francis, M., Costa, T., Chen, S., Zavialov, A. V. & Francis, M. S. (2018). Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion. Frontiers in Cellular and Infection Microbiology, 8, Article ID 80.
Open this publication in new window or tab >>Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion
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2018 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 8, article id 80Article in journal (Refereed) Published
Abstract [en]

Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic Yersinia species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an yscX nor yscY null mutant of Yersinia is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of Pseudomonas aeruginosa (PscX and PscY), Aeromonas species (AscX and AscY), Vibrio species (VscX and VscY), and Photorhabdus luminescens (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native yscX in the near full-length yscX deletion and native yscY in the near full-length yscY deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for Yersinia type III secretion.

Place, publisher, year, edition, pages
Frontiers Research Foundation, 2018
Keywords
T3S chaperone, secretion hierarchy, substrate sorting, LcrH/SycD, YscV, protein-protein interaction
National Category
Microbiology
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-146348 (URN)10.3389/fcimb.2018.00080 (DOI)000427608900001 ()29616194 (PubMedID)
Funder
Swedish Research Council
Available from: 2018-04-05 Created: 2018-04-05 Last updated: 2018-06-09Bibliographically approved
Francis, M. S., Amer, A. A., Milton, D. & Costa, T. R. (2017). Site-directed mutagenesis and its application in studying the interactions of T3S components. In: Matthew L. Nilles and Danielle L. Jessen Condry (Ed.), Type 3 secretion systems: methods and protocols (pp. 11-31). Humana Press
Open this publication in new window or tab >>Site-directed mutagenesis and its application in studying the interactions of T3S components
2017 (English)In: Type 3 secretion systems: methods and protocols / [ed] Matthew L. Nilles and Danielle L. Jessen Condry, Humana Press, 2017, p. 11-31Chapter in book (Refereed)
Abstract [en]

Type III secretion systems are a prolific virulence determinant among Gram-negative bacteria. They are used to paralyze the host cell, which enables bacterial pathogens to establish often fatal infections—unless an effective therapeutic intervention is available. However, as a result of a catastrophic rise in infectious bacteria resistant to conventional antibiotics, these bacteria are again a leading cause of worldwide mortality. Hence, this report describes a pDM4-based site-directed mutagenesis strategy that is assisting in our foremost objective to better understand the fundamental workings of the T3SS, using Yersinia as a model pathogenic bacterium. Examples are given that clearly document how pDM4-mediated site-directed mutagenesis has been used to establish clean point mutations and in-frame deletion mutations that have been instrumental in identifying and understanding the molecular interactions between components of the Yersinia type III secretion system.

Place, publisher, year, edition, pages
Humana Press, 2017
Series
Methods in Molecular Biology, ISSN 1064-3745 ; 1531
Keywords
Site-directed mutagenesis, Type III secretion systems, Suicide vector pDM4, Mutant libraries, Genetic-based screens, Protein-protein interaction assays
National Category
Biochemistry and Molecular Biology
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-128091 (URN)10.1007/978-1-4939-6649-3_2 (DOI)27837478 (PubMedID)978-1-4939-6647-9 (ISBN)978-1-4939-6649-3 (ISBN)
Funder
Swedish Research Council, 2014–2105
Available from: 2016-11-22 Created: 2016-11-22 Last updated: 2018-06-09Bibliographically approved
Amer, A., Gurung, J., Costa, T., Ruuth, K., Zavialov, A., Forsberg, Å. & Francis, M. S. (2016). YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis. Frontiers in Cellular and Infection Microbiology, 6, Article ID 66.
Open this publication in new window or tab >>YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis
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2016 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 6, article id 66Article in journal (Refereed) Published
Abstract [en]

Yersinia bacteria target Yop effector toxins to the interior of host immune cells by the Ysc-Yop type III secretion system. A YopN-TyeA heterodimer is central to controlling Ysc-Yop targeting activity. A + 1 frameshift event in the 3-prime end of yopN can also produce a singular secreted YopN-TyeA polypeptide that retains some regulatory function even though the C-terminal coding sequence of this YopN differs greatly from wild type. Thus, this YopN C-terminal segment was analyzed for its role in type III secretion control. Bacteria producing YopN truncated after residue 278, or with altered sequence between residues 279 and 287, had lost type III secretion control and function. In contrast, YopN variants with manipulated sequence beyond residue 287 maintained full control and function. Scrutiny of the YopN-TyeA complex structure revealed that residue W279 functioned as a likely hydrophobic contact site with TyeA. Indeed, a YopNW279G mutant lost all ability to bind TyeA. The TyeA residue F8 was also critical for reciprocal YopN binding. Thus, we conclude that specific hydrophobic contacts between opposing YopN and TyeA termini establishes a complex needed for regulating Ysc-Yop activity.

Keywords
protein-protein interaction, molecular modelling, protein secretion, mutagenesis, bacterial pathogenesis, regulation
National Category
Microbiology in the medical area Biochemistry and Molecular Biology
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-122904 (URN)10.3389/fcimb.2016.00066 (DOI)000378543500001 ()
Funder
Swedish Research Council
Available from: 2016-06-23 Created: 2016-06-23 Last updated: 2018-06-07Bibliographically approved
Costa, T., Amer, A., Farag, S., Wolf-Watz, H., Fällman, M., Fahlgren, A., . . . Francis, M. (2013). Type III secretion translocon assemblies that attenuate Yersinia virulence. Cellular Microbiology, 15(7), 1088-1110
Open this publication in new window or tab >>Type III secretion translocon assemblies that attenuate Yersinia virulence
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2013 (English)In: Cellular Microbiology, ISSN 1462-5814, E-ISSN 1462-5822, Vol. 15, no 7, p. 1088-1110Article in journal (Refereed) Published
Abstract [en]

Type III secretion enables bacteria to intoxicate eukaryotic cells with anti-host effectors. A class of secreted cargo are the two hydrophobic translocators that form a translocon pore in the host cell plasma membrane through which the translocated effectors may gain cellular entry. In pathogenic Yersinia, YopB and YopD shape this translocon pore. Here, four in cis yopD mutations were constructed to disrupt a predicted α-helix motif at the C-terminus. Mutants YopD(I262P) and YopD(K267P) poorly localized Yop effectors into target eukaryotic cells and failed to resist uptake and killing by immune cells. These defects were due to deficiencies in host-membrane insertion of the YopD-YopB translocon. Mutants YopD(A263P) and YopD(A270P) had no measurable in vitro translocation defect, even though they formed smaller translocon pores in erythrocyte membranes. Despite this, all four mutants were attenuated in a mouse infection model. Hence, YopD variants have been generated that can spawn translocons capable of targeting effectors in vitro, yet were bereft of any lethal effect in vivo. Therefore, Yop translocators may possess other in vivo functions that extend beyond being a portal for effector delivery into host cells.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2013
Keywords
virulence, coiled-coil, effector delivery, pore formation, regulation, YopD
National Category
Microbiology Biochemistry and Molecular Biology Microbiology in the medical area
Research subject
Infectious Diseases; Microbiology; Molecular Biology
Identifiers
urn:nbn:se:umu:diva-67117 (URN)10.1111/cmi.12100 (DOI)000320394800004 ()
Funder
Swedish Research Council
Note

This work, performed within the framework of the Umea Centre for Microbial Research-Linnaeus Program, was supported by grants from the Carl Tryggers Foundation for Scientific Research (M. S. F.), Swedish Research Council (H.W.-W., M. F., T. E., M. S. F.), Foundation for Medical Research at Umea University (M. S. F.) and J C Kempe Memorial Fund (T. R. C., A. A. A.).

Available from: 2013-03-13 Created: 2013-03-13 Last updated: 2018-06-08Bibliographically approved
Costa, T. R. D., Amer, A. A. A., Fällman, M., Fahlgren, A. & Francis, M. (2012). Coiled-coils in the YopD translocator family: A predicted structure unique to the YopD N-terminus contributes to full virulence of Yersinia pseudotuberculosis. Infection, Genetics and Evolution, 12(8), 1729-1742
Open this publication in new window or tab >>Coiled-coils in the YopD translocator family: A predicted structure unique to the YopD N-terminus contributes to full virulence of Yersinia pseudotuberculosis
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2012 (English)In: Infection, Genetics and Evolution, ISSN 1567-1348, E-ISSN 1567-7257, Vol. 12, no 8, p. 1729-1742Article in journal (Refereed) Published
Abstract [en]

Pathogenic Yersinia all harbor a virulence plasmid-encoded Ysc–Yop T3SS. In this system, translocator function is performed by the hydrophobic proteins YopB and YopD. With the goal to better understand how YopD orchestrates yop-regulatory control, translocon pore formation and Yop effector translocation, we performed an in silico prediction of coiled-coil motifs in YopD and YopD-like sequences from other bacteria. Of interest was a predicted N-terminal coiled-coil that occurred solely in Yersinia YopD sequences. To investigate if this unique feature was biologically relevant, two in cis point mutations were generated with a view to disrupting this putative structure. Both mutants maintained full T3SS function in vitro in terms of environmental control of Yops synthesis and secretion, effector toxin translocation and evasion of phagocytosis and killing by cultured immune cells. However, these same mutants were attenuated for virulence in a murine oral-infection model. The cause of this tardy disease progression is unclear. However, these data indicate that any structural flaw in this element unique to the N-terminus will subtly compromise an aspect of YopD biology. Sub-optimal T3SSs are then formed that are unable to fortify Yersinia against attack by the host innate and adaptive immune response.

Place, publisher, year, edition, pages
Elsevier, 2012
Keywords
Pathogen-Host Interaction, Virulence Factor, Viruelnce, Bacteria
National Category
Medical and Health Sciences
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-59466 (URN)10.1016/j.meegid.2012.07.016 (DOI)
Funder
Swedish Research Council, 2009-5628
Available from: 2012-09-19 Created: 2012-09-14 Last updated: 2018-06-08Bibliographically approved
Costa, T. R. D. (2012). YopD translocator function in Yersinia pseudotuberculosis type III secretion. (Doctoral dissertation). Umeå: Umeå universitet
Open this publication in new window or tab >>YopD translocator function in Yersinia pseudotuberculosis type III secretion
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Type III secretion systems (T3SS) are a common feature of Gram-negative bacteria, allowing them to inject anti-host effectors into the interior of infected eukaryotic cells. By this mechanism, these virulence factors help the bacteria to modulate eukaryotic cell function in its favor and subvert host innate immunity. This promotes a less hostile environment in which infecting bacteria can colonize and cause disease.

In pathogenic Yersinia, a crucial protein in this process is YopD. YopD is a T3S substrate that, together with YopB, forms a translocon pore in the host cell membrane through which the Yop effectors may gain access to the target-cell cytosol. The assembly of the translocator pore in plasma membranes is considered a fundamental feature of all T3SSs. How the pore is formed, what determines the correct size and ultimately the stoichiometry between YopD YopB, is still unknown. Portions of YopD are also observed inside HeLa cells. Moreover, YopD functions together with its T3S chaperone, LcrH, to control Yops synthesis in the bacterial cytoplasm. The multifunctional YopD may influence all these processes by compartmentalizing activities into discrete modular domains along the protein length. Therefore, understanding how particular domains and/or residues within these regions coordinate multiple functions of the protein will provide a platform to improve our knowledge of the molecular mechanisms behind translocation through T3SSs.

Comprehensive site-directed mutagenesis of the YopD C-terminal amphipathic α-helix domain, pinpointed hydrophobic residues as important for YopD function. Some YopD variants were defective in self-assembly and in the ability to interact with the needle tip protein, LcrV, which were required to facilitate bacterial T3S activity. A similar mutagenesis approach was used to understand the role of the two predicted coiled-coils located at the N-terminal and C-terminal region of YopD. The predicted N-terminal element that occurs solely in the Yersinia YopD translocator family is essential for optimal T3SS and full disease progression. The predicted YopD C-terminal coiled-coil shapes a functional translocon inserted into host cell membranes. This translocon was seen to be a dynamic structure facilitating at least two roles during effectors delivery into cells; one to guarantee translocon pore insertion into target cell membranes and the other to promote targeted activity of internalized effector toxins.

In Yersinia expression of yop genes and secretion of the corresponding polypeptides is tightly regulated at a transcriptional and post-transcriptional level. If T3S chaperones of the translocator class are known to influence transcriptional output of T3SS genes in other bacteria, we show that in Yersinia the class II T3S chaperone LcrH has no such effect on the LcrF transcriptional activator activity. We also demonstrate that there are possibly additional yop-regulatory roles for the LcrH chaperone besides forming a stable complex with YopD to impose post-transcriptional silencing on Yops synthesis. This mechanism that relies upon an active T3SS, might act independently of both YopD and the regulatory element LcrQ.

In conclusion, this work has sought to delineate the encrypted functions of the YopD translocator that contribute to Yersinia T3SS-dependent pathogenesis. Contributions of the YopD cognate chaperone LcrH in yop regulatory control are also presented.  

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2012. p. 222
Keywords
Y. pseudotuberculosis, T3SS, translocon, YopD, coiled-coil, effector delivery, regulation, virulence
National Category
Medical and Health Sciences
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-61544 (URN)978-91-7459-483-6 (ISBN)
Public defence
2012-12-14, Major Groove, Biomedicinhuset, Byggnad 6L, Umeå University, Umeå, 09:00 (English)
Opponent
Supervisors
Available from: 2012-11-23 Created: 2012-11-19 Last updated: 2018-06-08Bibliographically approved
Costa, T. R., Edqvist, P. J., Bröms, J. E., Åhlund, M. K., Forsberg, Å. & Francis, M. S. (2010). YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis. Journal of Biological Chemistry, 285(33), 25269-25284
Open this publication in new window or tab >>YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis
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2010 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 285, no 33, p. 25269-25284Article in journal (Refereed) Published
Abstract [en]

YopD-like translocator proteins encoded by several Gram-negative bacteria are important for type III secretion-dependent delivery of anti-host effectors into eukaryotic cells. This probably depends on their ability to form pores in the infected cell plasma membrane, through which effectors may gain access to the cell interior. In addition, Yersinia YopD is a negative regulator essential for the control of effector synthesis and secretion. As a prerequisite for this functional duality, YopD may need to establish molecular interactions with other key T3S components. A putative coiled-coil domain and an alpha-helical amphipathic domain, both situated in the YopD C terminus, may represent key protein-protein interaction domains. Therefore, residues within the YopD C terminus were systematically mutagenized. All 68 mutant bacteria were first screened in a variety of assays designed to identify individual residues essential for YopD function, possibly by providing the interaction interface for the docking of other T3S proteins. Mirroring the effect of a full-length yopD gene deletion, five mutant bacteria were defective for both yop regulatory control and effector delivery. Interestingly, all mutations clustered to hydrophobic amino acids of the amphipathic domain. Also situated within this domain, two additional mutants rendered YopD primarily defective in the control of Yop synthesis and secretion. Significantly, protein-protein interaction studies revealed that functionally compromised YopD variants were also defective in self-oligomerization and in the ability to engage another translocator protein, LcrV. Thus, the YopD amphipathic domain facilitates the formation of YopD/YopD and YopD/LcrV interactions, two critical events in the type III secretion process.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 2010
Keywords
Bacteria, Bacterial Genetics, Protein Cross-linking, Protein-Protein Interactions, Secretion, Yersinia, Amphipathic, Coiled-coil, Pore Formation, Regulation
National Category
Microbiology in the medical area
Research subject
Infectious Diseases
Identifiers
urn:nbn:se:umu:diva-41848 (URN)10.1074/jbc.M110.144311 (DOI)000280682400020 ()20525687 (PubMedID)
Available from: 2011-04-11 Created: 2011-04-01 Last updated: 2018-06-08Bibliographically approved
Costa, T. R. D., Amer, A. A. A., Farag, S. I., Wolf-Watz, H., Fällman, M., Fahlgren, A., . . . Francis, M. S.Active type III translocon assemblies that attenuate Yersinia virulence.
Open this publication in new window or tab >>Active type III translocon assemblies that attenuate Yersinia virulence
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(English)Manuscript (preprint) (Other academic)
Abstract [en]

Type III secretion enables bacteria to intoxicate eukaryotic cells with anti-host effectors. A class of secreted cargo are the two hydrophobic translocators that form a translocon pore in the host cell plasma membrane through which the translocated effectors may gain cellular entry. In pathogenic Yersinia, YopB and YopD shape this translocon pore. Here, four in cis yopD mutations were constructed to disrupt a predicted a-helix motif at the C-terminus. Mutants YopDI262P and YopDK267P poorly localised Yop effectors into target eukaryotic cells and failed to resist uptake and killing by immune cells. These defects were due to deficiencies in host-membrane insertion of the YopD-YopB translocon. Mutants YopDA263P and YopDA270P had no measurable in vitro translocation defect, even though they formed smaller translocon pores in erythrocyte membranes. Despite this, all four mutants were attenuated in a mouse infection model. Hence, YopD variants have been generated that can spawn translocons capable of targeting effectors in vitro, yet were bereft of any lethal effect in vivo. It is therefore probable that an active translocon makes a range of contributions during bacteria-host cell contact that extends beyond effector delivery per se.

National Category
Microbiology in the medical area
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-61539 (URN)
Available from: 2012-11-19 Created: 2012-11-19 Last updated: 2018-06-08
Amer, A., Costa, T., Gurung,, J., Avican, U., Forsberg, Å. & Francis, M.Functional consequences of site-directed mutagenesis in theC-terminus of YopN, a Yersinia pseudotuberculosis regulator ofYop secretion.
Open this publication in new window or tab >>Functional consequences of site-directed mutagenesis in theC-terminus of YopN, a Yersinia pseudotuberculosis regulator ofYop secretion
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(English)Manuscript (preprint) (Other academic)
Abstract [en]

Pathogenic Yersinia spp. utilizes the Ysc-Yop type III secretion system to targetYop effector proteins into the cytosol of host immune cells. Internalizedeffectors alter specific signaling pathways to neutralize immune cell-dependentphagocytosis, killing and pro-inflammatory responsiveness. This enablesextracellular bacterial multiplication and survival in immune tissue. Central tothe temporal control of Yop type III secretion is the regulator YopN. Incomplex with TyeA, YopN acts to plug the inner face of the type III secretionchannel, denying entry to other Yop substrates until after YopN has beensecreted. A +1 frameshift event in the 3-prime end of yopN results in thesynthesis of a singular secreted YopN-TyeA polypeptide chimera that retainssome regulatory function. As the C-terminal coding sequence of YopN in thishybrid product differs greatly from native sequence, we used site-directedmutagenesis to determine the functional significance of this segment. YopNtruncated at residue 287 or containing a shuffled sequence covering 288 to 293retains full function both in vitro and in vivo. Thus, the extreme C-terminus isapparently superfluous to YopN function. In contrast, a YopN varianttruncated after residue 278 was completely unstable, and these bacteria hadlost all control of T3S activity, and failed to defend against immune cell killing.Interestingly, inclusion of a shuffled sequence from residues 279 to 287recovered some T3S control over function. Hence, the YopN segmentencompassing 279 to 287 is essential for full function, although the exact aminoacid sequence is less important.

National Category
Microbiology in the medical area
Research subject
Microbiology
Identifiers
urn:nbn:se:umu:diva-70112 (URN)
Projects
Controlling substrate export by the Ysc-Yop type III secretion system in Yersinia
Available from: 2013-05-05 Created: 2013-05-05 Last updated: 2018-06-08Bibliographically approved
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