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Publications (4 of 4) Show all publications
Nadeem, A., Nagampalli, R., Toh, E., Alam, A., Myint, S. L., Heidler, T., . . . Persson, K. (2021). A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion. Proceedings of the National Academy of Sciences of the United States of America, 118(47), Article ID e2111418118.
Open this publication in new window or tab >>A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion
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2021 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 118, no 47, article id e2111418118Article in journal (Refereed) Published
Abstract [en]

Vibrio cholerae, responsible for outbreaks of cholera disease, is a highly motile organism by virtue of a single flagellum. We describe how the flagellum facilitates the secretion of three V. cholerae proteins encoded by a hitherto-unrecognized genomic island. The proteins MakA/B/E can form a tripartite toxin that lyses erythrocytes and is cytotoxic to cultured human cells. A structural basis for the cytolytic activity of the Mak proteins was obtained by X-ray crystallography. Flagellum-facilitated secretion ensuring spatially coordinated delivery of Mak proteins revealed a role for the V. cholerae flagellum considered of particular significance for the bacterial environmental persistence. Our findings will pave the way for the development of diagnostics and therapeutic strategies against pathogenic Vibrionaceae.

National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-191257 (URN)10.1073/pnas.2111418118 (DOI)000727697700014 ()34799450 (PubMedID)2-s2.0-85121209218 (Scopus ID)
Funder
Swedish Research Council, 2016-05009Swedish Research Council, 2018-02914Swedish Research Council, 2019-01720Swedish Research Council, 2007-08673The Kempe Foundations, SMK-1756.2The Kempe Foundations, SMK-1553The Kempe Foundations, JCK-1728Swedish Cancer Society, 2017-419The Kempe Foundations, SMK-1961Swedish Research Council
Available from: 2022-01-12 Created: 2022-01-12 Last updated: 2023-05-11Bibliographically approved
Heidler, T. & Persson, K. (2021). Crystallization of Recombinant Fimbrial Proteins of Porphyromonas gingivalis (1ed.). In: Keiji Nagano and Yoshiaki Hasegawa (Ed.), Periodontal Pathogens: Methods and Protocols (pp. 87-96). Humana Press
Open this publication in new window or tab >>Crystallization of Recombinant Fimbrial Proteins of Porphyromonas gingivalis
2021 (English)In: Periodontal Pathogens: Methods and Protocols / [ed] Keiji Nagano and Yoshiaki Hasegawa, Humana Press, 2021, 1, p. 87-96Chapter in book (Refereed)
Abstract [en]

Porphyromonas gingivalis fimbriae play a critical role in colonization. Elucidation of the fimbrial structure in atomic detail is important for understanding the colonization mechanism and to provide means to combat periodontitis. X-ray crystallography is a technique that is used to obtain detailed information of proteins along with bound ligands and ions. Crystallization of the protein of interest is the first step toward structure determination. Unfortunately it is not possible to predict the crystallization condition of a certain protein or even if the protein can be crystallized. Protein crystallization is, on the contrary, a matter of trial and error. However, the best strategy for success is to focus on the protein purification step to obtain a sample that is pure, stable, homogeneous and of high concentration. This chapter addresses general methods for crystallization of fimbrial proteins.

Place, publisher, year, edition, pages
Humana Press, 2021 Edition: 1
Series
Methods in Molecular Biology (MIMB), ISSN 1064-3745, E-ISSN 1940-6029 ; 2210
Keywords
Protein purification, Crystallization, Optimization, Fimbriae
National Category
Microbiology in the medical area Structural Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-184186 (URN)10.1007/978-1-0716-0939-2_9 (DOI)32815130 (PubMedID)2-s2.0-85090229731 (Scopus ID)978-1-0716-0938-5 (ISBN)978-1-0716-0941-5 (ISBN)978-1-0716-0939-2 (ISBN)
Available from: 2021-06-10 Created: 2021-06-10 Last updated: 2021-11-26Bibliographically approved
Heidler, T. ., Ernits, K., Ziolkowska, A., Claesson, R. & Persson, K. (2021). Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide. Communications Biology, 4(1), Article ID 106.
Open this publication in new window or tab >>Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
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2021 (English)In: Communications Biology, E-ISSN 2399-3642, Vol. 4, no 1, article id 106Article in journal (Refereed) Published
Abstract [en]

The Gram-negative bacterium Porphyromonas gingivalis is a secondary colonizer of the oral biofilm and is involved in the onset and progression of periodontitis. Its fimbriae, of type-V, are important for attachment to other microorganisms in the biofilm and for adhesion to host cells. The fimbriae are assembled from five proteins encoded by the mfa1 operon, of which Mfa5 is one of the ancillary tip proteins. Here we report the X-ray structure of the N-terminal half of Mfa5, which reveals a von Willebrand factor domain and two IgG-like domains. One of the IgG-like domains is stabilized by an intramolecular isopeptide bond, which is the first such bond observed in a Gram-negative bacterium. These features make Mfa5 structurally more related to streptococcal adhesins than to the other P. gingivalis Mfa proteins. The structure reported here indicates that horizontal gene transfer has occurred among the bacteria within the oral biofilm.

Place, publisher, year, edition, pages
Springer Nature, 2021
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-180642 (URN)10.1038/s42003-020-01621-w (DOI)000613287300001 ()33495563 (PubMedID)2-s2.0-85099767147 (Scopus ID)
Available from: 2021-02-24 Created: 2021-02-24 Last updated: 2021-02-24Bibliographically approved
Persson, K., Hall, M., Heidler, T. & Hasegawa, Y. (2018). Structural studies of the five pilin proteins building up the type-V pilus Mfa1 of Porphyromonas gingivalis. Acta Crystallographica Section A: Foundations and Advances, 74, E425-E425
Open this publication in new window or tab >>Structural studies of the five pilin proteins building up the type-V pilus Mfa1 of Porphyromonas gingivalis
2018 (English)In: Acta Crystallographica Section A: Foundations and Advances, E-ISSN 2053-2733, Vol. 74, p. E425-E425Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
International Union of Crystallography, 2018
Keywords
pill, polynraerizaticxaa, bacteria
Identifiers
urn:nbn:se:umu:diva-161753 (URN)10.1107/S2053273318088800 (DOI)000474406600648 ()
Available from: 2019-07-25 Created: 2019-07-25 Last updated: 2024-01-05Bibliographically approved
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ORCID iD: ORCID iD iconorcid.org/0000-0002-5997-3945

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