Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide

Heidler et al. report a structure of the N-terminal half of a bacterial fimbrial protein, Mfa5, from Porphyromonas gingivalis that is a secondary colonizer of the oral biofilm. They find a von Willebrand factor domain and two IgG-like domains in this structure. This study suggests that horizontal ge...

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Main Authors: Thomas V. Heidler, Karin Ernits, Agnieszka Ziolkowska, Rolf Claesson, Karina Persson
Format: Article
Language:English
Published: Nature Publishing Group 2021-01-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-020-01621-w
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spelling doaj-4c8c2f86b7064af38855be75652269bb2021-01-31T16:16:40ZengNature Publishing GroupCommunications Biology2399-36422021-01-01411910.1038/s42003-020-01621-wPorphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptideThomas V. Heidler0Karin Ernits1Agnieszka Ziolkowska2Rolf Claesson3Karina Persson4Department of Chemistry, Umeå Centre for Microbial Research (UCMR), Umeå UniversityDepartment of Chemistry, Umeå Centre for Microbial Research (UCMR), Umeå UniversityDepartment of Chemistry, Umeå Centre for Microbial Research (UCMR), Umeå UniversityDepartment of Odontology, Umeå UniversityDepartment of Chemistry, Umeå Centre for Microbial Research (UCMR), Umeå UniversityHeidler et al. report a structure of the N-terminal half of a bacterial fimbrial protein, Mfa5, from Porphyromonas gingivalis that is a secondary colonizer of the oral biofilm. They find a von Willebrand factor domain and two IgG-like domains in this structure. This study suggests that horizontal gene transfer may have occurred among the bacteria within the oral biofilm.https://doi.org/10.1038/s42003-020-01621-w
collection DOAJ
language English
format Article
sources DOAJ
author Thomas V. Heidler
Karin Ernits
Agnieszka Ziolkowska
Rolf Claesson
Karina Persson
spellingShingle Thomas V. Heidler
Karin Ernits
Agnieszka Ziolkowska
Rolf Claesson
Karina Persson
Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
Communications Biology
author_facet Thomas V. Heidler
Karin Ernits
Agnieszka Ziolkowska
Rolf Claesson
Karina Persson
author_sort Thomas V. Heidler
title Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
title_short Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
title_full Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
title_fullStr Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
title_full_unstemmed Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide
title_sort porphyromonas gingivalis fimbrial protein mfa5 contains a von willebrand factor domain and an intramolecular isopeptide
publisher Nature Publishing Group
series Communications Biology
issn 2399-3642
publishDate 2021-01-01
description Heidler et al. report a structure of the N-terminal half of a bacterial fimbrial protein, Mfa5, from Porphyromonas gingivalis that is a secondary colonizer of the oral biofilm. They find a von Willebrand factor domain and two IgG-like domains in this structure. This study suggests that horizontal gene transfer may have occurred among the bacteria within the oral biofilm.
url https://doi.org/10.1038/s42003-020-01621-w
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