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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2021-01-01
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Series: | Communications Biology |
Online Access: | https://doi.org/10.1038/s42003-020-01621-w |
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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 |
work_keys_str_mv |
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