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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2021-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-020-01621-w |
| Summary: | 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. |
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| ISSN: | 2399-3642 |