Publication: Coiled-coil irregularities of the M1 protein structure promote M1-fibrinogen interaction and influence group A Streptococcus host cell interactions and virulence
Coiled-coil irregularities of the M1 protein structure promote M1-fibrinogen interaction and influence group A Streptococcus host cell interactions and virulence
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Uchiyama, S., Andreoni, F., Zürcher, C., Schilcher, K., Ender, M., Madon, J., Matt, U., Ghosh, P., Nizet, V., Schuepbach, R. A., & Zinkernagel, A. S. (2013). Coiled-coil irregularities of the M1 protein structure promote M1-fibrinogen interaction and influence group A Streptococcus host cell interactions and virulence. Journal of Molecular Medicine, 91(7), 861–869. https://doi.org/10.1007/s00109-013-1012-6
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Group A Streptococcus (GAS) is a human pathogen causing a wide range of mild to severe and life-threatening diseases. The GAS M1 protein is a major virulence factor promoting GAS invasiveness and resistance to host innate immune clearance. M1 displays an irregular coiled-coil structure, including the B-repeats that bind fibrinogen. Previously, we found that B-repeat stabilisation generates an idealised version of M1 (M1) characterised by decreased fibrinogen binding in vitro. To extend these findings based on a soluble truncated versi
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- Uchiyama, Satoshi
- Andreoni, Federica
- Zürcher, Claudia
- Schilcher, Katrin
- Ender, Miriam
- Madon, Jerzy
- Matt, Ulrich
- Ghosh, Partho
- Nizet, Victor
- Schuepbach, Reto A
- Zinkernagel, Annelies S
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Uchiyama, S., Andreoni, F., Zürcher, C., Schilcher, K., Ender, M., Madon, J., Matt, U., Ghosh, P., Nizet, V., Schuepbach, R. A., & Zinkernagel, A. S. (2013). Coiled-coil irregularities of the M1 protein structure promote M1-fibrinogen interaction and influence group A Streptococcus host cell interactions and virulence. Journal of Molecular Medicine, 91(7), 861–869. https://doi.org/10.1007/s00109-013-1012-6
