Structural insights into serine-rich fimbriae from Gram-positive bacteria.

Stéphanie Ramboarina (1) , James A Garnett (1) , Meixian Zhou (2) , Yuebin Li (2) , Zhixiang Peng (2) , Jonathan D Taylor (1) , Wei-Chao Lee (1) , Andrew Bodey (1) , James W Murray (1) , Yilmaz Alguel (1) , Julien Bergeron (1, 3) , Benjamin Bardiaux (4) , Elizabeth Sawyer (1) , Rivka Isaacson (1) , Camille Tagliaferri (1) , Ernesto Cota (1) , Michael Nilges (4) , Peter Simpson (1) , Teresa Ruiz (5) , Hui Wu , Stephen Matthews (1)

1 Centre for Structural Biology [London]
2 UAB - University of Alabama at Birmingham [ Birmingham]
3 King‘s College London
4 Bioinformatique Structurale
5 University of Vermont [Burlington]

The serine-rich repeat family of fimbriae play important roles in the pathogenesis of streptococci and staphylococci. Despite recent attention, their finer structural details and precise adhesion mechanisms have yet to be determined. Fap1 (Fimbriae-associated protein 1) is the major structural subunit of serine-rich repeat fimbriae from Streptococcus parasanguinis and plays an essential role in fimbrial biogenesis, adhesion, and the early stages of dental plaque formation. Combining multidisciplinary, high resolution structural studies with biological assays, we provide new structural insight into adhesion by Fap1. We propose a model in which the serine-rich repeats of Fap1 subunits form an extended structure that projects the N-terminal globular domains away from the bacterial surface for adhesion to the salivary pellicle. We also uncover a novel pH-dependent conformational change that modulates adhesion and likely plays a role in survival in acidic environments.

Domains: Life Sciences [q-bio]; Quantitative Methods [q-bio.QM]

Stéphanie Ramboarina, James A Garnett, Meixian Zhou, Yuebin Li, Zhixiang Peng, et al.. Structural insights into serine-rich fimbriae from Gram-positive bacteria.. Journal of Biological Chemistry, 2010, 285 (42), pp.32446-57. ⟨10.1074/jbc.M110.128165⟩. ⟨pasteur-01500608⟩