TY - JOUR
T1 - Structural insights into serine-rich fimbriae from gram-positive bacteria
AU - Ramboarina, Stéphanie
AU - Garnett, James A.
AU - Zhou, Meixian
AU - Li, Yuebin
AU - Peng, Zhixiang
AU - Taylor, Jonathan D.
AU - Lee, Wei Chao
AU - Bodey, Andrew
AU - Murray, James W.
AU - Alguel, Yilmaz
AU - Bergeron, Julien
AU - Bardiaux, Benjamin
AU - Sawyer, Elizabeth
AU - Isaacson, Rivka
AU - Tagliaferri, Camille
AU - Cota, Ernesto
AU - Nilges, Michael
AU - Simpson, Peter
AU - Ruiz, Teresa
AU - Wu, Hui
AU - Matthews, Stephen
PY - 2010/10/15
Y1 - 2010/10/15
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M110.128165
DO - 10.1074/jbc.M110.128165
M3 - Article
C2 - 20584910
AN - SCOPUS:77957772755
SN - 0021-9258
VL - 285
SP - 32446
EP - 32457
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -