TY - JOUR
T1 - Two repetitive, biofilm-forming proteins from Staphylococci
T2 - From disorder to extension
AU - Whelan, Fiona
AU - Potts, Jennifer R.
PY - 2015/10/1
Y1 - 2015/10/1
N2 - Staphylococcus aureus and Staphylococcus epidermidis are an important cause of medical device-related infections that are difficult to treat with antibiotics. Biofilms, in which bacteria are embedded in a bacteriallyproduced exopolymeric matrix, form on the surface of the implanted medical device. Our understanding of the molecular mechanisms underlying the initial surface attachment and subsequent intercellular interactions as the biofilm matures is improving. Biofilm accumulation can be mediated by a partially deacetylated form of poly-N-acetylglucosamine (PNAG) but, more recently, the role of bacterial surface proteins is being recognized. Here we describe the structure and function of two S. aureus cell surface proteins, FnBPA and SasG, implicated in host interactions and biofilm accumulation. These multifunctional proteins employ intrinsic disorder for distinct molecular outcomes. In the case of FnBPA, disorder generates adhesive arrays that bind fibronectin (Fn); in the case of SasG, disorder is, counterintuitively, used to maintain a strong extended fold.
AB - Staphylococcus aureus and Staphylococcus epidermidis are an important cause of medical device-related infections that are difficult to treat with antibiotics. Biofilms, in which bacteria are embedded in a bacteriallyproduced exopolymeric matrix, form on the surface of the implanted medical device. Our understanding of the molecular mechanisms underlying the initial surface attachment and subsequent intercellular interactions as the biofilm matures is improving. Biofilm accumulation can be mediated by a partially deacetylated form of poly-N-acetylglucosamine (PNAG) but, more recently, the role of bacterial surface proteins is being recognized. Here we describe the structure and function of two S. aureus cell surface proteins, FnBPA and SasG, implicated in host interactions and biofilm accumulation. These multifunctional proteins employ intrinsic disorder for distinct molecular outcomes. In the case of FnBPA, disorder generates adhesive arrays that bind fibronectin (Fn); in the case of SasG, disorder is, counterintuitively, used to maintain a strong extended fold.
KW - Biofilm
KW - FnBPA
KW - SasG
KW - Staphylococcus aureus
UR - http://www.scopus.com/inward/record.url?scp=84947272804&partnerID=8YFLogxK
U2 - 10.1042/BST20150088
DO - 10.1042/BST20150088
M3 - Article
AN - SCOPUS:84947272804
VL - 43
SP - 861
EP - 866
JO - Biochemical Society transactions
JF - Biochemical Society transactions
SN - 0300-5127
IS - 5
ER -