FbsA-driven fibrinogen polymerization: a bacterial "deceiving strategy".
We show that FbsA, a cell wall protein of the bacterium Streptococcus agalactiae, promotes large-scale aggregation of human plasma fibrinogen, leading to the formation of a semiflexible polymerlike network. This extensive aggregation process takes place not only in solution, but also on FbsA-functionalized colloidal particles, and leads to the formation of a thick layer on the bacterial cell wall itself, which becomes an efficient mask against phagocytosis.
Dipartimento di Ingegneria Nucleare, CSGI-Politecnico di Milano, via Ponzio 34/3, 20133 Milano, Italy.
Matteo
M
Pierno
Laura
L
Maravigna
Roberto
R
Piazza
Livia
L
Visai
Pietro
P
Speziale
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D003102:Colloids; D005340:Fibrinogen / Q000737:chemistry / Q000378:metabolism*; D013292:Streptococcus agalactiae / Q000378:metabolism*
D001426:Bacterial Proteins; D001704:Biopolymers; D002352:Carrier Proteins; D003102:Colloids; C499709:FbsA protein, Streptococcus agalactiae; D005340:Fibrinogen