Characterization of Afb, a novel bifunctional protein in Streptococcus agalactiae.
OBJECTIVE
Streptococcus agalactiae is the leading cause of bacterial sepsis and meningitis in newborns and results in pneumonia and bacteremia in adults. A number of S. agalactiae components are involved in colonization of target cells. Destruction of peptidoglycan and division of covalently linked daughter cells is mediated by autolysins. In this study, autolytic activity and plasma binding ability of AFb novel recombinant protein of S. agalactiae was investigated.


METHODS
The gbs1805 gene was cloned and expressed. E. coli strains DH5α and BL21 were used as cloning and expression hosts, respectively. After purification, antigenicity and binding ability to plasma proteins of the recombinant protein was evaluated.


RESULTS
AFb, the 18KDa protein was purified successfully. The insoluble mature protein revealed the ability to bind to fibrinogen and fibronectin. This insoluble mature protein revealed that it has the ability to bind to fibrinogen and fibronectin plasma proteins. Furthermore, in silico analysis demonstrated the AFb has an autolytic activity.


CONCLUSIONS
AFb is a novel protein capable of binding to fibrinogen and fibronectin. This findings lay a ground work for further investigation of the role of the bacteria in adhesion and colonization to the host.
Department of Pathobiology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran.
Sanaz
S
Dehbashi
Urology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
Mohammad Reza
MR
Pourmand
Urology Research Center, Tehran University of Medical Sciences, Tehran, Iran.
Rahil
R
Mashhadi
Autolysin; Fibrinogen; Fibronectin; Streptococcus agalactiae