Characterization of Afb, a Novel Bifunctional Protein in Streptococcus Agalactiae



Dehbashi S¹ ; Pourmand MR² ; Mashhadi R² Show Affiliations
Source: Iranian Journal of Microbiology Published:2016

Abstract

Background and Objectives: Streptococcus agalactiaeis the leading cause of bacterial sepsis and meningitis in newborns and results in pneumonia and bacteremia in adults. A number ofS. agalactiaecomponents 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 ofS. agalactiaewas investigated. Materials and Methods:Thegbs1805gene was cloned and expressed.E. colistrains 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, insilicoanalysis 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. © 2016, Tehran University of Medical Science. All Rights reserved.