Author/Authors :
AFSHAR, Davoud Dept. of Pathobiology - School of Public Health - Tehran University of Medical Sciences, Tehran , POURMAND, Mohammad Reza Dept. of Pathobiology - School of Public Health - Tehran University of Medical Sciences, Tehran , JEDDI-TEHRANI, Mahmood Monoclonal Antibody Research Center - Avicenna Research Institute - ACECR, Tehran , SABOOR YARAGHI, Ali Akbar Dept. of Pathobiology - School of Public Health - Tehran University of Medical Sciences, Tehran , AZARSA, Mohammad Dept. of Pathobiology - School of Public Health - Tehran University of Medical Sciences, Tehran , SHOKRI, Fazel Dept. of Immunology - School of Public Health - Tehran University of Medical Sciences, Tehran
Abstract :
Background: Choline-binding proteins (CBPs) are a group of surface-exposed proteins, which play crucial and physi-ological roles in Streptococcus pneumoniae. The novel member of CBPs, choline-binding protein M (CbpM) may have binding activity to plasma proteins. This study aimed to clone and express CbpM and demonstrate its interaction with plasma proteins and patients’ sera.
Methods: The total length of cbpM gene was cloned in pET21a vector and expressed in BL21 expression host. Verifi-cation of recombinant protein was evaluated by Western blot using anti-His tag monoclonal antibody. Binding ability of the recombinant protein to plasma proteins and the interaction with patients’ sera were assessed by Western blot and ELISA methods.
Results: The cbpM gene was successfully cloned into pET21a and expressed in BL21 host. Binding activity to fibro-nectin and fibrinogen and antibody reaction of CbpM to patients’ sera was demonstrated by Western blot and ELISA methods, respectively.
Conclusion: CbpM is one of the pneumococcal surface-exposed proteins, which mediates pneumococcal binding to fibronectin and fibrinogen proteins.
Keywords :
Streptococcus pneumoniae , Choline-binding protein M, Fibrinogen , Fibronectin
