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Fibrinogen and Fibronectin Binding Activity and Immunogenic Nature of Choline Binding Protein M



Afshar D1 ; Pourmand MR1, 2 ; Jedditehrani M3 ; Saboor Yaraghi AA1 ; Azarsa M1 ; Shokri F4
Authors
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Authors Affiliations
  1. 1. Dept. of Pathobiology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran
  2. 2. Urology Research Center, Tehran University of Medical Sciences, Tehran, Iran
  3. 3. Monoclonal Antibody Research Center, Avicenna Research Institute, ACECR, Tehran, Iran
  4. 4. Dept. of Immunology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran

Source: Iranian Journal of Public Health Published:2016

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 fibron-ectin 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. © 2016, Iranian Journal of Public Health. All rights reserved.