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<p><strong>Background:</strong> Choline-binding proteins (CBPs) are a group of surface-exposed proteins, which play crucial and physiological roles in <em>Streptococcus pneumoniae</em>. 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.</p><p><strong>Methods:</strong> The total length of <em>cbp</em>M gene was cloned in <em>p</em>ET21a vector and expressed in BL21 expression host. Verification 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.</p><p><strong>Results:</strong> The <em>cbp</em>M gene was successfully cloned into <em>p</em>ET21a and expressed in BL21 host. Binding activity to fibronectin and fibrinogen and antibody reaction of CbpM to patients’ sera was demonstrated by Western blot and ELISA methods, respectively.</p><p><strong>Conclusion:</strong> CbpM is one of the pneumococcal surface-exposed proteins, which mediates pneumococcal binding to fibronectin and fibrinogen proteins.</p><p> </p>