TAILIEUCHUNG - Báo cáo khoa học: CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site

CD91 plays an important role in the scavenging of apoptotic material, pos-sibly through binding to soluble pattern-recognition molecules. In this study, we investigated the interaction of CD91 with mannan-binding lectin (MBL), ficolins and lung surfactant proteins. Both MBL and L-ficolin were found to bind CD91. The MBL–CD91 interaction was time- and concentra-tion-dependent and could be inhibited by known ligands of CD91. | CD91 interacts with mannan-binding lectin MBL through the MBL-associated serine protease-binding site Karen Duus1 Nicole M. Thielens2 Monique Lacroix2 Pascale Tacnet2 Philippe Frachet2 Uffe Holmskov3 and Gunnar Houen1 1 Department of ClinicalBiochemistry and Immunology Statens Serum Institut Artillerivej 5 Copenhagen Denmark 2 Laboratoire d Enzymologie Moleculaire Institut de Biologie Structurale Jean-Pierre Ebel Commissariat à l Energie Atomique CNRS UMR 5075 Universite Joseph Fourier 41 rue Jules Horowitz Grenoble Cedex 1 France 3 Department of Cardiovascular and RenalResearch Institute of Molecular Medicine University of Southern Denmark Odense Denmark Keywords CD91 clearance ficolin complement mannan-binding lectin MBL scavenging Correspondence K. Duus Department of Clinical Biochemistry and Immunology Statens Serum Institut Artillerivej 5 DK-2300 Copenhagen Denmark Fax 45 32683149 Tel 45 32688241 E-mail kds@ Received 12 August 2010 revised 20 September 2010 accepted 4 October 2010 doi CD91 plays an important role in the scavenging of apoptotic material possibly through binding to soluble pattern-recognition molecules. In this study we investigated the interaction of CD91 with mannan-binding lectin MBL ficolins and lung surfactant proteins. Both MBL and L-ficolin were found to bind CD91. The MBL-CD91 interaction was time- and concentration-dependent and could be inhibited by known ligands of CD91. MBL-associated serine protease 3 MASP-3 also inhibited binding between MBL and CD91 suggesting that the site of interaction is located at or near the MASP-MBL interaction site. This was confirmed by using MBL mutants deficient for MASP binding that were unable to interact with CD91. These findings demonstrate that MBL and L-ficolin interact with CD91 strongly suggesting that they have the potential to function as soluble recognition molecules for scavenging microbial and apoptotic material by CD91. Structured digital abstract .

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