Abstract
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.
© 2010 The Authors Journal compilation © 2010 FEBS.
MeSH terms
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Amino Acid Substitution
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Antigens, CD / chemistry*
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Antigens, CD / metabolism*
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Binding Sites / genetics
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Calcium / metabolism
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Ficolins
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Humans
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In Vitro Techniques
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Kinetics
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Lectins / chemistry
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Lectins / metabolism
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Ligands
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Low Density Lipoprotein Receptor-Related Protein-1
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Mannose-Binding Lectin / chemistry*
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Mannose-Binding Lectin / genetics
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Mannose-Binding Lectin / metabolism*
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Mannose-Binding Protein-Associated Serine Proteases / chemistry*
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Mannose-Binding Protein-Associated Serine Proteases / metabolism*
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Mutagenesis, Site-Directed
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Mutant Proteins / chemistry
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Mutant Proteins / genetics
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Mutant Proteins / metabolism
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Protein Binding
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Surface Plasmon Resonance
Substances
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Antigens, CD
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LRP1 protein, human
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Lectins
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Ligands
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Low Density Lipoprotein Receptor-Related Protein-1
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MBL2 protein, human
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Mannose-Binding Lectin
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Mutant Proteins
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Recombinant Proteins
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MASP1 protein, human
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Mannose-Binding Protein-Associated Serine Proteases
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Calcium