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Duus, K. et al.

Karen Duus, Nicole M. Thielens, Monique Lacroix, Pascale Tacnet, Philippe Frachet, Uffe Holmskov, Gunnar Houen,

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, 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.[1]

References

CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site. Duus, K., Thielens, N.M., Lacroix, M., Tacnet, P., Frachet, P., Holmskov, U., Houen, G. FEBS J. (2010) [Pubmed]

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