Abstract
The lectin pathway provides an antibody independent route of complement activation. Mannan-binding lectin (MBL) can form compound with MBL-associated serine proteases (MASPs) through its collagen-like region (CLR) to initiate complement fixation. In this study, we designed and synthesized a range of peptides according to the sequence of CLR in human MBL, which were assumed to block the MBL-MASP interaction, in order to locate the serine protease binding motifs on human MBL. It was demonstrated that MASPs bind on the C-terminal side of the hinge region formed by an interruption in the Gly-X-Y repeat pattern of the collagen-like domain. In addition, Arg32Cys, Gly35Asp and Gly37Glu mutant proteins have the similar serine protease binding characteristic with wild type MBL, but the binding between mutated MBL proteins and MASPs is much weaker than that between wild type MBL protein and MASPs.
Keywords: Mannan-binding lectin (MBL), collagen-like region (CLR), interruption, MBL-associated serine proteases (MASPs), binding motifs, synthetic peptides
Protein & Peptide Letters
Title: Location of MBL-Associated Serine Proteases Binding Motifs on Human Mannan-Binding Lectin (MBL)
Volume: 17 Issue: 1
Author(s): Daming Zuo, Xuemin Cai, Na Zhao, Liyun Zhang and Zhengliang Chen
Affiliation:
Keywords: Mannan-binding lectin (MBL), collagen-like region (CLR), interruption, MBL-associated serine proteases (MASPs), binding motifs, synthetic peptides
Abstract: The lectin pathway provides an antibody independent route of complement activation. Mannan-binding lectin (MBL) can form compound with MBL-associated serine proteases (MASPs) through its collagen-like region (CLR) to initiate complement fixation. In this study, we designed and synthesized a range of peptides according to the sequence of CLR in human MBL, which were assumed to block the MBL-MASP interaction, in order to locate the serine protease binding motifs on human MBL. It was demonstrated that MASPs bind on the C-terminal side of the hinge region formed by an interruption in the Gly-X-Y repeat pattern of the collagen-like domain. In addition, Arg32Cys, Gly35Asp and Gly37Glu mutant proteins have the similar serine protease binding characteristic with wild type MBL, but the binding between mutated MBL proteins and MASPs is much weaker than that between wild type MBL protein and MASPs.
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Cite this article as:
Zuo Daming, Cai Xuemin, Zhao Na, Zhang Liyun and Chen Zhengliang, Location of MBL-Associated Serine Proteases Binding Motifs on Human Mannan-Binding Lectin (MBL), Protein & Peptide Letters 2010; 17 (1) . https://dx.doi.org/10.2174/092986610789909566
DOI https://dx.doi.org/10.2174/092986610789909566 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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