Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene
The Journal of Immunology, 1999•journals.aai.org
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-
associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway
of complement activation by binding to carbohydrate structures present on bacteria, yeast,
and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to
those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with
the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as …
associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway
of complement activation by binding to carbohydrate structures present on bacteria, yeast,
and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to
those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with
the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as …
Abstract
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
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