RGD Reference Report - Dominant effects of mutations in the collagenous domain of mannose-binding protein. - Rat Genome Database

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Dominant effects of mutations in the collagenous domain of mannose-binding protein.

Authors: Wallis, R 
Citation: Wallis R J Immunol 2002 May 1;168(9):4553-8.
RGD ID: 625609
Pubmed: PMID:11971002   (View Abstract at PubMed)

Individuals heterozygous for mutant alleles encoding serum mannose-binding protein (MBP, also known as mannose-binding lectin) show increased susceptibility to infections caused by a wide range of pathogenic microorganisms. To investigate the molecular defects associated with heterozygosity, wild-type rat serum MBP polypeptides (MBP-A: 56% identical in sequence to human MBP) and rat MBP polypeptides containing mutations associated with human immunodeficiency have been coexpressed using a well-characterized mammalian expression system. The resulting proteins are secreted almost exclusively as heterooligomers that are defective in activating the complement cascade. Functional defects are caused by structural changes to the N-terminal collagenous and cysteine-rich domains of MBP, disrupting interactions with associated serine proteases. The dominant effects of the mutations demonstrate how the presence of a single mutant allele gives rise to the molecular defects that lead to the disease phenotype in heterozygous individuals.



Objects referenced in this article
Gene Mbl1 mannose binding lectin 1 Rattus norvegicus

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