Helix pomatia Lectin, an inducer of Drosophila immune response, binds to Hemomucin, a novel surface Mucin
Date
1996
Authors
Theopold, Ulrich
Samakovlis, Christos
Erdjument-Bromage, Hediye
Dillon, Natalie
Axelsson, Bernt
Schmidt, Otto
Tempst, Paul
Hultmark, Dan
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Journal of Biological Chemistry, 1996; 271(22):12708-12715
Statement of Responsibility
Ulrich Theopold, Christos Samakovlis, Hediye Erdjument-Bromage, Natalie Dillon, Bernt Axelsson, Otto Schmidt, Paul Tempst, and Dan Hultmark
Conference Name
Abstract
We describe the isolation and initial characterization of hemomucin, a novel Drosophila surface mucin that is likely to be involved in the induction of antibacterial effector molecules after binding a snail lectin (Helix pomatia A hemagglutinin). Two proteins of 100 and 220 kDa were purified from the membrane fraction of a Drosophila blood cell line using lectin columns. The two proteins are products of the same gene, as demonstrated by peptide sequencing. The corresponding cDNAs code for a product that contains an amino-terminal putative transmembrane domain, a domain related to the plant enzyme strictosidine synthase, and a mucin-like domain in the carboxyl-terminal part of the protein. The gene is expressed throughout development. In adult flies, high expression is found in hemocytes, in specialized regions of the gut, and in the ovary, where the protein is deposited onto the egg surface. In the gut, the mucin co-localizes with the peritrophic membrane. The cytogenetic location of the gene is on the third chromosome in the region 97F-98A.
School/Discipline
School of Agriculture, Food and Wine : Plant and Food Science
Dissertation Note
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© 1996 by The American Society for Biochemistry and Molecular Biology, Inc.