Journal
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 34, Issue 3, Pages 323-330Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2009.11.003
Keywords
Saposin-like proteins; Caenopore-5; Structure; Pore-forming peptide; NMR; C. elegans
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Funding
- Deutsche Forschungsgemeinschaft
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The caenopore-5 protein encoded by the spp-5 gene is one of the 33 caenopores identified in Caenorhabditis elegans and is a pore-forming peptide which plays an important role in the elimination of Escherichia coli ingested by the worm. Thus, caenopore-5 appears to contribute to the nutrition of the worm while simultaneously protecting the organism against pathogens. Here, three-dimensional heteronuclear NMR spectroscopy was used to solve the solution structure of caenopore-5. The NMR data revealed that two conformers of caenopore-5 exist in solution which differ by the isomerization of the peptide bond of Pro-81. The overall structure of the two caenopore-5 conformers consists of five amphiphatic helices connected by three disulfide bonds. The five helices are arranged in a folded leaf which is the characteristic signature of the SAPLIP family. The structure presented here is the first of an effector protein of the defensive system elucidated for the well-known model organism C. elegans. (C) 2009 Elsevier Ltd. All rights reserved.
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