Sequence and Expression of an Eisenia‐Fetida‐Derived cDNA Clone That Encodes the 40‐kDa Fetidin Antibacterial Protein
- 1 June 1997
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 246 (3) , 756-762
- https://doi.org/10.1111/j.1432-1033.1997.00756.x
Abstract
Fetidins are 40‐kDa and 45‐kDa hemolytic and antibacterial glycoproteins present in the coelomic fluid of the earthworm Eisenia fetida andrei. By screening a cDNA library with a polyclonal anti‐fetidin serum, we have cloned a cDNA that encoded the 40‐kDa fetidin. The clone contains an insert of 1.44 kb encoding a protein of 34 kDa, which corresponds to the size of deglycosylated fetidins. The recombinant protein inhibits Bacillus megaterium growth. Restriction fragment polymorphisms were observed on Southern blots and correspond to a known protein polymorphism. The sequence of the cDNA contains a peroxidase signature and fetidins from earthworm coelomic fluid have peroxidase activity. The 40‐kDa and 45‐kDa fetidins therefore represent two related polymorphic defence factors in invertebrates.Keywords
This publication has 34 references indexed in Scilit:
- Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andreiBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Peptide Antibiotics and Their Role in Innate ImmunityAnnual Review of Immunology, 1995
- Peptide Antibiotics and Their Role in Innate ImmunityAnnual Review of Immunology, 1995
- Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamilyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Hemolin: an Insect-Immune Protein Belonging to the Immunoglobulin SuperfamilyScience, 1990
- Insect immunityEuropean Journal of Biochemistry, 1988
- Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase FBiochemistry, 1985
- Insect Immunity: Isolation and Structure of Cecropins B and D from Pupae of the Chinese Oak Silk Moth, Antheraea pernyiEuropean Journal of Biochemistry, 1982
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979