Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization

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A novel antimicrobial peptide was isolated and characterized from the earthworm, Lumbricus rubellus. The antimicrobial peptide was purified to homogeneity by a heparin-affinity column and C18 reverse-phase HPLC, and named lumbricin I. Lumbricin I was a proline-rich antimicrobial peptide of 62 amino acids (15% proline in molar ratio; molecular mass, 7231 Da), whose complete sequence was determined by a combination of peptide sequence and cDNA analysis. The peptide and cDNA sequence analysis revealed that lumbricin I was produced as a precursor form consisting of 76 amino acids, with 14 residues in a presegment and 62 residues in mature lumbricin I. Lumbricin I showed antimicrobial activity in vitro against a broad spectrum of microorganisms without hemolytic activity. In addition, a 29-amino acid peptide, named lumbricin I(6-34), which was derived from residues 6-34 of lumbricin I, showed marginally stronger antimicrobial activity than lumbricin I. Northern blot analysis on total RNA revealed that expression of lumbricin I gene was not induced by bacterial infection, but was constitutively expressed. Furthermore, the expression of lumbricin I gene was specific in adult L. rubellus: Lumbricin I mRNA was detected only in adult L, rubellus, but not in eggs and young L. rubellus. (C) 1998 Elsevier Science B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1998-10
Language
English
Article Type
Article
Keywords

EISENIA-FETIDA-ANDREI; ANTIBACTERIAL PEPTIDES; CELOMIC FLUID; PIG INTESTINE; ANTIBIOTICS; SEQUENCE; PROTEINS; SYSTEM; PR-39; BACTENECINS

Citation

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v.1408, no.1, pp.67 - 76

ISSN
0925-4439
URI
http://hdl.handle.net/10203/77703
Appears in Collection
BS-Journal Papers(저널논문)
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