Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5918219 | Molecular Immunology | 2010 | 9 Pages |
Abstract
The present study reports the characterization of Ls-Stylicin1, a novel antimicrobial peptide from the penaeid shrimp, Litopenaeus stylirostris. The predicted mature peptide of 82 residues is negatively charged (theoretical pI = 5.0) and characterized by a proline-rich N-terminal region and a C-terminal region containing 13 cysteine residues. The recombinant Ls-Stylicin1 has been isolated in both monomeric and dimeric forms. Both display strong antifungal activity against Fusarium oxysporum (1.25 μM < MIC < 2.5 μM), a pathogenic fungus of shrimp, but lower antimicrobial activity against Gram (â) bacteria, Vibrio sp. (40 μM < MIC < 80 μM). However, rLs-Stylicin1 is able to agglutinate Vibrio penaeicidae in vitro in agreement with its potent LPS-binding activity on immobilized LPS of V. penaeicidae (dissociation constant (Kd) of 9.6 Ã 10â8 M). This molecule with no evident homology to other hitherto described antimicrobial peptides but identified herein several species of penaeid shrimp is thought to be the first member of a shrimp antimicrobial peptide family, which we termed stylicins.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
J.L. Rolland, M. Abdelouahab, J. Dupont, F. Lefevre, E. Bachère, B. Romestand,