Stylicins, a new family of antimicrobial peptides from the Pacific blue shrimp Litopenaeus stylirostris
Rolland, J.L.; Abdelouahab, M.; Dupont, J.; Lefevre, F.; Bachere, E.; Romestand, B. (2010). Stylicins, a new family of antimicrobial peptides from the Pacific blue shrimp Litopenaeus stylirostris. Molecular Immunology 47(6): 1269-1277. https://dx.doi.org/10.1016/j.molimm.2009.12.007
In: Molecular Immunology. PERGAMON-ELSEVIER SCIENCE LTD: Oxford. ISSN 0161-5890, more
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| Keywords |
Litopenaeus stylirostris (Stimpson, 1871) [WoRMS]; Vibrio Pacini, 1854 [WoRMS]
Marine/Coastal |
| Author keywords |
Ls-Stylicin 1; Peptide; Shrimp; Antifungal; Agglutination; Vibrio |
| Authors | | Top |
- Rolland, J.L.
- Abdelouahab, M.
- Dupont, J.
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- Lefevre, F.
- Bachere, E.
- Romestand, B.
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| 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 (−) 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 × 10−8 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. |
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