Structural and functional differences of Litopenaeus vannamei crustins |
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Authors: | Vargas-Albores Francisco Yepiz-Plascencia Gloria Jiménez-Vega Florinda Avila-Villa Angélica |
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Affiliation: | a Marine Biotechnology, CIAD, PO Box 1735, Hermosillo, Sonora 83000, Mexico;b Aquatic Molecular Biology, CIAD, PO Box 1735, Hermosillo, Sonora 83000, Mexico;c CIBNOR, P.O. Box 128, La Paz, Baja California Sur 23000, Mexico |
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Abstract: | Penaeid crustins were described in Litopenaeus vannamei and L. setiferus as proteins belonging to an antibacterial peptide family with similar sequences but different sizes. Six crustin-coding clones were isolated from a cDNA library from L. vannamei hemocytes, sequenced and compared. Two different isoforms (named I and P) were found, based on two nucleotide differences that produce one change in amino acid sequence (Ile/Pro). Other single differences in nucleotide sequences were also noted, but they did not change the translated product. The mRNA steady state levels of crustin I, but not of crustin P, were down regulated by Vibrio alginolyticus inoculation. Thus, the differences among penaeid crustins seem to be associated with one amino acid substitution, which affects their expression after bacterial inoculation. By structural similarity, shrimp crustins seem to belong to an antibacterial WAP-domain containing protein family. |
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Keywords: | Antibacterial peptide WAP domain Vibrio alginolyticus Shrimp Crustaceans |
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