Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus.
Pathogenic challenges in decapod crustaceans are combated by innate immune responses, including the production and secretion of soluble antibacterial proteins into the hemolymph. Among the antibacterials that have been identified in decapod species are the crustins, a group of four-disulfide core/whey-acidic-protein (WAP) domain-containing proteins, which target marine/salt tolerant Gram-positive bacteria. To begin to assess the possible role of crustins in combating bacterial invasion in the American lobster Homarus americanus, we identified and sequenced a 744 base pair cDNA that encodes a novel 96 amino acid crustin-like protein. Comparison of H. americanus crustin (Hoa-crustin) with crustins from other decapod species showed that it is most similar to an isoform predicted from the European lobster Homarus gammarus ( approximately 86% identity). With our identification of the Hoa-crustin cDNA, we are positioned to begin molecular and physiological investigations of the regulation and function of this putative antibacterial protein in H. americanus.
Christie
Andrew E
AE
Department of Biology, University of Washington, Box 351800, Seattle, WA 98195-1800, USA. pdickins@bowdoin.edu
Rus
Szymon
S
Goiney
Christopher C
CC
Smith
Christine M
CM
Towle
David W
DW
Dickinson
Patsy S
PS
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics*; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry*; D007113:Immunity, Innate / Q000235:genetics; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000737:chemistry* / Q000235:genetics* / Q000276:immunology; D017434:Protein Structure, Tertiary / Q000235:genetics
D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary