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- Title
PURIFICATION AND MOLECULAR CLONING OF HEMOCYANIN FROM FENNEROPENAEUS MERGUIENSIS (DE MAN, 1888): RESPONSE TO VIBRIO HARVEYI EXPOSURE.
- Authors
Acharee Jiewkok; Tsukimura, Brian; Prapapom Utarabhand
- Abstract
Hemocyanin (HC) was purified from hemolymph of Fenneropenaeus merguiensis (de Man, 1888). Purified HC showed one band in non-denaturing PAGE with a molecular mass of 457 kDa, determined by gel filtration. Using an ELISA, HC content was 85.6% of total hemolymph protein. HC's hexamer form contained no phenoloxidase activity under trypsin or SDS activation. FmHC, cloned from F. merguiensis, had a full-length cDNA comprised of 2128 bp with an open reading frame encoding a peptide of 661 amino acids with two Cu-binding sites. Expression of FmHC was found only in the hepatopancreas where it was up-regulated after exposure to Vibrio harveyi injection into shrimp and with tissue incubations. HC protein levels in the hemolymph of bacterial injected shrimp also increased. FmHC expression was also up-regulated after shrimp were challenged with a lipopolysaccharide, which is a surface component of gram-negative bacteria. These results indicate that HC is inducible and up-regulated in response to pathogenic challenge, confirming that HC participates in the innate immune response in F. merguiensis.
- Subjects
MOLECULAR cloning; PENAEUS; HEMOCYANIN; HEMOLYMPH; BINDING sites
- Publication
Journal of Crustacean Biology, 2015, Vol 35, Issue 5, p659
- ISSN
0278-0372
- Publication type
Article
- DOI
10.1163/1937240X-00002356