Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon
1999 (English)In: Developmental and Comparative Immunology, ISSN 0145-305X, Vol. 23, no 3, 179-186 p.Article in journal (Refereed) Published
A cDNA encoding shrimp, Penaeus monodon, prophenoloxidase (proPO) was obtained by screening a hemocyte library by plaque hybridization using a proPO cDNA fragment from freshwater crayfish, Pacifastacus leniusculus, as a probe. The 3,002 bp cDNA contains an open reading frame of 2,121 bp and a 881 bp 3′-untranslated region. The molecular mass of the deduced amino acid sequence (688 amino acids) is 78,700 Da with an estimated pI of 5.8. Two putative copper binding sites are present and they have a highly conserved sequence around these sites. No signal peptide was detected in the shrimp proPO, as has been previously shown to be the case for all arthropod proPOs cloned so far. The cleavage site of zymogen activation is likely to be between Arg 44 and Val 45. A tentative complement-like motif (GCGWPQHM) is also present. Shrimp proPO mRNA is synthesized in the hemocytes and not in the hepatopancreas. Comparison of amino acid sequences showed that shrimp proPO is more closely related to another crustacean proPO, namely crayfish, than to the insect proPOs.
Place, publisher, year, edition, pages
1999. Vol. 23, no 3, 179-186 p.
prophenoloxidase, Penaeus monodon, hemocyanin, arthropod immunity, CRAYFISH PACIFASTACUS-LENIUSCULUS, PRO-PHENOL OXIDASE, BETA-1;3-GLUCAN BINDING-PROTEIN, AMINO-ACID-SEQUENCE, ACTIVATING SYSTEM, BLOOD-CELLS, CALIFORNIENSIS HOLMES, INVERTEBRATE IMMUNITY
IdentifiersURN: urn:nbn:se:uu:diva-78548DOI: 10.1016/S0145-305X(99)00005-1OAI: oai:DiVA.org:uu-78548DiVA: diva2:106461