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Molecular cloning, characterization and tissue expression of prophenoloxidase cDNA from the mosquito Armigeres subalbatus inoculated with Dirofilaria immitis microfilariae
Author(s) -
Cho W. L.,
Liu H. S.,
Lee C. H.,
Kuo C. C.,
Chang T. Y.,
Liu C. T.,
Chen C. C.
Publication year - 1998
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.1998.71049.x
Subject(s) - prophenoloxidase , dirofilaria immitis , biology , complementary dna , cloning (programming) , hemocyte , inoculation , gene , zoology , genetics , immunology , helminths , innate immune system , immune system , computer science , programming language
A cDNA encoding mosquito Armigeres subalbatus pro‐phenol oxidase (As‐pro‐PO) was obtained by rapid amplification of cDNA ends‐polymerase chain reaction (RACE‐PCR) after Dirofilaria immitis inoculation. The 2205 bp As‐pro‐PO cDNA contains a 32 bp 5′‐noncoding region, a 2055 bp open reading frame (685 amino acids), and a 118 bp 3′‐noncoding region. Hydrophobic signal peptide for the endoplasmic reticulum targeting is not found in the NH 2 ‐terminal region. Two potential copper‐binding domains, amino acids 197–245 and 345–412, are highly homologous to those of the other insect pro‐POs. A 2.2 kb As‐pro‐PO transcript was identified by Northern blot analysis using D. immitis microfilariae‐inoculated A. subalbatus . Both in situ hybridization and Northern blot analysis demonstrated that As‐pro‐PO mRNA was synthesized in mosquito haemocytes but not in other tissues, i.e. fat bodies, midguts and ovaries, etc.