New member of the protein disulfide isomerase (PDI) family identified in Amblyomma variegatum tick
Knizetova, Petra × Vancova, Iveta Kocakova, Paulina Slovak, Mirko Proost, Paul Kopacek, Juraj #
Insect Biochemistry and Molecular Biology vol:36 issue:12 pages:943-953
Ticks belonging to arthropoda are blood feeding, geographically widespread ectoparasites of mammals, reptiles and birds. Their saliva contains active substances that protect them from host immune attack and allow for transmission of various pathogens during the feeding process. Characterization of tick saliva components can therefore contribute to the development of effective methods for the control of tick-borne diseases. Here we describe the identification and basic characterization of a gene encoding a 55kDa protein found in the salivary glands (SG) of Amblyomma variegatum tick. Based on the primary structure and homology to the family of protein disulfide isomerases (PDI; EC 220.127.116.11) the gene was named AvPDI. The 1461nt long AvPDI open reading frame codes for a 487 amino acid protein. In vitro expressed AvPDI was exclusively localized in the endoplasmic reticulum. RT-PCR and Western blot analysis revealed that AvPDI expression is not restricted to the SG of the tick. More detailed analysis on tissue slides from SG detected an AvPDI specific signal in granular cells of the acini type II and III. Finally, reductase activity of AvPDI was confirmed in an insulin assay. The structural and functional characteristics suggest that AvPDI is another member of the PDI protein family and represents the first more closely characterized PDI in the ticks.