Abstract:
:The three-member Egf gene family from the polydnavirus Microplitis demolitor bracovirus (MdBV) encodes novel proteins distinguished by a shared cysteine-rich motif. Prior studies determined that one family member, Egf1.0, inhibits melanization of hemolymph from the moth Manduca sexta by disabling phenoloxidase activating proteinases (PAPs). Here we characterized a second family member, Egf1.5, which shares an identical cysteine-rich motif with Egf1.0, but possesses an extended C-terminal repeat domain. Similar to Egf1.0, Egf1.5 inhibited processing and the amidolytic activity of PAP1 and PAP3 from M. sexta. Egf1.5 also bound PAP1, PAP3 and serine proteinase homolog 2 (SPH2). Comparative studies indicated that Egf1.5 and Egf1.0 similarly inhibited melanization of plasma from two lepidopterans (Pseudoplusia includens and Helicoverpa zea) that are permissive hosts for M. demolitor and MdBV, and two lepidopterans (M. sexta and Bombyx mori) that are nonpermissive hosts. Expression studies showed that transcript abundance of egf1.5 and egf1.0 was also similar in MdBV-infected P. includens and H. zea. Taken together, our results indicate that Egf1.5 and Egf1.0 are functionally similar paralogs.
journal_name
Insect Biochem Mol Bioljournal_title
Insect biochemistry and molecular biologyauthors
Lu Z,Beck MH,Strand MRdoi
10.1016/j.ibmb.2010.04.009subject
Has Abstractpub_date
2010-07-01 00:00:00pages
497-505issue
7eissn
0965-1748issn
1879-0240pii
S0965-1748(10)00091-3journal_volume
40pub_type
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