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Centre de recherche de microbiologie et biotechnologie, INRS-Institut Armand-Frappier, Université du Québec, 531 boul. des Prairies, Laval, QC, CanadaH7V 1B71
Department of Bioscience, Faculty of Agriculture, Hokkaido University, Sapporo, Japan2
Center of Virology-IRD, Faculty of Agriculture, University of Cairo, Giza, Cairo, Egypt3
Author for correspondence: Peter Tijssen. Fax +1 450 686 5626. e-mail peter.tijssen{at}inrs-iaf.uquebec.ca
Bombyx mori densovirus (BmDNV-1), on the basis of the previously reported genome sequence, constitutes by itself a separate genus (Iteravirus) within the Densovirinae subfamily of parvoviruses. Inconsistencies in the genome organization, however, necessitated its reassessment. The genome sequence of new clones was determined and resulted in a completely different genome organization. The corrected sequence also contained conserved sequence motifs found in other parvoviruses. Some amino acids in the highly conserved domain in the unique region of VP1 were shared by critical amino acids in the catalytic site and Ca2+-binding loop of secreted phospholipase A2, such as from snake and bee venoms. Expression of this domain and determination of enzyme activity demonstrated that capsids have a phospholipase A2 activity thus far unknown to occur in viruses. This viral phospholipase A2, which is required shortly after entry into the cell, showed a substrate preference for phosphatidylethanolamine and phosphatidylcholine over phosphatidylinositol.
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