Interfacial Enzymology of Parvovirus Phospholipases A2

Stéphane Canaan, Zoltán Zádori, Farideh Ghomashchi, James Bollinger, Martin Sadilek, Marie Eve Moreau, Peter Tijssen, Michael H. Gelb

Research output: Contribution to journalArticle

85 Citations (Scopus)


The capsid of parvoviruses proteins were recently shown to contain secreted phospholipase A2 (sPLA2)-like activity that is required during host cell entry. Parvoviral PLA2 domains have little sequence identity with sPLA2s and lack disulfide bonds. In the present study, after bacterial expression and purification, the biochemical characterizations of these first PLA2s identified in viruses have been investigated, and a comparison has been made with other known PLA 2s. The specific activities of three viral PLA2s differed by 3 orders of magnitude, with porcine parvovirus PLA2 displaying a specific activity similar to that of the most active sPLA2s (e.g. human group IIA) and the human AAV2 and B19 parvoviral enzymes displaying approximately 103 lower specific activities (similar to human sPLA2 groups IIE and XIIA). These differences were not caused by weaker Ca2+ or interfacial binding. The specific activities of the viral PLA2s on zwitterionic or anionic phospholipid vesicles were comparable. The viral PLA2s did not display a preference for unsaturated versus saturated sn-2 fatty acyl chains and hydrolyzed all major classes of glycerophospholipids except phosphatidylinositol. Incubation of mammalian cells with porcine parvovirus PLA2 led to the release of arachidonic acid into the culture medium. Interestingly, among nine previously known sPLA2 inhibitors, only a subset showed inhibition of the viral PLA2s and with weak potency, indicating that the active sites of these new enzymes are structurally distinct from those of sPLA2s. Based on these distinct enzymatic and structural properties, we propose to classify the parvovirus PLA2s within the PLA2 superfamily as group XIII enzymes.

Original languageEnglish
Pages (from-to)14502-14508
Number of pages7
JournalJournal of Biological Chemistry
Issue number15
Publication statusPublished - Apr 9 2004


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Canaan, S., Zádori, Z., Ghomashchi, F., Bollinger, J., Sadilek, M., Moreau, M. E., Tijssen, P., & Gelb, M. H. (2004). Interfacial Enzymology of Parvovirus Phospholipases A2. Journal of Biological Chemistry, 279(15), 14502-14508.