A Viral Phospholipase A2 Is Required for Parvovirus Infectivity
Open accessAbstract
Sequence analysis revealed phospholipase A2 (PLA2) motifs in capsid proteins of parvoviruses. Although PLA2 activity is not known to exist in viruses, putative PLA2s from divergent parvoviruses, human B19, porcine parvovirus, and insect GmDNV (densovirus from Galleria mellonella), can emulate catalytic properties of secreted PLA2. Mutations of critical amino acids strongly reduce both PLA2 activity and, proportionally, viral infectivity, but cell surface attachment, entry, and endocytosis by PLA2-deficient virions are not affected. PLA2 activity is critical for efficient transfer of the viral genome from late endosomes/lysosomes to the nucleus to initiate replication. These findings offer the prospect of developing PLA2 inhibitors as a new class of antiviral drugs against parvovirus infections and associated diseases.
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A phospholipase domain essential for viral infectivity has been identified in the unique N terminus of Vp1.
“A phospholipase domain, essential for viral infectivity, has been identified in the unique N terminus of Vp1 (19, 53).”
From Packaging Capacity of Adeno-Associated Virus Serotypes: Impact of Larger Genomes on Infectivity and Postentry Steps (2005) · cites this paper as [53]
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- Authors
- Zádori, Z., Szelei, J., Lacoste, M.-C., Li, Y., Gariépy, S., Raymond, P., Allaire, M., Nabi, I. R., & Tijssen, P.
- Affiliations
- Institut National de la Recherche Scientifique (CA)
- Université de Montréal (CA)
- Corresponding author
- Tijssen, Peter
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2001-08
- Volume
- 1
- Issue
- 2
- Pages
- 291-302
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W2001738143
- Cited by
- 518
- References
- 59
- Citations by year
- 2026: 11 · 2025: 21 · 2024: 30 · 2023: 20 · 2022: 20 · 2021: 33 · 2020: 23 · 2019: 22 · 2018: 20 · 2017: 15 · 2016: 19 · 2015: 18 · 2014: 22 · 2013: 30 · 2012: 21
- FWCI
- 12.09
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Developmental Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Natural Sciences and Engineering Research Council of Canada
- Hungarian Scientific Research Fund
- Canadian Institutes of Health Research
- Magyar Tudományos Akadémia
- Topics
- Health Sciences › Medicine › Infectious Diseases › Parvovirus B19 Infection Studies
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- parvovirus, phospholipase A2, capsid protein, viral infectivity, parvovirus B19, porcine parvovirus, densovirus, antiviral drug targets, PLA2 inhibitors
- MeSH terms
- Amino Acid Sequence, Calcium, Capsid, Cell Nucleus, Chromatography, Thin Layer, DNA, Genetic Vectors, Lysosomes, Microscopy, Fluorescence, Models, Biological, Models, Molecular, Molecular Sequence Data, Mutation, Phospholipases A, Endosomes, Thioredoxins, Transfection, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, In Situ Hybridization, Protein Structure, Tertiary, Parvovirus, Amino Acid Motifs, Phospholipases A2
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