Intrinsic phospholipase A2 activity of adeno-associated virus is involved in endosomal escape of incoming particles

Virology. 2011 Jan 5;409(1):77-83. doi: 10.1016/j.virol.2010.09.025. Epub 2010 Oct 25.

Abstract

The unique region of the VP1 capsid protein of adeno-associated viruses (AAV) in common with autonomously replicating parvoviruses comprises a secreted phospholipase A2 (sPLA2) homology domain. While the sPLA2 domain of Minute Virus of Mice has recently been shown to mediate endosomal escape by lipolytic pore formation, experimental evidence for a similar function in AAV infection is still lacking. Here, we explored the function of the sPLA2 domain of AAV by making use of the serotype 2 mutant (76)HD/AN. The sPLA2 defect in (76)HD/AN, which severely impairs AAV's infectivity, could be complemented in trans by co-infection with wild-type AAV2. Furthermore, co-infection with endosomolytically active, but not with inactive adenoviral variants partially rescued (76)HD/AN, providing the first evidence for a function of this domain in endosomal escape of incoming AAV particles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Dependovirus / classification
  • Dependovirus / enzymology*
  • Dependovirus / genetics
  • Dependovirus / pathogenicity*
  • Endosomes / physiology
  • Endosomes / virology*
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Mutation
  • Phospholipases A2 / chemistry
  • Phospholipases A2 / genetics
  • Phospholipases A2 / metabolism*
  • Serotyping
  • Virion / metabolism*

Substances

  • Capsid Proteins
  • Phospholipases A2