Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry

Sarah Murray, Carol L. Nilsson, Joan T. Hare, Mark Emmett, Andrei Korostelev, Heather Ongley, Alan G. Marshall, Michael S. Chapman

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Adeno-associated virus type 2 (AAV-2) capsid proteins have eight sequence motifs that are potential sites for O- or N-linked glycosylation. Three are in prominent surface locations, close to the sites of cellular receptor attachment and to neutralizing epitopes on or near protrusions surrounding the three-fold axes, raising the possibility that AAV-2 might use glycosylation as a means of immune escape or for preventing reattachment on release of progeny virus. Peptide mapping and structural analysis by Fourier transform ion cyclotron resonance mass spectrometry demonstrates, however, no glycosylation of the capsid protein for virus prepared in cultured HeLa cells.

Original languageEnglish (US)
Pages (from-to)6171-6176
Number of pages6
JournalJournal of Virology
Volume80
Issue number12
DOIs
StatePublished - Jun 2006
Externally publishedYes

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ASJC Scopus subject areas

  • Immunology

Cite this

Murray, S., Nilsson, C. L., Hare, J. T., Emmett, M., Korostelev, A., Ongley, H., Marshall, A. G., & Chapman, M. S. (2006). Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry. Journal of Virology, 80(12), 6171-6176. https://doi.org/10.1128/JVI.02417-05