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J Virol. 2006 Jun;80(12):6171-6.

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

Author information

1
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA.

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.

PMID:
16731956
PMCID:
PMC1472596
DOI:
10.1128/JVI.02417-05
[Indexed for MEDLINE]
Free PMC Article

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