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

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.

SUBMITTER: Murray S

PROVIDER: S-EPMC1472596 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature

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

Murray Sarah S Nilsson Carol L CL Hare Joan T JT Emmett Mark R MR Korostelev Andrei A Ongley Heather H Marshall Alan G AG Chapman Michael S MS

Journal of virology 20060601 12

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 anal ...[more]

PMID: 16731956

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