期刊
JOURNAL OF VIROLOGY
卷 80, 期 12, 页码 6171-6176出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02417-05
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资金
- NIGMS NIH HHS [R01 GM66875, R01 GM066875] Funding Source: Medline
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.
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