Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry
(2006) In Journal of Virology 80(12). p.6-6171- 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.
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https://lup.lub.lu.se/record/5cd7bb97-3895-4c8e-884e-76bce938b2d0
- author
- Murray, Sarah S ; Nilsson, Carol L LU ; Hare, Joan T ; Emmett, Mark R ; Korostelev, Andrei ; Ongley, Heather ; Marshall, Alan G and Chapman, Michael S
- publishing date
- 2006-06
- type
- Contribution to journal
- publication status
- published
- keywords
- Capsid Proteins, Carbohydrates, Dependovirus, Glycosylation, HeLa Cells, Humans, Mass Spectrometry, Peptide Mapping, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
- in
- Journal of Virology
- volume
- 80
- issue
- 12
- pages
- 6 pages
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:33744937902
- pmid:16731956
- ISSN
- 0022-538X
- DOI
- 10.1128/JVI.02417-05
- language
- English
- LU publication?
- no
- id
- 5cd7bb97-3895-4c8e-884e-76bce938b2d0
- date added to LUP
- 2017-05-16 10:35:07
- date last changed
- 2024-04-14 11:30:55
@article{5cd7bb97-3895-4c8e-884e-76bce938b2d0, abstract = {{<p>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.</p>}}, author = {{Murray, Sarah S and Nilsson, Carol L and Hare, Joan T and Emmett, Mark R and Korostelev, Andrei and Ongley, Heather and Marshall, Alan G and Chapman, Michael S}}, issn = {{0022-538X}}, keywords = {{Capsid Proteins; Carbohydrates; Dependovirus; Glycosylation; HeLa Cells; Humans; Mass Spectrometry; Peptide Mapping; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.}}, language = {{eng}}, number = {{12}}, pages = {{6--6171}}, publisher = {{American Society for Microbiology}}, series = {{Journal of Virology}}, title = {{Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry}}, url = {{http://dx.doi.org/10.1128/JVI.02417-05}}, doi = {{10.1128/JVI.02417-05}}, volume = {{80}}, year = {{2006}}, }