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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 LU ; Hare, Joan T ; Emmett, Mark R ; Korostelev, Andrei ; Ongley, Heather ; Marshall, Alan G and Chapman, Michael S (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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author
; ; ; ; ; ; and
publishing date
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}},
}