Characterization of the capsid protein glycosylation of adeno-associated virus type 2 by high-resolution mass spectrometry.
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.
Murray
Sarah
S
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA.
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
D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism; D002241:Carbohydrates / Q000032:analysis; D000229:Dependovirus / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006367:HeLa Cells; D006801:Humans; D013058:Mass Spectrometry; D010449:Peptide Mapping
D036022:Capsid Proteins; D002241:Carbohydrates