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Journal of Virology, June 2006, p. 6171-6176, Vol. 80, No. 12
0022-538X/06/$08.00+0 doi:10.1128/JVI.02417-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Carol L. Nilsson,2
Joan T. Hare,3
Mark R. Emmett,1,2
Andrei Korostelev,3,
Heather Ongley,1
Alan G. Marshall,1,2 and
Michael S. Chapman1,3*
Department of Chemistry & Biochemistry, Florida State University, Tallahassee, Florida 32306-4390,1 National High Magnetic Field Laboratory, Florida State University, 1800 E. Paul Dirac Dr., Tallahassee, Florida 32310-4005,2 Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-43803
Received 16 November 2005/ Accepted 3 March 2006
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.
Supplemental material for this article may be found at http://jvi.asm.org/.
Present address: Medical Scientist Training Program, Albert Einstein College of Medicine, 1300 Morris Park Ave., Belfer 201, Bronx, NY 10461.
Present address: Molecular, Cell & Developmental Biology, 225 Sinsheimer, University of California, Santa Cruz, CA 95064.
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