Glycobiology Advance Access originally published online on June 23, 2004
Glycobiology 2004 14(11):969-977; doi:10.1093/glycob/cwh118
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Glycobiology vol. 14 no. 11 © Oxford University Press 2004; all rights reserved.
Analysis of the interaction between adeno-associated virus and heparan sulfate using atomic force microscopy
2 Curriculum in Applied and Materials Sciences, Program in Cellular and Molecular Biophysics, CB# 3287, University of North Carolina, Chapel Hill, NC 27599; 3 Division of Medicinal Chemistry and Natural Products, School of Pharmacy, CB# 7630, University of North Carolina, Chapel Hill, NC 27599; 4 Gene Therapy Center, CB# 7352, University of North Carolina, Chapel Hill, NC 27599; and 5 Department of Physics and Astronomy, CB# 3255, University of North Carolina, Chapel Hill, NC 27599
Received on March 23, 2004; revised on June 11, 2004; accepted on June 17, 2004
Adeno-associated virus (AAV) has been widely used as a viral vector to deliver genes to animal and human tissues in gene therapy studies. Both AAV-2 and AAV-3 use cell surface heparan sulfate (HS), a highly sulfated polysaccharide, as a receptor to establish infections. In this study, we used atomic force microscopy (AFM) to investigate the interaction of HS and AAV. A silicon chip functionalized with HS was used as a substrate for binding AAV for AFM analysis. To validate our approach, we found that the binding of AAV-2 to the HS surface was effectively competed by soluble HS, suggesting that the binding of AAV-2 to the functionalized surface was specific. In addition, we examined the binding of various AAV serotypes, including AAV-1, AAV-2, AAV-3, and AAV-5, to the HS surface. As expected, only AAV-2 and AAV-3 bound, whereas AAV-1 and AAV-5 did not. This observation was consistent with the previous conclusion that AAV-1 and AAV-5 do not use HS as a receptor for infection. In conclusion, we developed a novel approach to investigate the interaction of AAV virus with its polysaccharide-based receptor at the level of a single viral particle. Given that HSs serve as receptor for numerous viruses, this approach has the potential to become a generalized method for studying interactions between the viral particle and HS, as well as other virus–cell interactions, and potentially serve as a platform for screening antiviral therapies.
1 To whom correspondence should be addressed; e-mail: rsuper{at}physics.unc.edu and jian_liu{at}unc.edu
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