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Site-Specific N-Glycosylation on the AAV8 Capsid Protein

Publication Type : Journal Article

Publisher : Viruses 10(11):644, 2018

Source : Viruses, , Volume 10, Issue 11, p.644, DOI:10.3390/v10110644 (2018)

Campus : Amritapuri

School : School of Biotechnology

Department : biotechnology

Year : 2018

Abstract : Adeno associated virus (AAV) is a versatile gene delivery tool, which has been approved as a human gene therapy vector for combating genetic diseases. AAV capsid proteins are the major components that determine the tissue specificity, immunogenicity and in vivo transduction performance of the vector. In this study, the AAV8 capsid glycosylation profile was systemically analyzed by peptide mass fingerprinting utilizing high-resolution mass spectrometry to determine the presence of capsid glycosylation. We identified N-glycosylation on the amino acid N499 of the capsid protein. We characterized the overall sugar profile for vector produced in 293 cells. Multiple N-glycosylated host-cell proteins (HCPs) copurified with AAV8 vectors and were identified by analyzing LC-MS data utilizing a human database and proteome discoverer search engine. The N-glycosylation analysis by MALDI-TOF MS, highlighted the probability of AAV8 interaction with terminal galactosylated N-glycans within the HCPs.

Cite this Research Publication : Dr. Arya Aloor, Zhang, J., Parameswaran, A., Gashash, E., Ma, C., Wang, P., Chrzanowski, M., Diao, Y., and Xiao, W., “Site-Specific N-Glycosylation on the AAV8 Capsid Protein”, Viruses, , vol. 10, no. 11, p. 644, DOI:10.3390/v10110644, 2018.

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