期刊
VIRUSES-BASEL
卷 10, 期 11, 页码 -出版社
MDPI
DOI: 10.3390/v10110644
关键词
Adeno associated virus; mass spectrometry; site specific N-glycan analysis; host cell protein analysis; virus-host interaction
类别
资金
- Key Grant Project of Chinese Ministry of Education [313033]
- National Natural Science Foundation of China [81371672, 81371669]
- Major project of University and Industry Cooperation in Fujian Province of China [2018Y4009]
- Project of Science and Technology of Quanzhou [2016N006]
- NIH [HL114152, HL130871]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL114152, U54HL142019, R01HL130871] Funding Source: NIH RePORTER
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.
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