PMID- 37774344
OWN - NLM
STAT- MEDLINE
DCOM- 20240321
LR  - 20240322
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 34
IP  - 1
DP  - 2024 Mar 19
TI  - N-glycomic profiling of capsid proteins from Adeno-Associated Virus serotypes.
LID - 10.1093/glycob/cwad074 [doi]
LID - cwad074
AB  - Adeno-associated virus (AAV) vector has become the leading platform for gene 
      delivery. Each serotype exhibits a different tissue tropism, immunogenicity, and 
      in vivo transduction performance. Therefore, selecting the most suitable AAV 
      serotype is critical for efficient gene delivery to target cells or tissues. 
      Genome divergence among different serotypes is due mainly to the hypervariable 
      regions of the AAV capsid proteins. However, the heterogeneity of capsid 
      glycosylation is largely unexplored. In the present study, the N-glycosylation 
      profiles of capsid proteins of AAV serotypes 1 to 9 have been systemically 
      characterized and compared using a previously developed high-throughput and 
      high-sensitivity N-glycan profiling platform. The results showed that all 9 
      investigated AAV serotypes were glycosylated, with comparable profiles. The most 
      conspicuous feature was the high abundance mannosylated N-glycans, including FM3, 
      M5, M6, M7, M8, and M9, that dominated the chromatograms within a range of 74 to 
      83%. Another feature was the relatively lower abundance of fucosylated and 
      sialylated N-glycan structures, in the range of 23%-40% and 10%-17%, 
      respectively. However, the exact N-glycan composition differed. These differences 
      may be utilized to identify potential structural relationships between the 9 AAV 
      serotypes. The current research lays the foundation for gaining better 
      understanding of the importance of N-glycans on the AAV capsid surface that may 
      play a significant role in tissue tropism, interaction with cell surface 
      receptors, cellular uptake, and intracellular processing.
CI  - (c) The Author(s) 2023. Published by Oxford University Press.
FAU - Xie, Yongjing
AU  - Xie Y
AD  - National Institute for Bioprocessing Research and Training, Foster Avenue, Mount 
      Merrion, Blackrock, Co. Dublin, A94 X099, Ireland.
FAU - Butler, Michael
AU  - Butler M
AD  - National Institute for Bioprocessing Research and Training, Foster Avenue, Mount 
      Merrion, Blackrock, Co. Dublin, A94 X099, Ireland.
AD  - School of Chemical and Bioprocess Engineering, University College Dublin (UCD), 
      Belfield, Dublin 4, D04 V1W8, Ireland.
LA  - eng
GR  - Agilent Technologies/
PT  - Journal Article
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Capsid Proteins)
RN  - 0 (Polysaccharides)
RN  - Adeno-associated virus-1
SB  - IM
MH  - *Capsid Proteins/chemistry
MH  - *Dependovirus/genetics/metabolism
MH  - Serogroup
MH  - Glycomics
MH  - Genetic Vectors
MH  - Polysaccharides/metabolism
PMC - PMC10950483
OTO - NOTNLM
OT  - InstantPC
OT  - adeno-associated virus
OT  - capsid protein
OT  - gene therapy
OT  - glycosylation
COIS- The authors declare that there is no conflict of interest.
EDAT- 2023/09/29 18:42
MHDA- 2024/03/21 12:42
PMCR- 2023/09/29
CRDT- 2023/09/29 16:13
PHST- 2023/05/01 00:00 [received]
PHST- 2023/09/14 00:00 [revised]
PHST- 2023/09/23 00:00 [accepted]
PHST- 2024/03/21 12:42 [medline]
PHST- 2023/09/29 18:42 [pubmed]
PHST- 2023/09/29 16:13 [entrez]
PHST- 2023/09/29 00:00 [pmc-release]
AID - 7286508 [pii]
AID - cwad074 [pii]
AID - 10.1093/glycob/cwad074 [doi]
PST - ppublish
SO  - Glycobiology. 2024 Mar 19;34(1):cwad074. doi: 10.1093/glycob/cwad074.