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Adeno-associated Virus
CDMS mass histogram of the ATCC AAV2 Reference material. The peak at 3.752 MDa is in good agreement with the expected mass of a 1:1:10 VP1:VP2:VP3 AAV2 capsid. The full peak has a mass of 5.197 MDa. Mass measurements by CDMS allow for a direct calculation of the packaged genome mass.
CDMS mass histogram of the ATCC AAV8 Reference material. The prominent peak at 5.237 corresponds to the peak containing the genome of interest. In the AAV8 reference standard two populations of partially filled capsid are detected at 4.423 and 5.038 MDa.
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Recent Publications
Analysis of thermally driven structural changes, genome release, disassembly, and aggregation of recombinant AAV by CDMS, Mol. Ther. Meth & Clin. Dev. 2021
Comparison of analytical techniques to quantitate the capsid content of adeno-associated viral vectors, Mol. Ther. Meth & Clin. Dev. 2021
Quantitative analysis of genome packaging in recombinant AAV vectors by charge detection mass spectrometry, Mol. Ther. Meth & Clin. Dev. 2021
Lot-to-Lot Variation in Adeno-Associated Virus Serotype 9 (AAV9) Preparations; Human Gene Therapy Meth. 2019
Resolving Adeno-Associated Viral Particle Diversity With Charge Detection Mass Spectrometry; Anal. Chem. 2016
Vaccines & VLPs
CDMS mass spectrum of ATCC Human Ad5 virus shows resolved full, partial, empty and incomplete particles of adenovirus. Adenovirus is comprised of over 2000 individual building blocks and the mass information from CDMS can not only differentiate particles, but give stoichiometry. CDMS has also been used to track the amount of packaging protein in different recombinant adenovirus lots. Check our the publication below.
CDMS mass histogram of the Inactivated Polio Vaccine (iPOL). CDMS can quantify the relative abundances of the desired capsid at ~8MDa as well as the peak ~6 MDa that is not responsible for an immune response. iPol is one vaccine example, but CDMS can measure all classical and next generation approaches providing information on lot-to-lot variability
Assembly of cp149 HBV capsid. The assembly and aggregation of protein complexes is difficult to characterize by most analytical techniques, but early stage resolving power of CDMS allows us to resolve the addition of individual subunits from early nucleation to the intact capsid
Recent Publications
Analysis of Recombinant Adenovirus Vectors by Ion Trap Charge Detection Mass Spectrometry: Accurate Molecular Weight Measurements beyond 150 MDa, Anal. Chem. 2022
Characterization of Classical Vaccines by Charge Detection Mass Spectrometry, Anal. Chem. 2021
Higher Resolution Charge Detection Mass Spectrometry, Anal. Chem. 2020
Multiple Pathways in Capsid Assembly, JACS 2018
Hepatitis B Virus Capsid Completion Occurs through Error Correction, JACS 2017
