ArticleMolecular therapy. Methods & clinical development2025
Characterization of difficult-to-remove host cell proteins in adeno-associated virus downstream processing.
Article in Molecular therapy. Methods & clinical development, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Integrated Continuous Biomanufacturing of Recombinant Adeno-Associated Virus.bioRxiv : the preprint server for biology · 2026Article
- Impact of downstream purification process and AAV serotype on protein-impurity clearance.Molecular therapy. Advances · 2026Article
- AAV2 Crosslinks Actin Filaments: Implications for AAV Gene Therapy Vector Design.bioRxiv : the preprint server for biology · 2026Article
- CRISPR-Cas9 and next-generation gene editing strategies for therapeutic intervention of neurodegenerative pathways in Alzheimer's disease: a state-of-the-art review.Acta neurologica Belgica · 2026Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A scalable, serotype-agnostic, and fully chromatographic downstream platform was developed for the purification of adeno-associated virus (AAV) based on affinity chromatography (AC), anion-exchange chromatography (AEX), and multi-modal polishing chromatography (MMC). Quantitative proteomic profiling across each purification stage was performed using sequential window acquisition of all theoretical fragment ion mass spectra (SWATH-MS) to characterize residual host cell protein (HCP) retention for four AAV serotypes (AAV2, -5, -8, and -9) produced with suspension HEK293 cells. The downstream process showed cumulative vector genome (VG) yields ranging from 44.6 to 69.2% with full capsid enrichments ranging from 2.62- to 5.93-fold across all AAV samples. A total of 880, 99, and 21 HCPs were identified in all AAV samples after AC, AEX, and MMC, respectively. Vector-mediated mechanisms of retention are proposed (i.e., capsid or genome association) based on enrichment in protein- and nucleic acid-binding properties of difficult-to-remove HCPs, little clearance across multiple modes of separation, and divergence of HCP profiles for AAV-containing samples vs. null lysate material. The characterization of HCP retention described here advances the understanding of process-related impurity clearance in scalable AAV downstream systems, with implications for both purification process design and AAV interactions with host cell factors.
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