Evidence map›Paper›PMID 42267823›Full record

ArticleJournal of virology2026

Natural and evolved membrane-associated accessory proteins differentially engage SNARE machinery for AAV egress.

Robert M Fusco, Joshua A Hull, Chenxuan Tong, Xinlong Wan, Zachary C Elmore, Aravind Asokan

Abstract read
In one paragraph

Article in Journal of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Robert M FuscoDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Joshua A HullDepartment of Surgery, Duke University School of Medicine, Durham, North Carolina, USA.
Chenxuan TongDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.
Xinlong WanDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.ORCID 0000-0002-7764-5531
Zachary C ElmoreDepartment of Surgery, Duke University School of Medicine, Durham, North Carolina, USA.
Aravind AsokanDepartment of Biomedical Engineering, Duke University, Durham, North Carolina, USA.ORCID 0000-0001-5563-4877

Funding

Engineering the biology of AAV secretion and productionR01EB034573 · NIBIB · DUKE UNIVERSITY · PI Aravind Asokan · 2023 to 2026
$1.9M
NIBIB NIH HHS R01 EB034573NIBIB NIH HHS R01EB034573
6 · The paper itself

Abstract

Adeno-associated viruses (AAV) are non-enveloped parvoviruses widely utilized for therapeutic gene delivery. The membrane-associated accessory protein (MAAP), a key viral protein, is critical for cellular egress of both infectious and recombinant AAV particles. However, the structure-function correlates of this process have remained largely elusive. Here, we applied structure-guided evolution to enhance AAV egress and dissect the biology of both natural and synthetic MAAP (synMAAP) variants. Three structurally distinct combinatorial libraries focused on disordered domains within MAAP8 (derived from AAV serotype 8) were subjected to selection through both transfection and infectious cycling. Newly enriched synMAAPs obtained as a function of enhanced AAV secretion from host cells revealed a profound bias toward mutations within the C-terminal domain. The most potent synMAAPs showed increased propensity to form extended alpha-helix structures as predicted by structural modeling, amphipathicity, and hydrophobicity scores. Confocal microscopy demonstrated that, unlike natural MAAP8, synMAAPs are excluded from the nucleus and exhibit strong perinuclear accumulation within the Golgi. Proximity ligation analysis, biochemical analysis, and gene deletion studies further corroborated that synMAAPs appear to more efficiently engage SNARE complex proteins, notably involving VAMP3, to potentiate AAV egress. Together, these findings reveal new insights into structure-function correlates of viral egress from host cells and may help improve recombinant vector production for gene therapy applications.IMPORTANCEViruses must exit infected cells to spread, yet this process is poorly understood for adeno-associated virus. In this study, we examine how adeno-associated virus exits mammalian cells without causing cell death. By engineering and evolving new versions of the viral egress factor, we identify cellular trafficking pathways that are exploited during viral release. These findings improve our understanding of how viruses interact with host cells. Additionally, the engineered egress factors described in this study may be used to improve the efficiency of adeno-associated virus production for gene therapy applications.

Indexed as

DependovirusSNARE ProteinsViral ProteinsVirus ReleaseGolgi ApparatusHEK293 CellsHumansReceptors, Cell SurfaceKIAA0319L protein, humanReceptors, Cell SurfaceSNARE ProteinsViral Proteinsadeno-associated virusGolgi transportparvovirussecretory pathwaySNARE machineryviral egress

Identifiers

PMID42267823
PMCPMC13386907

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.