Evidence map›Paper›PMID 30533449›Full record

ArticleMolecular therapy. Methods & clinical development2018

Highly Efficient Ultracentrifugation-free Chromatographic Purification of Recombinant AAV Serotype 9.

Taro Tomono, Yukihiko Hirai, Hironori Okada, Yoshitaka Miyagawa, Kumi Adachi, Shuhei Sakamoto, Yasuhiro Kawano, Hideto Chono, Junichi Mineno, Akiko Ishii and 4 more

Open access · goldAbstract read
In one paragraph

Article in Molecular therapy. Methods & clinical development, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 11% of its field
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

23 citing papers in PubMed, 53 citations in OpenAlex.

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  14. Review
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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

14 authors at 4 institutions in 1 country.

Taro TomonoDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Yukihiko HiraiDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Hironori OkadaDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Yoshitaka MiyagawaDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Kumi AdachiDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Shuhei SakamotoCDM center, Takara Bio Inc., Shiga, Japan.
Yasuhiro KawanoCDM center, Takara Bio Inc., Shiga, Japan.
Hideto ChonoCDM center, Takara Bio Inc., Shiga, Japan.
Junichi MinenoCDM center, Takara Bio Inc., Shiga, Japan.
Akiko IshiiDepartment of Neurology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Takashi ShimadaDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Masafumi OnoderaDepartment of Human Genetics, National Center for Child Health and Development, Tokyo, Japan.
Akira TamaokaDepartment of Neurology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Takashi OkadaDepartment of Biochemistry and Molecular Biology, Nippon Medical School, Tokyo, Japan.
Nippon Medical School · JPTakara (Japan) · JPUniversity of Tsukuba · JPNational Center For Child Health and Development · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant adeno-associated virus serotype 9 (rAAV9) can specifically transduce muscle and neuronal tissues; thus, rAAV9 can potentially be used in gene therapy. However, rAAV9 is the most challenging rAAV serotype to purify. Traditionally, rAAV9 has been purified by ultracentrifugation, which is not scalable. We recently described a chromatographic purification protocol for rAAV1; this protocol can achieve scalable purifications. In this study, we attempted to optimize this protocol for purifying rAAV9 preparations, and we developed a novel, effective method for high-yield purification of rAAV9 using quaternary ammonium anion exchangers and size-exclusion chromatography. The final purified rAAV9 contained mainly three capsid proteins, as observed by SDS-PAGE. Furthermore, negative-stain electron microscopy demonstrated that 96.1% ± 1.1% of rAAV9 particles carried the viral genome containing the EGFP transgene, indicating that impurities and empty capsids can be eliminated with our purification protocol. The final rAAV9 titer obtained by our protocol totaled 2.5 ± 0.4 × 10

Indexed as

adeno-associated virusquaternary ammonium anion exchangersrAAV9ultracentrifugation-free protocol

Identifiers

PMID30533449
PMCPMC6276309
OpenAlexW2899451645

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.