Evidence map›Paper›PMID 31330090›Full record

ArticleThe FEBS journal2019

Post-translational modifications in capsid proteins of recombinant adeno-associated virus (AAV) 1-rh10 serotypes.

Bertin Mary, Shubham Maurya, Sathyathithan Arumugam, Vikas Kumar, Giridhara R Jayandharan

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  6. Navigating the Hurdles of Intra-Articular AAV Gene Therapy.International journal of molecular sciences · 2025
    Review
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  9. A clinician's guide to AAV production - How manufacturing platforms shape vector properties.Medizinische Genetik : Mitteilungsblatt des Berufsverbandes Medizinische Genetik e.V · 2025
    Article
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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

5 authors at 4 institutions in 2 countries.

Bertin MaryDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Shubham MauryaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Sathyathithan ArumugamDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.
Vikas KumarMass Spectrometry and Proteomics Core Facility, University of Nebraska Medical Center, Omaha, NE, USA.
Giridhara R JayandharanDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, India.ORCID 0000-0001-9353-9053
Indian Institute of Technology Kanpur · INSASTRA University · INUniversity of Nebraska Medical Center · USVellore Institute of Technology University · IN

Funding

Department of Biotechnology, Ministry of Science and Technology BT/PR14748/MED/12/491/2010Department of Science and Technology, Ministry of Science and Technology Swarnajayanti FellowshipSenior Innovative Young Biotechnologist Award 2010 BT/03/IYBA/2010Wellcome Trust
6 · The paper itself

Abstract

Post-translational modifications in viral capsids are known to fine-tune and regulate several aspects of the infective life cycle of several viruses in the host. Recombinant viruses that are generated in a specific producer cell line are likely to inherit unique post-translational modifications during intra-cellular maturation of its capsid proteins. Data on such post-translational modifications in the capsid of recombinant adeno-associated virus serotypes (AAV1-rh10) is limited. We have employed liquid chromatography and mass spectrometry analysis to characterize post-translational modifications in AAV1-rh10 capsid protein. Our analysis revealed a total of 52 post-translational modifications in AAV2-AAVrh10 capsids, including ubiquitination (17%), glycosylation (36%), phosphorylation (21%), SUMOylation (13%) and acetylation (11%). While AAV1 had no detectable post-translational modification, at least four AAV serotypes had >7 post-translational modifications in their capsid protein. About 82% of these post-translational modifications are novel. A limited validation of AAV2 capsids by MALDI-TOF and western blot analysis demonstrated minimal glycosylation and ubiquitination of AAV2 capsids. To further validate this, we disrupted a glycosylation site identified in AAV2 capsid (AAV2-N253Q), which severely compromised its packaging efficiency (~ 100-fold vs. AAV2 wild-type vectors). In order to confirm other post-translational modifications detected such as SUMOylation, mutagenesis of a SUMOylation site(K258Q) in AAV2 was performed. This mutant vector demonstrated reduced levels of SUMO-1/2/3 proteins and negligible transduction, 2 weeks after ocular gene transfer. Our study underscores the heterogeneity of post-translational modifications in AAV vectors. The data presented here, should facilitate further studies to understand the biological relevance of post-translational modifications in AAV life cycle and the development of novel bioengineered AAV vectors for gene therapy applications. ENZYMES: Trypsin, EC 3.4.21.4.

Indexed as

AcetylationCapsid ProteinsDependovirusGenetic VectorsGlycosylationHeLa CellsHumansMutationParvovirinaePhosphorylationProtein Processing, Post-TranslationalSerogroupTransduction, GeneticUbiquitinationCapsid ProteinsAAVcapsidLCMSMALDI-TOF analysispost-translational modification

Identifiers

PMID31330090
PMCPMC7496479
OpenAlexW2964135966

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.