Evidence map›Paper›PMID 34291903›Full record

ArticleAnalytical chemistry2021

Rapid Highly-Efficient Digestion and Peptide Mapping of Adeno-Associated Viruses.

Estee Naggar Toole, Craig Dufresne, Somak Ray, Alexander Schwann, Ken Cook, Alexander R Ivanov

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
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  8. Article
  9. Predicting epitopes for vaccine development using bioinformatics tools.Therapeutic advances in vaccines and immunotherapy · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 3 countries.

Estee Naggar TooleThermo Fisher Scientific, West Palm Beach, Florida 33401, United States.ORCID 0000-0002-0785-1073
Craig DufresneThermo Fisher Scientific, West Palm Beach, Florida 33401, United States.
Somak RayBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115, United States.
Alexander SchwannThermo Fisher Scientific, Neuhofstrasse 11, 4153 Reinach, Switzerland.
Ken CookThermo Fisher Scientific, Stafford House, 1 Boundary Park, Hemel Hempstead HP2 7GE, United Kingdom.ORCID 0000-0001-5176-7736
Alexander R IvanovBarnett Institute of Chemical and Biological Analysis, Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115, United States.ORCID 0000-0002-4691-8488
Northeastern University · USThermo Fisher Scientific (Switzerland) · CHThermo Fisher Scientific (United Kingdom) · GBThermo Fisher Scientific (United States) · US

Funding

Effect of methodological and biological variability on molecular profiling of extracellular vesicles in cancer detectionR01CA218500 · NCI · NORTHEASTERN UNIVERSITY · PI GHIRAN, IONITA CALIN, IVANOV, ALEXANDER R. · 2018 to 2022
$4.0M
Robust ultra-high sensitivity proteomic technologies for limited samplesR35GM136421 · NIGMS · NORTHEASTERN UNIVERSITY · PI Alexander R. Ivanov · 2020 to 2026
$3.4M
Deep Proteomic Profiling of Rare CellsR01GM120272 · NIGMS · NORTHEASTERN UNIVERSITY · PI IVANOV, ALEXANDER R. · 2016 to 2019
$1.5M
NCI NIH HHS R01 CA218500NIGMS NIH HHS R01 GM120272NIGMS NIH HHS R35 GM136421
6 · The paper itself

Abstract

Adeno-associated viruses (AAVs) comprise an area of rapidly growing interest due to their ability to act as a gene delivery vehicle in novel gene therapy strategies and vaccine development. Peptide mapping is a common technique in the biopharmaceutical industry to confirm the correct sequence, product purity, post-translational modifications (PTMs), and stability. However, conventional peptide mapping is time-consuming and has proven difficult to reproduce with viral capsids because of their high structural stability and the suboptimal localization of trypsin cleavage sites in the AAV protein sequences. In this study, we present an optimized peptide mapping-based workflow that provides thorough characterization within 1 day. This workflow is also highly reproducible due to its simplicity having very few steps and is easy to perform proteolytic digestion utilizing thermally stable pepsin, which is active at 70 °C in acidic conditions. The acidic conditions of the peptic digestions drive viral capsid denaturation and improve cleavage site accessibility. We characterized the efficiency and ease of digestion through peptide mapping of the AAV2 viral capsid protein. Using nanoflow liquid chromatography coupled with tandem mass spectrometry, we achieved 100% sequence coverage of the low-abundance VP1 capsid protein with a digestion process taking only 10 min to prepare and 45 min to complete the digestion.

Indexed as

CapsidDependovirusCapsid ProteinsDigestionHumansPeptide MappingCapsid Proteins

Identifiers

PMID34291903
PMCPMC8743033
OpenAlexW3186432004

What OpenQuestion holds

Textmetadata
LicenceTDM
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.