Evidence map›Paper›PMID 29883666›Full record

ArticleJournal of pharmaceutical sciences2018

Effect of 2 Emulsion-Based Adjuvants on the Structure and Thermal Stability of Staphylococcus aureus Alpha-Toxin.

Yangjie Wei, Jian Xiong, Nicholas R Larson, Vidyashankara Iyer, Gautam Sanyal, Sangeeta B Joshi, David B Volkin, C Russell Middaugh

Abstract read
In one paragraph

Article in Journal of pharmaceutical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Yangjie WeiMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.
Jian XiongMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.
Nicholas R LarsonMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.
Vidyashankara IyerBiopharmaceutical Development, Medimmune Inc., Gaithersburg, Maryland 20878.
Gautam SanyalBiopharmaceutical Development, Medimmune Inc., Gaithersburg, Maryland 20878.
Sangeeta B JoshiMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.
David B VolkinMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.
C Russell MiddaughMacromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047. Electronic address: middaugh@ku.edu.
University of Kansas · US

Funding

PHARMACEUTICAL ASPECTS OF BIOTECHNOLOGY TRAININGT32GM008359 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SIAHAAN, TERUNA J., VOLKIN, DAVID · 1989 to 2018
$5.0M
NIGMS NIH HHS T32 GM008359
6 · The paper itself

Abstract

The effects of 2 squalene-based emulsion adjuvant systems (MedImmune emulsion 0 [ME.0] and Stable Emulsion [SE]) on the structure and stability of the recombinant protein antigen alpha-toxin (AT), a potential vaccine candidate for Staphylococcus aureus infection, were investigated using Fourier-transform infrared spectroscopy and both steady-state and time-resolved intrinsic fluorescence spectroscopy as well as differential scanning calorimetry (DSC). A component study, performed to identify the effects of the individual emulsion's components, showed negligible interactions between AT and ME.0. DSC analysis showed the ME.0 emulsion thermally destabilized AT, probably because of changes in the buffer composition of AT upon mixing. The SE emulsion caused increased alpha-helix and decreased beta-sheet content in AT, and a significant blue shift in the fluorescence spectra relative to that of AT in solution. DSC analysis showed SE exerted a dramatic thermal stabilization effect on AT, probably attributable to an interaction between AT and SE. Size exclusion chromatography showed a complete loss in the recovery of AT when mixed with SE, but not ME.0, indicating a high degree of interaction with SE. This work successfully characterized the biophysical properties of AT in the presence of 2 emulsion adjuvants including a component study to rationalize how emulsion components affect protein antigen stability.

Indexed as

Hot TemperatureAdjuvants, ImmunologicAdjuvants, PharmaceuticBacterial ToxinsEmulsionsHemolysin ProteinsProtein StabilitySpectroscopy, Fourier Transform InfraredStaphylococcus aureusAdjuvants, ImmunologicAdjuvants, PharmaceuticBacterial ToxinsEmulsionsHemolysin Proteinsstaphylococcal alpha-toxinemulsion adjuvantprotein structuresqualenestabilityStaphylococcus aureus alpha-toxinvaccine formulation

Identifiers

PMID29883666
PMCPMC6089638
OpenAlexW2807070994

What OpenQuestion holds

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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.