Evaluating the Structural Stability of Recombinant Rotavirus Capsid Protein VP6 in Altered Physicochemical States Using Fluorescence and CD Spectroscopy.

Modibedi Lesego Gladys, Preenan Pillay

Abstract read

In one paragraph

Article in The protein journal, 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

2 authors.

Modibedi Lesego GladysCAES Laboratories, College of Agriculture and Environmental Sciences, University of South Africa, Florida, Roodepoort, 1709, South Africa. modiblg@unisa.ac.za.

Preenan PillayDepartment of Environmental and Life Science, College of Agriculture and Environmental Sciences, University of South Africa, Florida, Roodepoort, 1709, South Africa.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rotaviruses (RV) are a major cause of severe childhood diarrhoea, particularly in developing nations, necessitating stable vaccines. Therefore, the presented preliminary study aimed to assess the impact of altered physicochemical properties on the structural stability of recombinant rotavirus capsid protein VP6 (RV-VP6). The expression system used in this study was designed by genetically engineering the RV-VP6 into E. coli (NiCo21(DE3))-pET28a host-vector system and purified using liquid chromatography. The purified RV-VP6 homology detection and structure prediction were conducted using LC-MS and HHpred computational analysis, which indicated a 100% probability of 1QHD_A Viral Capsid VP6 (1.95 Å), representing the crystal structure of VP6. The secondary and tertiary structural stability of RV-VP6 was evaluated in altered pH and Ca

Indexed as

Antigens, ViralCapsid ProteinsRotavirusCalciumCircular DichroismEscherichia coliHydrogen-Ion ConcentrationProtein StabilityRecombinant ProteinsSpectrometry, FluorescenceAntigens, ViralCalciumCapsid ProteinsRecombinant ProteinsVP6 protein, RotavirusRecombinant proteinRotavirusStructural stabilityViral protein 6

Identifiers

PMID41243058

DOI10.1016/j.biologicals.2024.101782

What OpenQuestion holds

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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.