Evidence map›Paper›PMID 26839079›Full record

ArticleHuman vaccines & immunotherapeutics2016

Expression and purification of an engineered, yeast-expressed Leishmania donovani nucleoside hydrolase with immunogenic properties.

Elissa M Hudspeth, Qian Wang, Christopher A Seid, Molly Hammond, Junfei Wei, Zhuyun Liu, Bin Zhan, Jeroen Pollet, Michael J Heffernan, C Patrick McAtee and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Human vaccines & immunotherapeutics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 8 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

16 authors at 6 institutions in 1 country.

Elissa M Hudspetha Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Qian Wanga Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Christopher A Seida Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Molly Hammonda Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Junfei Weia Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Zhuyun Liua Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Bin Zhana Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Jeroen Polleta Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Michael J Heffernana Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
C Patrick McAteea Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
David A Englerc Proteomics Programmatic Core Laboratory, Houston Methodist Hospital Research Institute , Houston , TX , USA.
Risë K Matsunamic Proteomics Programmatic Core Laboratory, Houston Methodist Hospital Research Institute , Houston , TX , USA.
Ulrich Strycha Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Oluwatoyin A Asojoa Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Peter J Hoteza Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Maria Elena Bottazzia Department of Pediatrics (Section of Tropical Medicine) , National School of Tropical Medicine, Baylor College of Medicine , Houston , TX , USA.
Sabin Vaccine Institute · USTexas Children's Hospital · USBaylor College of Medicine · USBaylor University · USHouston Methodist · USMethodist Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leishmania donovani is the major cause of visceral leishmaniasis (kala-azar), now recognized as the parasitic disease with the highest level of mortality second only to malaria. No human vaccine is currently available. A 36 kDa L. donovani nucleoside hydrolase (LdNH36) surface protein has been previously identified as a potential vaccine candidate antigen. Here we present data on the expression of LdNH36 in Pichia pastoris and its purification at the 20 L scale to establish suitability for future pilot scale manufacturing. To improve efficiency of process development and ensure reproducibility, 4 N-linked glycosylation sites shown to contribute to heterogeneous high-mannose glycosylation were mutated to glutamine residues. The mutant LdNH36 (LdNH36-dg2) was expressed and purified to homogeneity. Size exclusion chromatography and light scattering demonstrated that LdNH36-dg2 existed as a tetramer in solution, similar to the wild-type recombinant L. major nucleoside hydrolase. The amino acid mutations do not affect the tetrameric interface as confirmed by theoretical modeling, and the mutated amino acids are located outside the major immunogenic domain. Immunogenic properties of the LdNH36-dg2 recombinant protein were evaluated in BALB/c mice using formulations that included a synthetic CpG oligodeoxynucleotide, together with a microparticle delivery platform (poly(lactic-co-glycolic acid)). Mice exhibited high levels of IgG1, IgG2a, and IgG2b antibodies that were reactive to both LdNH36-dg2 and LdNH36 wild-type. While the point mutations did affect the hydrolase activity of the enzyme, the IgG antibodies elicited by LdNH36-dg2 were shown to inhibit the hydrolase activity of the wild-type LdNH36. The results indicate that LdNH36-dg2 as expressed in and purified from P. pastoris is suitable for further scale-up, manufacturing, and testing in support of future first-in-humans phase 1 clinical trials.

Indexed as

Gene ExpressionAnimalsAntibodies, ProtozoanAntigens, ProtozoanChromatography, GelDynamic Light ScatteringFemaleImmunoglobulin GLeishmania donovaniMice, Inbred BALB CModels, MolecularMolecular WeightMutant ProteinsN-Glycosyl HydrolasesPichiaProtein MultimerizationAntibodies, ProtozoanAntigens, ProtozoanImmunoglobulin GMutant ProteinsN-Glycosyl HydrolasesRecombinant ProteinsCpG OligodeoxynucleotidefermentationLeishmania donovaniPoly(lactic-co-glycolic acid) (PLGA)purification

Identifiers

PMID26839079
PMCPMC4964838
OpenAlexW2264557064

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.