Evidence map›Paper›PMID 32070701›Full record

ArticleJournal of pharmaceutical sciences2020

Process Characterization and Biophysical Analysis for a Yeast-Expressed Phlebotomus papatasi Salivary Protein (PpSP15) as a Leishmania Vaccine Candidate.

Wen-Hsiang Chen, Mun Peak Nyon, Mohan V Poongavanam, Zhuyun Liu, Amadeo B Biter, Rakhi T Kundu, Ulrich Strych, Peter J Hotez, Maria Elena Bottazzi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of pharmaceutical sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. 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

9 authors.

Wen-Hsiang ChenDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030. Electronic address: Wen-Hsiang.Chen@bcm.edu.
Mun Peak NyonDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Mohan V PoongavanamDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Zhuyun LiuDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Amadeo B BiterDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Rakhi T KunduDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Ulrich StrychDepartments of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Texas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030.
Peter J HotezTexas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Department of Biology, College of Arts and Sciences, Baylor University, Waco, Texas 76706; James A. Baker III Institute for Public Policy, Rice University, Houston, Texas 77005; Hagler Institute for Advanced Study at Texas A&M University, College Station, Houston, Texas 77843.
Maria Elena BottazziTexas Children's Hospital Center for Vaccine Development, Baylor College of Medicine, 1102 Bates Street, Houston, Texas 77030; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, One Baylor Plaza, BCM113, Houston, Texas 77030; Department of Biology, College of Arts and Sciences, Baylor University, Waco, Texas 76706. Electronic address: bottazzi@bcm.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cutaneous leishmaniasis is a neglected tropical disease caused by the parasite Leishmania and transmitted by sandflies. It has become a major health problem in many tropical and subtropical countries, especially in regions of conflict and political instability. Currently, there are only limited drug treatments and no available licensed vaccine; thus, the need for more therapeutic interventions remains urgent. Previously, a DNA vaccine encoding a 15 kDa sandfly (Phlebotomus papatasi) salivary protein (PpSP15) and recombinant nonpathogenic Leishmania tarentolae secreting PpSP15 have been shown to induce protective immunity against Leishmania major in mice, demonstrating that PpSP15 is a promising vaccine candidate. In this study, we developed a fermentation process in yeast with a yield of ~1g PpSP15/L and a scalable purification process consisting of only 2 chromatographic purification steps with high binding capacity for PpSP15, suggesting that PpSP15 can be produced economically. The biophysical/biochemical analysis of the purified PpSP15 indicated that the protein was of high purity (>97%) and conformationally stable between pH 4.4 and 9.0. More importantly, the recombinant protein had a defined structure similar to that of the related PdSP15 from Phlebotomus duboscqi, implying the suitability of the yeast expression system for producing a correctly folded PpSP15.

Indexed as

Leishmaniasis VaccinesPhlebotomusAnimalsInsect ProteinsMiceSaccharomyces cerevisiaeSalivary Proteins and PeptidesInsect ProteinsLeishmaniasis VaccinesSalivary Proteins and Peptidesanalytical biochemistrybiopharmaceutical characterizationbiotechnologychromatographyprotein(s)vaccine(s)

Identifiers

PMID32070701
PMCPMC7125844

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.