Evidence map›Paper›PMID 26343612›Full record

ArticleMolecules (Basel, Switzerland)2015

Autodisplay of Human Hyaluronidase Hyal-1 on Escherichia coli and Identification of Plant-Derived Enzyme Inhibitors.

Zoya Orlando, Isabelle Lengers, Matthias F Melzig, Armin Buschauer, Andreas Hensel, Joachim Jose

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Hyaluronidase-ExpressingMolecular cancer therapeutics · 2020
    Article
  7. Article
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

6 authors.

Zoya OrlandoInstitute of Pharmaceutical and Medicinal Chemistry, Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany. zoya.orlando@uni-muenster.de.
Isabelle LengersInstitute of Pharmaceutical and Medicinal Chemistry, Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany. isabelle.lengers@uni-muenster.de.
Matthias F MelzigInstitute of Pharmacy, Pharmaceutical Biology, Freie Universität Berlin, Königin-Luise Str. 2+4, 14195 Berlin, Germany. melzig@zedat.fu-berlin.de.
Armin BuschauerDepartment of Pharmaceutical/Medicinal Chemistry II, Institute of Pharmacy, University Regensburg, Universitätsstr. 31, 93040 Regensburg, Germany. armin.buschauer@ur.de.
Andreas HenselInstitute of Pharmaceutical Biology and Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany. ahensel@uni-muenster.de.
Joachim JoseInstitute of Pharmaceutical and Medicinal Chemistry, Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany. joachim.jose@uni-muenster.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hyaluronan (HA) is the main component of the extracellular matrix (ECM). Depending on its chain size, it is generally accepted to exert diverse effects. High molecular weight HA is anti-angiogenic, immunosuppressive and anti-inflammatory, while lower fragments are angiogenic and inflammatory. Human hyaluronidase Hyal-1 (Hyal-1) is one of the main enzymes in the metabolism of HA. This makes Hyal-1 an interesting target. Not only for functional and mechanistic studies, but also for drug development. In this work, Hyal-1 was expressed on the surface of E. coli, by applying Autodisplay, to overcome formation of inactive "inclusion bodies". With the cells displaying Hyal-1 an activity assay was performed using "stains-all" dye. Subsequently, the inhibitory effects of four saponins and 14 plant extracts on the activity of surface displayed Hyal-1 were evaluated. The determined IC50 values were 177 µM for glycyrrhizic acid, 108 µM for gypsophila saponin 2, 371 µM for SA1657 and 296 µM for SA1641. Malvae sylvestris flos, Equiseti herba and Ononidis radix extracts showed IC50 values between 1.4 and 1.7 mg/mL. In summary, Autodisplay enabled the expression of functional human target protein Hyal-1 in E. coli and facilitated an accelerated testing of potential inhibitors.

Indexed as

Antigens, NeoplasmCell MembraneEnzyme InhibitorsEscherichia coliEscherichia coli ProteinsGlycyrrhizic AcidHistone AcetyltransferasesHumansHyaluronoglucosaminidasePlant ExtractsSaponinsAntigens, NeoplasmEnzyme InhibitorsEscherichia coli ProteinsGlycyrrhizic AcidHistone AcetyltransferasesHyaluronoglucosaminidaseOGA protein, humanPlant ExtractsSaponinsAutodisplayHyal-1hyaluronannatural inhibitors

Identifiers

PMID26343612
PMCPMC6331893

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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.