Evidence map›Paper›PMID 27637945›Full record

ArticleAMB Express2016

NFAP2, a novel cysteine-rich anti-yeast protein from Neosartorya fischeri NRRL 181: isolation and characterization.

Liliána Tóth, Zoltán Kele, Attila Borics, László G Nagy, Györgyi Váradi, Máté Virágh, Miklós Takó, Csaba Vágvölgyi, László Galgóczy

Open access · goldAbstract read
In one paragraph

Article in AMB Express, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 63 citations in OpenAlex.

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  13. Current Perspectives of Antifungal Therapy: A Special Focus onJournal of fungi (Basel, Switzerland) · 2024
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  19. Special Issue "Control of Postharvest PathogenicJournal of fungi (Basel, Switzerland) · 2022
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  20. Antimicrobial Peptides with Anti-International journal of molecular sciences · 2022
    Review
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 at 3 institutions in 2 countries.

Liliána TóthDepartment of Microbiology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary.
Zoltán KeleDepartment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm tér 8, Szeged, 6720, Hungary.
Attila BoricsInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Szeged, 6726, Hungary.
László G NagyInstitute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Szeged, 6726, Hungary.
Györgyi VáradiDepartment of Medical Chemistry, Faculty of Medicine, University of Szeged, Dóm tér 8, Szeged, 6720, Hungary.
Máté VirághDepartment of Microbiology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary.
Miklós TakóDepartment of Microbiology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary.
Csaba VágvölgyiDepartment of Microbiology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary.
László GalgóczyDepartment of Microbiology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, Szeged, 6726, Hungary. galgoczi@gmail.com.ORCID http://orcid.org/0000-0002-6976-8910
University of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUInnsbruck Medical University · AT

Funding

Austrian Science Fund FWF M 1776
6 · The paper itself

Abstract

The increasing incidence of fungal infections and damages due to drug-resistant fungi urges the development of new antifungal strategies. The cysteine-rich antifungal proteins from filamentous ascomycetes provide a feasible base for protection against molds due to their potent antifungal activity on them. In contrast to this, they show no or weak activity on yeasts, hence their applicability against this group of fungi is questionable. In the present study a 5.6 kDa anti-yeast protein (NFAP2) is isolated, identified and characterized from the ferment broth of Neosartorya fischeri NRRL 181. Based on a phylogenetic analysis, NFAP2 and its putative homologs represent a new group of ascomycetous cysteine-rich antifungal proteins. NFAP2 proved to be highly effective against tested yeasts involving clinically relevant Candida species. NFAP2 did not cause metabolic inactivity and apoptosis induction, but its plasma membrane disruption ability was observed on Saccharomyces cerevisiae. The antifungal activity was maintained after high temperature treatment presumably due to the in silico predicted stable tertiary structure. The disulfide bond-stabilized, heat-resistant folded structure of NFAP2 was experimentally proved. After further investigations of antifungal mechanism, structure and toxicity, NFAP2 could be applicable as a potent antifungal agent against yeasts.

Indexed as

Anti-yeast activityCandida spp.Cysteine-rich antifungal proteinNeosartorya fischeriProtein isolationProtein structure

Identifiers

PMID27637945
PMCPMC5025423
OpenAlexW2520227115

What OpenQuestion holds

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LicenceCC BY
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.