Evidence map›Paper›PMID 31073667›Full record

ArticleCurrent genetics2019

Identification and functional characterization of Candida albicans mannose-ethanolamine phosphotransferase (Mcd4p).

Satoru Hasegawa, Yuimi Yamada, Noboru Iwanami, Yusuke Nakayama, Hironobu Nakayama, Shun Iwatani, Takahiro Oura, Susumu Kajiwara

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Article in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
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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

8 authors at 2 institutions in 1 country.

Satoru HasegawaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Yuimi YamadaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Noboru IwanamiSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Yusuke NakayamaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Hironobu NakayamaFaculty of Pharmaceutical Sciences, Suzuka University of Medical Science, Minami-Tamagakicho, 3500-3, Suzuka, Mie, 513-8670, Japan.
Shun IwataniSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Takahiro OuraSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Susumu KajiwaraSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 J3-07 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan. skajiwar@bio.titech.ac.jp.ORCID http://orcid.org/0000-0003-4272-2944
Tokyo Institute of Technology · JPSuzuka University of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylphosphatidylinositol (GPI) is an important compound for the growth of fungi, because GPI-anchored proteins including glycosyltransferases and adhesins are involved in cell-wall integrity, adhesion, and nutrient uptake in this organism. In this study, we examined orf19.5244 in the genome database of the pathogenic fungus Candida albicans, a homologue of the Saccharomyces cerevisiae mannose-ethanolamine phosphotransferase gene, MCD4, which plays a role in GPI synthesis. Expression of this homologue, designated CaMCD4, restored cell growth in a defective conditional mcd4 mutant of S. cerevisiae, Scmcd4t, in which expression of native MCD4 was repressed in the presence of doxycycline (Dox). Analysis of radiolabeled lipids showed that the accumulation of abnormal GPI anchor precursors in Scmcd4t decreased markedly upon expression of CaMCD4. Moreover, we constructed a single mutant (Camcd4/CaMCD4) and a conditional double mutant (Camcd4/Camcd4t) at the MCD4 locus of C. albicans. Repression of CaMCD4 expression by Dox led to a decrease in growth and appearance of abnormal morphology in C. albicans, both in vitro and in a silkworm infection model. These results suggest that CaMcd4p is indispensable for growth of C. albicans both in vitro and in infected hosts and a candidate target for the development of new antifungals.

Indexed as

Candida albicansCodonFungal ProteinsGene Expression Regulation, FungalGlycosylphosphatidylinositolsMembrane ProteinsMutationPhenotypeVirulenceCodonFungal ProteinsGlycosylphosphatidylinositolsMembrane ProteinsCandida albicansCodon optimizationGlycosylphosphatidylinositol (GPI)-anchor synthesis

Identifiers

PMID31073667
OpenAlexW2944808462

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.