Evidence map›Paper›PMID 25568977›Full record

ArticleToxins2015

Plectasin, first animal toxin-like fungal defensin blocking potassium channels through recognizing channel pore region.

Fang Xiang, Zili Xie, Jing Feng, Weishan Yang, Zhijian Cao, Wenxin Li, Zongyun Chen, Yingliang Wu

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

8 authors at 1 institution in 1 country.

Fang XiangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. xiangfang2012@126.com.
Zili XieState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. zlxie@whu.edu.cn.
Jing FengState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. jfeng@whu.edu.cn.
Weishan YangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. weishanyang@whu.edu.cn.
Zhijian CaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. zjcao@whu.edu.cn.
Wenxin LiState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. wxli@whu.edu.cn.
Zongyun ChenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. zjcao@whu.edu.cn.
Yingliang WuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China. ylwu@whu.edu.cn.
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The potassium channels were recently found to be inhibited by animal toxin-like human β-defensin 2 (hBD2), the first defensin blocker of potassium channels. Whether there are other defensin blockers from different organisms remains an open question. Here, we reported the potassium channel-blocking plectasin, the first defensin blocker from a fungus. Based on the similar cysteine-stabilized alpha-beta (CSαβ) structure between plectasin and scorpion toxins acting on potassium channels, we found that plectasin could dose-dependently block Kv1.3 channel currents through electrophysiological experiments. Besides Kv1.3 channel, plectasin could less inhibit Kv1.1, Kv1.2, IKCa, SKCa3, hERG and KCNQ channels at the concentration of 1 μΜ. Using mutagenesis and channel activation experiments, we found that outer pore region of Kv1.3 channel was the binding site of plectasin, which is similar to the interacting site of Kv1.3 channel recognized by animal toxin blockers. Together, these findings not only highlight the novel function of plectasin as a potassium channel inhibitor, but also imply that defensins from different organisms functionally evolve to be a novel kind of potassium channel inhibitors.

Indexed as

DefensinsHEK293 CellsHumansMycotoxinsPeptidesPotassium Channel BlockersPotassium ChannelsDefensinsMycotoxinsPeptidesplectasinPotassium Channel BlockersPotassium Channels

Identifiers

PMID25568977
PMCPMC4303811
OpenAlexW2080352183

What OpenQuestion holds

Textmetadata
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.