Evidence map›Paper›PMID 36140018›Full record

ArticleAntibiotics (Basel, Switzerland)2022

Dual Roles of Extracellular Histone H3 in Host Defense: Its Differential Regions Responsible for Antimicrobial and Cytotoxic Properties and Their Modes of Action.

Yuri Tanaka, Nanako Yamanaka, Izumi Koyano, Itaru Hasunuma, Tetsuya Kobayashi, Sakae Kikuyama, Shawichi Iwamuro

Open access · goldAbstract read
In one paragraph

Article in Antibiotics (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. UnderstandingCells · 2023
    Article
  4. Article
  5. 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

7 authors at 3 institutions in 1 country.

Yuri TanakaDepartment of Biology, Faculty of Science, Toho University, Chiba 274-8510, Japan.
Nanako YamanakaDepartment of Biology, Faculty of Science, Toho University, Chiba 274-8510, Japan.
Izumi KoyanoDepartment of Biology, Faculty of Science, Toho University, Chiba 274-8510, Japan.
Itaru HasunumaDepartment of Biology, Faculty of Science, Toho University, Chiba 274-8510, Japan.
Tetsuya KobayashiDivision of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Sakae KikuyamaDepartment of Biology, Faculty of Education and Integrated Arts and Sciences, Center for Advanced Biomedical Sciences, Waseda University, Tokyo 162-8480, Japan.
Shawichi IwamuroDepartment of Biology, Faculty of Science, Toho University, Chiba 274-8510, Japan.
Toho University · JPSaitama University · JPWaseda University · JP

Funding

JSPS KAKENHI 18K06319
6 · The paper itself

Abstract

Extracellular histones play a dual role-antimicrobial and cytotoxic-in host defense. In this study, we evaluated the antimicrobial and cytotoxic activities of histone H3 and identified the responsible molecular regions for these properties. Broth microdilution assays indicated that histone H3 exhibits growth inhibitory activity against not only Gram-negative and -positive bacteria but also fungi. Observations under scanning electron microscopy (SEM) revealed that histone H3 induced morphological abnormalities on the cell surface of a wide range of reference pathogens. MTT assays and SEM observations indicated that histone H3 has strong cytotoxic and cell lytic effects on mammalian normal, immortal, and tumor cell lines. Assays using synthetic peptides corresponding to fragments 1-34 (H3DP1), 35-68 (H3DP2), 69-102 (H3DP3), and 103-135 (H3DP4) of histone H3 molecule demonstrated that its antimicrobial activity and cytotoxicity are elicited by the H3DP2 and H3DP3 protein regions, respectively. Enzyme-linked endotoxin binding assays indicated that histones H3 and H3DP1, H3DP2, and H3DP4, but not H3DP3, exhibited high affinities toward lipopolysaccharide and lipoteichoic acid. Our findings are expected to contribute to the development of new histone H3-based peptide antibiotics that are not cytotoxic.

Indexed as

antimicrobial activitycell membrane destructioncytotoxicityELEBAhistone H3

Identifiers

PMID36140018
PMCPMC9495139
OpenAlexW4295814341

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.