Evidence map›Paper›PMID 31209048›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Low cationicity is important for systemic in vivo efficacy of database-derived peptides against drug-resistant Gram-positive pathogens.

Biswajit Mishra, Jayaram Lakshmaiah Narayana, Tamara Lushnikova, Xiuqing Wang, Guangshun Wang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

67 citing papers in PubMed, 117 citations in OpenAlex.

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7 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 2 countries.

Biswajit MishraDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198-5900.
Jayaram Lakshmaiah NarayanaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198-5900.
Tamara LushnikovaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198-5900.
Xiuqing WangDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198-5900.
Guangshun WangDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198-5900; gwang@unmc.edu.
University of Nebraska Medical Center · USNingxia Medical University · CN

Funding

Database designed novel anti-MRSA peptidesR01AI105147 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN · 2015 to 2019
$1.9M
Database designed novel anti-MRSA peptidesR56AI105147 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN · 2013 to 2013
$354k
NIAID NIH HHS R01 AI105147NIAID NIH HHS R56 AI105147
6 · The paper itself

Abstract

As bacterial resistance to traditional antibiotics continues to emerge, new alternatives are urgently needed. Antimicrobial peptides (AMPs) are important candidates. However, how AMPs are designed with in vivo efficacy is poorly understood. Our study was designed to understand structural moieties of cationic peptides that would lead to their successful use as antibacterial agents. In contrast to the common perception, serum binding and peptide stability were not the major reasons for in vivo failure in our studies. Rather, our systematic study of a series of peptides with varying lysines revealed the significance of low cationicity for systemic in vivo efficacy against Gram-positive pathogens. We propose that peptides with biased amino acid compositions are not favored to associate with multiple host factors and are more likely to show in vivo efficacy. Thus, our results uncover a useful design strategy for developing potent peptides against multidrug-resistant pathogens.

Indexed as

Amino AcidsAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesComputer SimulationDrug DesignDrug Resistance, Multiple, BacterialGram-Positive BacteriaGram-Positive Bacterial InfectionsMiceMicrobial Sensitivity TestsAmino AcidsAnti-Bacterial AgentsAntimicrobial Cationic Peptidesantimicrobial peptidesbasic amino acidsin vivo efficacypeptide designprotease stability

Identifiers

PMID31209048
PMCPMC6613076
OpenAlexW2949619879

What OpenQuestion holds

Textmetadata
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.