Evidence map›Paper›PMID 25558400›Full record

ArticleActa naturae2014

Acipensins - Novel Antimicrobial Peptides from Leukocytes of the Russian Sturgeon Acipenser gueldenstaedtii.

O V Shamova, D S Orlov, S V Balandin, E I Shramova, E V Tsvetkova, P V Panteleev, Yu F Leonova, A A Tagaev, V N Kokryakov, T V Ovchinnikova

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PubMed Full text at PMC
In one paragraph

Article in Acta naturae, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

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  8. Recent updates of marine antimicrobial peptides.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018
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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

10 authors at 5 institutions in 3 countries.

O V ShamovaInstitute of Experimental Medicine, Northwest Branch of the Russian Academy of Medical Sciences, Academician Pavlov Street, 12, Saint-Petersburg 197376, Russia ; Saint-Petersburg State University, Universitetskaya Embankment, 7/9, Saint-Petersburg 199034, Russia.
D S OrlovInstitute of Experimental Medicine, Northwest Branch of the Russian Academy of Medical Sciences, Academician Pavlov Street, 12, Saint-Petersburg 197376, Russia ; Saint-Petersburg State University, Universitetskaya Embankment, 7/9, Saint-Petersburg 199034, Russia.
S V BalandinShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia ; Moscow Institute of Physics and Technology (State University), Department of Physicochemical Biology and Biotechnology, Institutskii Pereulok, 9, Dolgoprudny 141700, Moscow Region, Russia.
E I ShramovaShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia.
E V TsvetkovaSaint-Petersburg State University, Universitetskaya Embankment, 7/9, Saint-Petersburg 199034, Russia.
P V PanteleevShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia.
Yu F LeonovaShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia.
A A TagaevShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia.
V N KokryakovInstitute of Experimental Medicine, Northwest Branch of the Russian Academy of Medical Sciences, Academician Pavlov Street, 12, Saint-Petersburg 197376, Russia ; Saint-Petersburg State University, Universitetskaya Embankment, 7/9, Saint-Petersburg 199034, Russia.
T V OvchinnikovaShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street, 16/10, Moscow 117997, Russia ; Moscow Institute of Physics and Technology (State University), Department of Physicochemical Biology and Biotechnology, Institutskii Pereulok, 9, Dolgoprudny 141700, Moscow Region, Russia.
Institute of Bioorganic Chemistry · RUAcademy of Medical Sciences · GBCzech Academy of Sciences, Institute of Experimental Medicine · CZMoscow Institute of Physics and Technology · RUSt Petersburg University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) play an important role in the innate defense mechanisms in humans and animals. We have isolated and studied a set of antimicrobial peptides from leukocytes of the Russian sturgeon Acipenser gueldenstaedtii belonging to a subclass of chondrosteans, an ancient group of bony fish. Structural analysis of the isolated peptides, designated as acipensins (Ac), revealed in leukocytes of the Russian sturgeon six novel peptides with molecular masses of 5336.2 Da, 3803.0 Da, 5173.0 Da, 4777.5 Da, 5449.4 Da, and 2740.2 Da, designated as Ac1-Ac6, respectively. Complete primary structures of all the isolated peptides were determined, and the biological activities of three major components - Ac1, Ac2, and Ac6 - were examined. The peptides Ac1, Ac2, Ac3, Ac4, and Ac5 were found to be the N-terminal acetylated fragments 1-0, 1-5, 1-9, 1-4, and 1-1 of the histone H2A, respectively, while Ac6 was shown to be the 62-5 fragment of the histone H2A. The peptides Ac1 and Ac2 displayed potent antimicrobial activity towards Gram-negative and Gram-positive bacteria (Escherichia coli ML35p, Listeria monocytogenes EGD, MRSA ATCC 33591) and the fungus Candida albicans 820, while Ac6 proved effective only against Gram-negative bacteria. The efficacy of Ac 1 and Ac2 towards the fungus and MRSA was reduced upon an increase in the ionic strength of the solution. Ac1, Ac2, and Ac6, at concentrations close to their minimum inhibitory concentrations, enhanced the permeability of the E.coli ML35p outer membrane to the chromogenic marker, but they did not affect appreciably the permeability of the bacterial inner membrane in comparison with a potent pore-forming peptide, protegrin 1. Ac1, Ac2, and Ac6 revealed no hemolytic activity against human erythrocytes at concentrations of 1 to 40 μM and had no cytotoxic effect (1 to 20 μM) on K-562 and U-937 cells in vitro. Our findings suggest that histone-derived peptides serve as important anti-infective host defense molecules.

Indexed as

acipensinantimicrobial peptideshistone H2A derivativesinnate immunitysturgeon leukocytes

Identifiers

PMID25558400
PMCPMC4273097
OpenAlexW240653073

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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.