Evidence map›Paper›PMID 23880927›Full record

ArticleMarine drugs2013

pH-dependent solution structure and activity of a reduced form of the host-defense peptide myticin C (Myt C) from the mussel Mytilus galloprovincialis.

Alicia Martinez-Lopez, Jose Antonio Encinar, Regla Maria Medina-Gali, Pablo Balseiro, Pablo Garcia-Valtanen, Antonio Figueras, Beatriz Novoa, Amparo Estepa

Open access · goldAbstract read
In one paragraph

Article in Marine drugs, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

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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.

Alicia Martinez-LopezMolecular and Cell Institute, University Miguel Hernández (IBMC-UMH), Elche 03202, Spain. alicia.martinez@umh.es
Jose Antonio Encinar
Regla Maria Medina-Gali
Pablo Balseiro
Pablo Garcia-Valtanen
Antonio Figueras
Beatriz Novoa
Amparo Estepa
Universitat de Miguel Hernández d'Elx · ESInstituto de Investigacións Mariñas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myticin C (Myt C) is a highly variable host-defense peptide (HDP) associated to the immune response in the mediterranean mussel (Mytilus galloprovincialis), which has shown to be active across species due to its strong antiviral activity against a fish rhabdovirus found in fish cells overexpressing this HDP. However, the potential antimicrobial properties of any synthetic analogue of Myt C has not yet been analysed. Thus, in this work we have synthesised the sequence of the mature peptide of Myt C variant c and analysed the structure activity relationships of its reduced (non-oxidized) form (red-MytCc). In contrast to results previously reported for oxidized isoforms of mussel myticins, red-MytCc was not active against bacteria at physiological pH and showed a moderate antiviral activity against the viral haemorrhagic septicaemia (VHS) rhabdovirus. However, its chemotactic properties remained active. Structure/function studies in neutral and acid environments by means of infrared spectroscopy indicated that the structure of red-MytCc is pH dependent, with acid media increasing its alpha-helical content. Furthermore, red-MytCc was able to efficiently aggregate artificial phospholipid membranes at low pH, as well as to inhibit the Escherichia coli growth, suggesting that this activity is attributable to its more structured form in an acidic environment. All together, these results highlight the dynamic and environmentally sensitive behavior of red-Myt C in solution, and provide important insights into Myt C structure/activity relationships and the requirements to exert its antimicrobial/immunomodulatory activities. On the other hand, the pH-dependent direct antimicrobial activity of Myt C suggests that this HDP may be a suitable template for the development of antimicrobial agents that would function selectively in specific pH environments, which are sorely needed in this "antibiotic-resistance era".

Indexed as

AnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesAntiviral AgentsBivalviaBlood ProteinsCells, CulturedEscherichia coliFishesHydrogen-Ion ConcentrationMytilusPeptidesProtein IsoformsProtein Structure, SecondaryRhabdoviridaeSolutionsAnti-Infective AgentsAntimicrobial Cationic PeptidesAntiviral AgentsBlood ProteinsmyticinPeptidespolypeptide CProtein IsoformsSolutions

Identifiers

PMID23880927
PMCPMC3736426
OpenAlexW2168938047

What OpenQuestion holds

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LicenceCC BY
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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.