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New Potent Membrane-Targeting Antibacterial Peptides from Viral Capsid Proteins

Identifieur interne : 000733 ( Main/Merge ); précédent : 000732; suivant : 000734

New Potent Membrane-Targeting Antibacterial Peptides from Viral Capsid Proteins

Auteurs : Susana A. Dias [Portugal] ; João M. Freire [Portugal, France] ; Clara Pérez-Peinado [Espagne] ; Marco M. Domingues [Portugal] ; Diana Gaspar [Portugal] ; Nuno Vale [Portugal] ; Paula Gomes [Portugal] ; David Andreu [Espagne] ; S Nia T. Henriques [Australie] ; Miguel A. R. B. Castanho [Portugal] ; Ana S. Veiga [Portugal]

Source :

RBID : PMC:5415599

Abstract

The increasing prevalence of multidrug-resistant bacteria urges the development of new antibacterial agents. With a broad spectrum activity, antimicrobial peptides have been considered potential antibacterial drug leads. Using bioinformatic tools we have previously shown that viral structural proteins are a rich source for new bioactive peptide sequences, namely antimicrobial and cell-penetrating peptides. Here, we test the efficacy and mechanism of action of the most promising peptides among those previously identified against both Gram-positive and Gram-negative bacteria. Two cell-penetrating peptides, vCPP 0769 and vCPP 2319, have high antibacterial activity against Staphylococcus aureus, MRSA, Escherichia coli, and Pseudomonas aeruginosa, being thus multifunctional. The antibacterial mechanism of action of the two most active viral protein-derived peptides, vAMP 059 and vCPP 2319, was studied in detail. Both peptides act on both Gram-positive S. aureus and Gram-negative P. aeruginosa, with bacterial cell death occurring within minutes. Also, these peptides cause bacterial membrane permeabilization and damage of the bacterial envelope of P. aeruginosa cells. Overall, the results show that structural viral proteins are an abundant source for membrane-active peptides sequences with strong antibacterial properties.


Url:
DOI: 10.3389/fmicb.2017.00775
PubMed: 28522994
PubMed Central: 5415599

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PMC:5415599

Le document en format XML

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<name sortKey="Gomes, Paula" sort="Gomes, Paula" uniqKey="Gomes P" first="Paula" last="Gomes">Paula Gomes</name>
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<name sortKey="Castanho, Miguel A R B" sort="Castanho, Miguel A R B" uniqKey="Castanho M" first="Miguel A. R. B." last="Castanho">Miguel A. R. B. Castanho</name>
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<p>The increasing prevalence of multidrug-resistant bacteria urges the development of new antibacterial agents. With a broad spectrum activity, antimicrobial peptides have been considered potential antibacterial drug leads. Using bioinformatic tools we have previously shown that viral structural proteins are a rich source for new bioactive peptide sequences, namely antimicrobial and cell-penetrating peptides. Here, we test the efficacy and mechanism of action of the most promising peptides among those previously identified against both Gram-positive and Gram-negative bacteria. Two cell-penetrating peptides, vCPP 0769 and vCPP 2319, have high antibacterial activity against
<italic>Staphylococcus aureus</italic>
, MRSA,
<italic>Escherichia coli</italic>
, and
<italic>Pseudomonas aeruginosa</italic>
, being thus multifunctional. The antibacterial mechanism of action of the two most active viral protein-derived peptides, vAMP 059 and vCPP 2319, was studied in detail. Both peptides act on both Gram-positive
<italic>S. aureus</italic>
and Gram-negative
<italic>P. aeruginosa</italic>
, with bacterial cell death occurring within minutes. Also, these peptides cause bacterial membrane permeabilization and damage of the bacterial envelope of
<italic>P. aeruginosa</italic>
cells. Overall, the results show that structural viral proteins are an abundant source for membrane-active peptides sequences with strong antibacterial properties.</p>
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<name sortKey="Yeaman, M R" uniqKey="Yeaman M">M. R. Yeaman</name>
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<author>
<name sortKey="Yount, N Y" uniqKey="Yount N">N. Y. Yount</name>
</author>
</analytic>
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<analytic>
<author>
<name sortKey="Zasloff, M" uniqKey="Zasloff M">M. Zasloff</name>
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<analytic>
<author>
<name sortKey="Zhu, W L" uniqKey="Zhu W">W. L. Zhu</name>
</author>
<author>
<name sortKey="Lan, H" uniqKey="Lan H">H. Lan</name>
</author>
<author>
<name sortKey="Park, I S" uniqKey="Park I">I. S. Park</name>
</author>
<author>
<name sortKey="Kim, J" uniqKey="Kim J">J. Kim</name>
</author>
<author>
<name sortKey="Jin, H Z" uniqKey="Jin H">H. Z. Jin</name>
</author>
<author>
<name sortKey="Hahm, K S" uniqKey="Hahm K">K. S. Hahm</name>
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