Effective inhibition of Clostridioides difficile by the novel peptide CM-A.

Clostridioides difficile infection is the most common cause of nosocomial and antibiotic-associated diarrhea. C. difficile treatment is increasingly likely to fail, and the recurrence rate is high. Antimicrobial peptides are considered an alternative treatment for many infectious diseases, including...

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Autores principales:	Sirirak Arthithanyaroj, Surang Chankhamhaengdecha, Urai Chaisri, Ratchaneewan Aunpad, Amornrat Aroonnual
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fe207abfbfb442eaa7f132fa99f6e14b
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spelling	oai:doaj.org-article:fe207abfbfb442eaa7f132fa99f6e14b2021-12-02T20:06:17ZEffective inhibition of Clostridioides difficile by the novel peptide CM-A.1932-620310.1371/journal.pone.0257431https://doaj.org/article/fe207abfbfb442eaa7f132fa99f6e14b2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0257431https://doaj.org/toc/1932-6203Clostridioides difficile infection is the most common cause of nosocomial and antibiotic-associated diarrhea. C. difficile treatment is increasingly likely to fail, and the recurrence rate is high. Antimicrobial peptides are considered an alternative treatment for many infectious diseases, including those caused by antibiotic resistant bacteria. In the present study, we identified a CM peptide, a hybrid of cecropin A and melittin, and its derivative which possesses potent antimicrobial activity against C. difficile strain 630. CM peptide exhibited antibacterial activity with minimum inhibitory concentration of 3.906 μg/ml (2.21 μM). A modified derivative of CM, CM-A, exhibited even greater activity with a minimum inhibitory concentration of 1.953 μg/ml (1.06 μM) and a minimum bactericidal concentration of 7.8125 μg/ml (4.24 μM), which indicates that CM-A peptide is more efficient than its parent peptide. A fluorescence-activated cell sorter analysis revealed that the membrane of C. difficile 630 could be an important target for CM-A. This peptide induced high levels of cell depolarization and cell permeability on C. difficile cell membrane. Moreover, electron microscopy imaging showed that CM-A interferes with the C. difficile cell membrane. Hence, the antimicrobial peptide CM-A may represent a promising novel approach for the treatment of C. difficile infections.Sirirak ArthithanyarojSurang ChankhamhaengdechaUrai ChaisriRatchaneewan AunpadAmornrat AroonnualPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 9, p e0257431 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sirirak Arthithanyaroj Surang Chankhamhaengdecha Urai Chaisri Ratchaneewan Aunpad Amornrat Aroonnual Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
description	Clostridioides difficile infection is the most common cause of nosocomial and antibiotic-associated diarrhea. C. difficile treatment is increasingly likely to fail, and the recurrence rate is high. Antimicrobial peptides are considered an alternative treatment for many infectious diseases, including those caused by antibiotic resistant bacteria. In the present study, we identified a CM peptide, a hybrid of cecropin A and melittin, and its derivative which possesses potent antimicrobial activity against C. difficile strain 630. CM peptide exhibited antibacterial activity with minimum inhibitory concentration of 3.906 μg/ml (2.21 μM). A modified derivative of CM, CM-A, exhibited even greater activity with a minimum inhibitory concentration of 1.953 μg/ml (1.06 μM) and a minimum bactericidal concentration of 7.8125 μg/ml (4.24 μM), which indicates that CM-A peptide is more efficient than its parent peptide. A fluorescence-activated cell sorter analysis revealed that the membrane of C. difficile 630 could be an important target for CM-A. This peptide induced high levels of cell depolarization and cell permeability on C. difficile cell membrane. Moreover, electron microscopy imaging showed that CM-A interferes with the C. difficile cell membrane. Hence, the antimicrobial peptide CM-A may represent a promising novel approach for the treatment of C. difficile infections.
format	article
author	Sirirak Arthithanyaroj Surang Chankhamhaengdecha Urai Chaisri Ratchaneewan Aunpad Amornrat Aroonnual
author_facet	Sirirak Arthithanyaroj Surang Chankhamhaengdecha Urai Chaisri Ratchaneewan Aunpad Amornrat Aroonnual
author_sort	Sirirak Arthithanyaroj
title	Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
title_short	Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
title_full	Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
title_fullStr	Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
title_full_unstemmed	Effective inhibition of Clostridioides difficile by the novel peptide CM-A.
title_sort	effective inhibition of clostridioides difficile by the novel peptide cm-a.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/fe207abfbfb442eaa7f132fa99f6e14b
work_keys_str_mv	AT sirirakarthithanyaroj effectiveinhibitionofclostridioidesdifficilebythenovelpeptidecma AT surangchankhamhaengdecha effectiveinhibitionofclostridioidesdifficilebythenovelpeptidecma AT uraichaisri effectiveinhibitionofclostridioidesdifficilebythenovelpeptidecma AT ratchaneewanaunpad effectiveinhibitionofclostridioidesdifficilebythenovelpeptidecma AT amornrataroonnual effectiveinhibitionofclostridioidesdifficilebythenovelpeptidecma
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Effective inhibition of Clostridioides difficile by the novel peptide CM-A.

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