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Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides

Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel AMP...

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Autores principales: Krämer, Jonas, Lüddecke, Tim, Marner, Michael, Maiworm, Elena, Eichberg, Johanna, Hardes, Kornelia, Schäberle, Till F., Vilcinskas, Andreas, Predel, Reinhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778599/
https://www.ncbi.nlm.nih.gov/pubmed/35051034
http://dx.doi.org/10.3390/toxins14010058
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author Krämer, Jonas
Lüddecke, Tim
Marner, Michael
Maiworm, Elena
Eichberg, Johanna
Hardes, Kornelia
Schäberle, Till F.
Vilcinskas, Andreas
Predel, Reinhard
author_facet Krämer, Jonas
Lüddecke, Tim
Marner, Michael
Maiworm, Elena
Eichberg, Johanna
Hardes, Kornelia
Schäberle, Till F.
Vilcinskas, Andreas
Predel, Reinhard
author_sort Krämer, Jonas
collection PubMed
description Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel AMPs are arthropod venoms, especially those of hitherto neglected groups such as pseudoscorpions. In this study, we describe for the first time pharmacological effects of AMPs discovered in pseudoscorpion venom. We examined the antimicrobial, cytotoxic, and insecticidal activity of full-length Checacin1, a major component of the Chelifer cancroides venom, and three truncated forms of this peptide. The antimicrobial tests revealed a potent inhibitory activity of Checacin1 against several bacteria and fungi, including methicillin resistant Staphylococcus aureus (MRSA) and even Gram-negative pathogens. All peptides reduced survival rates of aphids, with Checacin1 and the C-terminally truncated Checacin1(1−21) exhibiting effects comparable to Spinosad, a commercially used pesticide. Cytotoxic effects on mammalian cells were observed mainly for the full-length Checacin1. All tested peptides might be potential candidates for developing lead structures for aphid pest treatment. However, as these peptides were not yet tested on other insects, aphid specificity has not been proven. The N- and C-terminal fragments of Checacin1 are less potent against aphids but exhibit no cytotoxicity on mammalian cells at the tested concentration of 100 µM.
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spelling pubmed-87785992022-01-22 Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides Krämer, Jonas Lüddecke, Tim Marner, Michael Maiworm, Elena Eichberg, Johanna Hardes, Kornelia Schäberle, Till F. Vilcinskas, Andreas Predel, Reinhard Toxins (Basel) Article Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel AMPs are arthropod venoms, especially those of hitherto neglected groups such as pseudoscorpions. In this study, we describe for the first time pharmacological effects of AMPs discovered in pseudoscorpion venom. We examined the antimicrobial, cytotoxic, and insecticidal activity of full-length Checacin1, a major component of the Chelifer cancroides venom, and three truncated forms of this peptide. The antimicrobial tests revealed a potent inhibitory activity of Checacin1 against several bacteria and fungi, including methicillin resistant Staphylococcus aureus (MRSA) and even Gram-negative pathogens. All peptides reduced survival rates of aphids, with Checacin1 and the C-terminally truncated Checacin1(1−21) exhibiting effects comparable to Spinosad, a commercially used pesticide. Cytotoxic effects on mammalian cells were observed mainly for the full-length Checacin1. All tested peptides might be potential candidates for developing lead structures for aphid pest treatment. However, as these peptides were not yet tested on other insects, aphid specificity has not been proven. The N- and C-terminal fragments of Checacin1 are less potent against aphids but exhibit no cytotoxicity on mammalian cells at the tested concentration of 100 µM. MDPI 2022-01-14 /pmc/articles/PMC8778599/ /pubmed/35051034 http://dx.doi.org/10.3390/toxins14010058 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Krämer, Jonas
Lüddecke, Tim
Marner, Michael
Maiworm, Elena
Eichberg, Johanna
Hardes, Kornelia
Schäberle, Till F.
Vilcinskas, Andreas
Predel, Reinhard
Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title_full Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title_fullStr Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title_full_unstemmed Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title_short Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides
title_sort antimicrobial, insecticidal and cytotoxic activity of linear venom peptides from the pseudoscorpion chelifer cancroides
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778599/
https://www.ncbi.nlm.nih.gov/pubmed/35051034
http://dx.doi.org/10.3390/toxins14010058
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