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Tissue Specificity in Social Context-Dependent lysozyme Expression in Bumblebees
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Antibacterial Peptides

Université Aix-Marseille, Institut de Neurophysiopathologie (INP), UMR 7051, 13005 Marseille, France
Antibiotics 2020, 9(4), 142;
Received: 24 March 2020 / Accepted: 25 March 2020 / Published: 26 March 2020
(This article belongs to the Special Issue Antibacterial Peptides)
As natural host defense compounds produced by numerous prokaryotic and eukaryotic life forms, antimicrobial peptides (AMPs) are now emerging as solid candidate chemotherapeutic drugs to fight against the various types of pathogenic Gram-positive and Gram-negative bacteria, especially those resistant to current antibiotics. This special issue of ‘Antibiotics’ has been focused on the various aspects of such AMPs, from their discovery to the structural and functional characterization thereof. The authors of articles published in this special issue (10 articles, including a review article) are thanked for their important contributions to this essential field of applied research, by allowing a more ‘in-depth’ knowledge on the AMPs.
A first original article by Lattorff deals with the social environment-dependency of two lysozyme genes expression in bumblebees (lysozyme being part of the antimicrobial response of these insects), as well as its tissue specificity [1]. Boix-Lemonche and collaborators [2] developed an interesting fast fluorescence-based microplate assay to examine the effects of AMPs on membranes of whole Gram-positive bacteria. Apart from providing a tool to investigate the mode of action of antibacterials on Gram-positive bacteria, this approach might be particularly useful to screen novel AMPs. Other key studies by Flórez-Castillo [3], Della Pelle [4], Paquette [5], and their collaborators have reported on the structural properties, molecular docking simulation experiments, and/or antibacterial potential of specific antimicrobials, i.e., Ib-M6, Antarctic fish (transcriptome-derived) Trematocine, and E. coli antimicrobial molecule, respectively. The data presented are of great interest in the field and may help the design of potent candidate AMPs. Shelenkov and coworkers [6], by performing a computer-based search for potential AMPs in 1267 plant transcriptomes (50–150 peptides were highlighted in each transcriptome), also provided us with a large number of candidate AMPs to examine. By peptide/protein engineering, some ‘optimized’ chemical structures of AMPs can be selected and chemically produced, an approach used by Liscano et al. with Alyteserin 1c [7] and Woodburn et al. [8]. Such antibacterial compounds were shown to possess distinct potencies and/or selectivities toward Gram-positive and Gram-negative bacteria and may lead to newly designed AMP(s) with potent activity on antibiotic-resistant bacterial strain(s) [8]. Importantly, Cheng and collaborators [9] found that a scorpion venom defensin (BmKDfsin3, a host defense antimicrobial peptide) was able to dose-dependently inhibit Hepatitis C viral infection of target cells via suppression of the p38 mitogen-activated protein kinase (MAPK) activation. Finally, an outstanding up-to-date review article by Gray and Wenzel [10] on the marketed cyclic lipopeptide antibiotic Daptomycin is provided in this special issue on ‘Antimicrobial peptides’. I strongly believe that the scientists and clinicians working in the field will find the special issue of particular interest and a real source of inspiration.

Conflicts of Interest

The author declares no conflict of interest.


  1. Lattorff, H.M. Tissue specificity in social context-dependent lysozyme expression in bumblebees. Antibiotics 2020, 9, 130. [Google Scholar] [CrossRef][Green Version]
  2. Boix-Lemonche, G.; Lekka, M.; Skerlavaj, B. A rapid fluorescence-based microplate assay to investigate the interaction of membrane active antimicrobial peptides with whole Gram-positive bacteria. Antibiotics 2020, 9, 92. [Google Scholar] [CrossRef] [PubMed][Green Version]
  3. Flórez-Castillo, J.M.; Rondón-Villareal, P.; Ropero-Vega, J.L.; Mendoza-Espinel, S.Y.; Moreno-Amézquita, J.A.; Méndez-Jaimes, K.D.; Farfán-García, A.E.; Gómez-Rangel, S.Y.; Gómez-Duarte, O.G. Ib-M6 Antimicrobial peptide: Antibacterial activity against clinical isolates of Escherichia coli and molecular docking. Antibiotics 2020, 9, 79. [Google Scholar] [CrossRef] [PubMed][Green Version]
  4. Della Pelle, G.; Pera, G.; Belardinelli, M.C.; Gerdol, M.; Felli, M.; Crognale, S.; Scapigliati, G.; Ceccacci, F.; Buonocore, F.; Porcelli, F. Trematocine, a novel antimicrobial peptide from the antarctic fish Trematomus bernacchii: Identification and biological activity. Antibiotics 2020, 9, 66. [Google Scholar] [CrossRef] [PubMed][Green Version]
  5. Paquette, S.J.; Reuter, T. Properties of an antimicrobial molecule produced by an Escherichia coli champion. Antibiotics 2020, 9, 6. [Google Scholar] [CrossRef] [PubMed][Green Version]
  6. Shelenkov, A.; Slavokhotova, A.; Odintsova, T. Predicting antimicrobial and other cysteine-rich peptides in 1267 plant transcriptomes. Antibiotics 2020, 9, 60. [Google Scholar] [CrossRef] [PubMed][Green Version]
  7. Liscano, Y.; Salamanca, C.H.; Vargas, L.; Cantor, S.; Laverde-Rojas, V.; Oñate-Garzón, J. Increases in hydrophilicity and charge on the polar face of Alyteserin 1c helix change its selectivity towards Gram-positive bacteria. Antibiotics 2019, 8, 238. [Google Scholar] [CrossRef] [PubMed][Green Version]
  8. Woodburn, K.W.; Jaynes, J.; Clemens, L.E. Designed antimicrobial peptides for topical treatment of antibiotic resistant Acne vulgaris. Antibiotics 2020, 9, 23. [Google Scholar] [CrossRef] [PubMed][Green Version]
  9. Cheng, Y.; Sun, F.; Li, S.; Gao, M.; Wang, L.; Sarhan, M.; Abdel-Rahman, M.A.; Li, W.; Kwok, H.F.; Wu, Y.; et al. Inhibitory activity of a scorpion defensin BmKDfsin3 against Hepatitis C virus. Antibiotics 2020, 9, 33. [Google Scholar] [CrossRef] [PubMed][Green Version]
  10. Gray, D.A.; Wenzel, M. More than a pore: A current perspective on the in vivo mode of action of the lipopeptide antibiotic Daptomycin. Antibiotics 2020, 9, 17. [Google Scholar] [CrossRef] [PubMed][Green Version]

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Sabatier, J.-M. Antibacterial Peptides. Antibiotics 2020, 9, 142.

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Sabatier J-M. Antibacterial Peptides. Antibiotics. 2020; 9(4):142.

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Sabatier, Jean-Marc. 2020. "Antibacterial Peptides" Antibiotics 9, no. 4: 142.

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