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Article

Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster

by
Bernadetta Bilska
1,
Urszula Godlewska
2,3,
Milena Damulewicz
1,
Krzysztof Murzyn
4,
Mateusz Kwitniewski
2,
Joanna Cichy
2 and
Elżbieta Pyza
1,*
1
Department of Cell Biology and Imaging, Institute of Zoology and Biomedical Research, Jagiellonian University, 30-387 Cracow, Poland
2
Department of Immunology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Cracow, Poland
3
Laboratory of Host-Microbiome Interactions, Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland
4
Department of Computational Biophysics and Bioinformatics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Cracow, Poland
*
Author to whom correspondence should be addressed.
Curr. Issues Mol. Biol. 2022, 44(3), 1169-1181; https://doi.org/10.3390/cimb44030076
Submission received: 1 January 2022 / Revised: 13 February 2022 / Accepted: 23 February 2022 / Published: 28 February 2022
(This article belongs to the Section Bioinformatics and Systems Biology)
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Abstract

Antimicrobial peptides (AMPs) are important components of innate immunity. Here, we report the antimicrobial properties of a peptide derived from the Male fertility factor kl2 (MFF-kl2) protein of Drosophila melanogaster, which was identified as a functional analog of the mammalian antibacterial chemerin-p4 peptide. The antimicrobial activity of multifunctional chemerin is mainly associated with a domain localized in the middle of the chemerin sequence, Val66-Pro85 peptide (chemerin-p4). Using bioinformatic tools, we found homologs of the chemerin-p4 peptide in the proteome of D. melanogaster. One of them is MFF-p1, which is a part of the MFF kl2 protein, encoded by the gene male fertility factor kl2 (kl-2) located on the long arm of the Y chromosome. The second detected peptide (Z-p1) is a part of the Zizimin protein belonging to DOCK family, which is involved in cellular signaling processes. After testing the antimicrobial properties of both peptides, we found that only MFF-p1 possesses these properties. Here, we demonstrate its antimicrobial potential both in vitro and in vivo after infecting D. melanogaster with bacteria. MFF-p1 strongly inhibits the viable counts of E. coli and B. subtilis after 2 h of treatment and disrupts bacterial cells. The expression of kl-2 is regulated by exposure to bacteria and by the circadian clock.
Keywords: antimicrobial proteins; p4 peptide; Drosophila melanogaster; circadian rhythms antimicrobial proteins; p4 peptide; Drosophila melanogaster; circadian rhythms

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MDPI and ACS Style

Bilska, B.; Godlewska, U.; Damulewicz, M.; Murzyn, K.; Kwitniewski, M.; Cichy, J.; Pyza, E. Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster. Curr. Issues Mol. Biol. 2022, 44, 1169-1181. https://doi.org/10.3390/cimb44030076

AMA Style

Bilska B, Godlewska U, Damulewicz M, Murzyn K, Kwitniewski M, Cichy J, Pyza E. Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster. Current Issues in Molecular Biology. 2022; 44(3):1169-1181. https://doi.org/10.3390/cimb44030076

Chicago/Turabian Style

Bilska, Bernadetta, Urszula Godlewska, Milena Damulewicz, Krzysztof Murzyn, Mateusz Kwitniewski, Joanna Cichy, and Elżbieta Pyza. 2022. "Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster" Current Issues in Molecular Biology 44, no. 3: 1169-1181. https://doi.org/10.3390/cimb44030076

APA Style

Bilska, B., Godlewska, U., Damulewicz, M., Murzyn, K., Kwitniewski, M., Cichy, J., & Pyza, E. (2022). Antimicrobial Properties of a Peptide Derived from the Male Fertility Factor kl2 Protein of Drosophila melanogaster. Current Issues in Molecular Biology, 44(3), 1169-1181. https://doi.org/10.3390/cimb44030076

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