Antibacterial Efficacy and Mechanisms of Action of a Novel Beta-Defensin from Snakehead Murrel, Channa Striata

Overview

Journal Probiotics Antimicrob Proteins

Publisher Springer

Specialties Infectious Diseases
Microbiology
Nutritional Sciences
Pharmacology

Date 2024 Jul 4

PMID 38963507

Authors

P P Athira

V V Anooja

M V Anju

K Archana

S Neelima

S Muhammed Musthafa

I S Bright Singh

Rosamma Philip

Affiliations

Soon will be listed here.

Abstract

Beta-defensins, identified from fishes, constitute a crucial category of antimicrobial peptides important in combating bacterial fish pathogens. The present investigation centers on the molecular and functional characterization of CsDef, a 63-amino acid beta-defensin antimicrobial peptide derived from snakehead murrel (Channa striata). The physicochemical attributes of CsDef align with the distinctive characteristics observed in AMPs. CsDef was recombinantly produced, and the recombinant peptide, rCsDef, exhibited notable antibacterial efficacy against bacterial fish pathogens with an MIC of 16 μM for V. proteolyticus. A. hydrophila exhibited 91% inhibition, E. tarda 92%, and V. harveyi 53% at 32 μM of rCsDef. The rCsDef exhibited a multifaceted mechanism of action against bacteria, i.e., through membrane depolarization, membrane permeabilization, and generation of ROS. The rCsDef was non-hemolytic to hRBCs and non-cytotoxic to normal mammalian cell line CHO-K1. However, it exhibited anticancer properties in MCF-7. rCsDef demonstrated notable stability with respect to pH, temperature, salt, metal ions, and proteases. These findings suggest it is a potential candidate molecule for prospective applications in aquaculture.

References

Hancock R, Scott M . The role of antimicrobial peptides in animal defenses. Proc Natl Acad Sci U S A. 2000; 97(16):8856-61. PMC: 34023. DOI: 10.1073/pnas.97.16.8856. View

Zasloff M . Antimicrobial peptides of multicellular organisms. Nature. 2002; 415(6870):389-95. DOI: 10.1038/415389a. View

Noga E, Ullal A, Corrales J, Fernandes J . Application of antimicrobial polypeptide host defenses to aquaculture: Exploitation of downregulation and upregulation responses. Comp Biochem Physiol Part D Genomics Proteomics. 2010; 6(1):44-54. DOI: 10.1016/j.cbd.2010.06.001. View

Masso-Silva J, Diamond G . Antimicrobial peptides from fish. Pharmaceuticals (Basel). 2014; 7(3):265-310. PMC: 3978493. DOI: 10.3390/ph7030265. View

Jenssen H, Hamill P, Hancock R . Peptide antimicrobial agents. Clin Microbiol Rev. 2006; 19(3):491-511. PMC: 1539102. DOI: 10.1128/CMR.00056-05. View

Das S, Pradhan C, Devika Pillai . β-Defensin: An adroit saviour in teleosts. Fish Shellfish Immunol. 2022; 123:417-430. DOI: 10.1016/j.fsi.2022.03.017. View

Zhao J, Zhou L, Jin J, Zhao Z, Lan J, Zhang Y . Antimicrobial activity-specific to Gram-negative bacteria and immune modulation-mediated NF-kappaB and Sp1 of a medaka beta-defensin. Dev Comp Immunol. 2008; 33(4):624-37. DOI: 10.1016/j.dci.2008.11.006. View

Jin J, Zhou L, Wang Y, Li Z, Zhao J, Zhang Q . Antibacterial and antiviral roles of a fish β-defensin expressed both in pituitary and testis. PLoS One. 2010; 5(12):e12883. PMC: 3004800. DOI: 10.1371/journal.pone.0012883. View

Cuesta A, Meseguer J, Esteban M . Molecular and functional characterization of the gilthead seabream β-defensin demonstrate its chemotactic and antimicrobial activity. Mol Immunol. 2011; 48(12-13):1432-8. DOI: 10.1016/j.molimm.2011.03.022. View

10.

Ruangsri J, Kitani Y, Kiron V, Lokesh J, Brinchmann M, Karlsen B . A novel beta-defensin antimicrobial peptide in Atlantic cod with stimulatory effect on phagocytic activity. PLoS One. 2013; 8(4):e62302. PMC: 3636224. DOI: 10.1371/journal.pone.0062302. View

11.

Chen Y, Zhao H, Zhang X, Luo H, Xue X, Li Z . Identification, expression and bioactivity of Paramisgurnus dabryanus β-defensin that might be involved in immune defense against bacterial infection. Fish Shellfish Immunol. 2013; 35(2):399-406. DOI: 10.1016/j.fsi.2013.04.049. View

12.

Dong J, Wu F, Ye X, Sun C, Tian Y, Lu M . Β-defensin in Nile tilapia (Oreochromis niloticus): Sequence, tissue expression, and anti-bacterial activity of synthetic peptides. Gene. 2015; 566(1):23-31. DOI: 10.1016/j.gene.2015.04.025. View

13.

Zhu J, Wang H, Wang J, Wang X, Peng S, Geng Y . Identification and characterization of a β-defensin gene involved in the immune defense response of channel catfish, Ictalurus punctatus. Mol Immunol. 2017; 85:256-264. DOI: 10.1016/j.molimm.2017.03.009. View

14.

Yang K, Hou B, Ren F, Zhou H, Zhao T . Characterization of grass carp () beta-defensin 1: implications for its role in inflammation control. Biosci Biotechnol Biochem. 2018; 83(1):87-94. DOI: 10.1080/09168451.2018.1519386. View

15.

Thakur N, Qureshi A, Kumar M . AVPpred: collection and prediction of highly effective antiviral peptides. Nucleic Acids Res. 2012; 40(Web Server issue):W199-204. PMC: 3394244. DOI: 10.1093/nar/gks450. View

16.

Agrawal P, Bhagat D, Mahalwal M, Sharma N, Raghava G . AntiCP 2.0: an updated model for predicting anticancer peptides. Brief Bioinform. 2020; 22(3). DOI: 10.1093/bib/bbaa153. View

17.

Win T, Malik A, Prachayasittikul V, Wikberg J, Nantasenamat C, Shoombuatong W . HemoPred: a web server for predicting the hemolytic activity of peptides. Future Med Chem. 2017; 9(3):275-291. DOI: 10.4155/fmc-2016-0188. View

18.

Onuma Y, Satake M, Ukena T, Roux J, Chanteau S, Rasolofonirina N . Identification of putative palytoxin as the cause of clupeotoxism. Toxicon. 1999; 37(1):55-65. DOI: 10.1016/s0041-0101(98)00133-0. View

19.

Park C, Yi K, Matsuzaki K, Kim M, Kim S . Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc Natl Acad Sci U S A. 2000; 97(15):8245-50. PMC: 26932. DOI: 10.1073/pnas.150518097. View

20.

Boulos L, Prevost M, Barbeau B, Coallier J, Desjardins R . LIVE/DEAD BacLight : application of a new rapid staining method for direct enumeration of viable and total bacteria in drinking water. J Microbiol Methods. 1999; 37(1):77-86. DOI: 10.1016/s0167-7012(99)00048-2. View