Chicken cathelicidin-2 promotes IL-1β secretion via the NLRP3 inflammasome pathway and serine proteases activity in LPS-primed murine neutrophils

Peng, Lianci; Lü, Yi; Tian, Hongliang; Jia, Kaixiang; Qi, Tao; Li, Gang; Wan, Chao; Ye, Chao; Veldhuizen, Edwin J.A.; Chen, Hongwei; Fang, Rendong

doi:10.1016/j.dci.2022.104377

Cited by 4 publications

(3 citation statements)

References 32 publications

(41 reference statements)

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“…Viral infection can be resisted in many ways by antimicrobial peptides, drugs, and other small-molecule inhibitors. For example, the antimicrobial peptide CATH-2 has been reported to modulate the inflammatory response by regulating the secretion of inflammatory cytokines and activation of the NLRP3 inflammasome, resulting in protection against IAV infection (Coorens et al, 2017 ; Peng et al, 2022 ). A defense peptide called An1a restricts dengue and Zika virus infection by inhibiting the viral NS2B-NS3 protease (Ji et al, 2019 ).…”

Section: Discussionmentioning

confidence: 99%

Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection

Guo

Tan

et al. 2023

Front. Microbiol.

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Herpes simplex virus 1 (HSV-1) is a widely distributed virus. HSV-1 is a growing public health concern due to the emergence of drug-resistant strains and the current lack of a clinically specific drug for treatment. In recent years, increasing attention has been paid to the development of peptide antivirals. Natural host-defense peptides which have uniquely evolved to protect the host have been reported to have antiviral properties. Cathelicidins are a family of multi-functional antimicrobial peptides found in almost all vertebrate species and play a vital role in the immune system. In this study, we demonstrated the anti-HSV-1 effect of an antiviral peptide named WL-1 derived from human cathelicidin. We found that WL-1 inhibited HSV-1 infection in epithelial and neuronal cells. Furthermore, the administration of WL-1 improved the survival rate and reduced viral load and inflammation during HSV-1 infection via ocular scarification. Moreover, facial nerve dysfunction, involving the abnormal blink reflex, nose position, and vibrissae movement, and pathological injury were prevented when HSV-1 ear inoculation-infected mice were treated with WL-1. Together, our findings demonstrate that WL-1 may be a potential novel antiviral agent against HSV-1 infection-induced facial palsy.

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Section: Discussionmentioning

confidence: 99%

Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection

Guo

Tan

et al. 2023

Front. Microbiol.

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“…Similarly, activation of downstream signaling pathways of TLR such as NF-κB and ERK was also inhibited by CATH-1. Notably, CATH-1 dose-dependently upregulated the secretion of IL-1β when CATH-1 was incubated with cells at post-infection, which is similar to CATH-2 which promotes NLRP3 inflammasome activation, leading to IL-1β secretion [ 23 , 37 ], suggesting the possibility that CATH-1 serves as a second signal activating inflammasome. These results demonstrate that CATH-1 regulates pro-inflammatory cytokine expression by direct bactericidal effect and modulating TLR2/4-mediated activation of NF-κB and ERK1/2 pathways.…”

Section: Discussionmentioning

confidence: 99%

The protective role of chicken cathelicidin-1 against Streptococcus suis serotype 2 in vitro and in vivo

Lu,

Xiang,

et al. 2023

Vet Res

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Streptococcus suis serotype 2 (SS2) is an important zoonotic pathogen with the characteristics of high mortality and morbidity, which brings great challenges to prevent and control epidemic disease in the swine industry. Cathelicidins (CATH) are antimicrobial peptides with antimicrobial and immunomodulatory activities. In this study, bactericidal and anti-inflammatory effects of chicken cathelicidin-1 (CATH-1) were investigated in vitro and in vivo against SS2 infection. The results show that CATH-1 exhibited a better bactericidal effect compared to other species’ cathelicidins including chickens (CATH-2, -3, and -B1), mice (CRAMP) and pigs (PMAP-36 and PR-39), which rapidly killed bacteria in 20 min by a time-killing curve assay. Furthermore, CATH-1 destroyed the bacterial morphology and affected bacterial ultrastructure as observed under electron microscopy. Moreover, CATH-1 antibacterial activity in vivo shows that CATH-1 increased survival rate of SS2-infected mice by 60% and significantly reduced the bacterial load in the lungs, liver, spleen, blood, and peritoneal lavage as well as the release of SS2-induced inflammatory cytokines including IL-1α, IL-1β, IL-12, and IL-18. Importantly, CATH-1 did not show severe histopathological changes in mice. Further studies on the mechanism of anti-inflammatory activity show that CATH-1 not only reduced the inflammatory response through direct neutralization, but also by regulating the TLR2/4/NF-κB/ERK pathway. This study provides a scientific basis for the research and development of antimicrobial peptides as new antimicrobial agents.

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“…Cationic host defense peptides known as antimicrobial peptides (AMPs) are key components of the innate immune system with immunomodulatory and antimicrobial activities (Peng et al, 2022). AMPs are widely expressed in different species, such as microorganisms, plants, insects, and mammals, which show broad-spectrum antimicrobial activity against bacteria, fungi, viruses, and parasites (Jenssen et al, 2006;Choi et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Synergistic Antimicrobial Effect of Antimicrobial Peptides CATH-1, CATH-3, and PMAP-36 With Erythromycin Against Bacterial Pathogens

et al. 2022

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With the increasing bacterial resistance to traditional antibiotics, there is an urgent need for the development of alternative drugs or adjuvants of antibiotics to enhance antibacterial efficiency. The combination of antimicrobial peptides (AMPs) and traditional antibiotics is a potential alternative to enhance antibacterial efficiency. In this study, we investigated the synergistic bactericidal effect of AMPs, including chicken (CATH-1,−2,−3, and -B1), mice (CRAMP), and porcine (PMAP-36 and PR-39) in combination with conventional antibiotics containing ampicillin, tetracycline, gentamicin, and erythromycin against Staphylococcus aureus, Salmonella enteritidis, and Escherichia coli. The results showed that the minimum bactericidal concentration (MBC) of CATH-1,−3 and PMAP-36 was lower than 10 μM, indicating that these three AMPs had good bacterial activity against S. aureus, S. enteritidis, and E. coli. Then, the synergistic antibacterial activity of AMPs and antibiotics combination was determined by the fractional bactericidal concentration index (FBCI). The results showed that the FBCI of AMPs (CATH-1,−3 and PMAP-36) and erythromycin was lower than 0.5 against bacterial pathogens, demonstrating that they had a synergistic bactericidal effect. Furthermore, the time-killing kinetics of AMPs (CATH-1,−3 and PMAP-36) in combination with erythromycin showed that they had a continuous killing effect on bacteria within 3 h. Notably, the combination showed lower hemolytic activity and cytotoxicity to mammal cells compared to erythromycin and peptide alone treatment. In addition, the antibacterial mechanism of CATH-1 and erythromycin combination against E. coli was studied. The results of the scanning electron microscope showed that CATH-1 enhanced the antibacterial activity of erythromycin by increasing the permeability of bacterial cell membrane. Moreover, the results of bacterial migration movement showed that the combination of CATH-1 and erythromycin significantly inhibits the migration of E. coli. Finally, drug resistance analysis was performed and the results showed that CATH-1 delayed the emergence of E. coli resistance to erythromycin. In conclusion, the combination of CATH-1 and erythromycin has synergistic antibacterial activity and reduces the emergence of bacterial drug resistance. Our study provides valuable information to develop AMPs as potential substitutes or adjuvants for traditional antibiotics.

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Chicken cathelicidin-2 promotes IL-1β secretion via the NLRP3 inflammasome pathway and serine proteases activity in LPS-primed murine neutrophils

Cited by 4 publications

References 32 publications

Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection

Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection

The protective role of chicken cathelicidin-1 against Streptococcus suis serotype 2 in vitro and in vivo

Synergistic Antimicrobial Effect of Antimicrobial Peptides CATH-1, CATH-3, and PMAP-36 With Erythromycin Against Bacterial Pathogens

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