The immunomodulatory function of the porcine β-defensin 129: Alleviate inflammatory response induced by LPS in IPEC-J2 cells

Xie, Kunhong; Su, Guoqi; Chen, Shuai; Yu, Bing; Huang, Zhiqing; Yu, Jie; Zheng, Ping; Luo, Yuheng; Yan, Hui; Li, Hua; He, Jun

doi:10.1016/j.ijbiomac.2021.07.194

Cited by 12 publications

(8 citation statements)

References 38 publications

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“…pBD2 could inhibit E. coli and S. aureus , as well as some clinically isolated multidrug-resistant bacteria [ 9 ]. pBD2 has the strongest antimicrobial activity among the porcine beta defensins (pBDs) detected, including pBD1, pBD2, pBD114, and pBD129 [ 9 , 10 , 11 , 12 ]. In addition, pBD2 could alleviate the inflammatory response induced by exogenous stimulation in mice [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Transcriptome Analysis Reveals the Multiple Functions of pBD2 in IPEC-J2 Cells against E. coli

Lian

Lin

Zhan

et al. 2022

IJMS

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Defensins play an important role in fighting bacteria, and are a good candidate for bactericidal agents. However, the function and mechanism of defensins in regulating host responses against bacteria is unclear. In this study, transcriptome analysis was used to study the comprehensive functions of pBD2 in IPEC-J2 cells against E. coli. In total, 230 differentially expressed genes (DEGs) were identified in IPEC-J2 cells between the control and E. coli groups, and were found by KEGG analysis to be involved in many signaling pathways related to immunity. Furthermore, 812 DEGs were observed between E. coli and E. coli +pBD2 groups, involved in the ribosome, oxidative phosphorylation, and certain disease pathways. Among these, 94 overlapping DEGs were in the two DEG groups, and 85 DEGs were reverse expression, which is involved in microRNA in cancer, while PTEN and CDC6 were key genes according to PPI net analysis. The results of qRT-PCR verified those of RNA-seq. The results indicated that pBD2 plays an important role against E. coli by acting on the genes related to immune response, cell cycle, ribosomes, oxidative phosphorylation, etc. The results provide new insights into the potential function and mechanism of pBD2 against E. coli. Meanwhile, this study provides a certain theoretical basis for research and the development of novel peptide drugs.

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Section: Introductionmentioning

confidence: 99%

Transcriptome Analysis Reveals the Multiple Functions of pBD2 in IPEC-J2 Cells against E. coli

Lian

Lin

Zhan

et al. 2022

IJMS

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“…β-defensins generally display a broad range of antibacterial activities. In this study, MIC assays were used to evaluate the antibacterial activities of the recombinant pBD129 protein against E. coli DH5α and Streptococcus dysgalactiae ATCC12394 [ 25 ]. As illustrated in Figure 2 , the recombinant pBD129 protein exhibits dose-dependent antimicrobial activity against E. coli DH5α and S. dysgalactiae , and MICs of 35 μg/mL for both vectors.…”

Section: Resultsmentioning

confidence: 99%

“…A high expression of β-defensin 129 (DEFB129) was first reported in porcine epididymis and small intestine in 2006 [ 23 ]. Previous studies have found that porcine β-defensin 129 (pBD129) attenuates lipopolysaccharide (LPS)-induced inflammatory responses by decreasing the serum concentrations of inflammatory cytokines [ 24 , 25 ]. In addition, DEFB129 was considered to have high antibacterial and anti-inflammatory activity in the semen of non-obstructive azoospermic men [ 26 ].…”

Section: Introductionmentioning

confidence: 99%

Involvement of Porcine β-Defensin 129 in Sperm Capacitation and Rescue of Poor Sperm in Genital Tract Infection

Zeng

Wang

et al. 2022

IJMS

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In mammals, β-defensins have been reported to play pivotal roles in sperm protection and fertilization. However, the function and mechanism of porcine β-defensin 129 (pBD129) in the sperm remain unclear. Here, we demonstrate that pBD129 is a glycosylated protein and broadly exists in accessory sex glands and coats the sperm surface. We inhibited the pBD129 protein on the sperm surface with an anti-pBD129 antibody and found that sperm motility was not significantly affected; however, sperm acrosome integrity and tyrosine phosphorylation levels increased significantly with time (p < 0.05) during capacitation. These changes were accompanied by an increase in sperm Ca2+ influx, resulting in a significantly reduced in vitro fertilization cleavage rate (p < 0.05). Further investigation revealed that treatment with recombinant pBD129 markedly restored the sperm motility in semen contaminated with Escherichia coli. The results suggest that pBD129 is not only associated with poor sperm motility after genital tract infection but can also protect the spermatozoa from premature capacitation, which may be beneficial for semen preservation.

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“…32 DEFB 129 and 118 were initially reported by Kao, et al They performed a genome-wide search using ORFeome-based peptide databases of airway epithelial cells, which showed six novel β-defensins, including those. 33 DEFB129 mRNA is known to be expressed in human testis specimens, whereas Xie, et al found that they are highly expressed in various segments of the epididymis in pigs, 34 and another study showed that porcine DEFB129 protein decreased bacterial endotoxin-induced inflammation and apoptosis in intestinal epithelial cells. 35 The DEFB 118 gene is located on chromosome 20q11, and its mRNA expression can be detected in pancreas and testis specimens.…”

Section: Discussionmentioning

confidence: 99%

Expression of anti-fungal peptide, β-defensin 118 in oral fibroblasts induced by C. albicans β-glucan-containing particles

et al. 2022

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Expression of anti-fungal peptide, b-defensin 118 in oral fibroblasts induced by C. albicans b-glucancontaining particles Objective: Although oral fibroblasts are thought to have the potential to enhance host defenses against Candida albicans, it is unknown whether they are able to recognize Candida cell components to increase the expression of antifungal peptides, such as defensin factors, against Candida infection. Methodology: We performed expression profiles of defensin genes induced by heat-killed C. albicans in oral immortalized fibroblasts (GT1) using cDNA microarray analysis. From those results, quantitative RT-PCR was used to examine the effects of Candida b-glucan-containing particles (b-GPs) on b-Defensin 118 (DEFB 118) expression in oral mucosal cells. Furthermore, the antifungal activities of recombinant DEFB 118 against C. albicans and C. glabrata were investigated using fungicidal assays. Results: Microarray analysis showed that DEFB118, b-Defensin 129 (DEFB129), and a-Defensin 1 (DEFA1) genes were induced by heat-killed C. albicans and that their mRNA expressions were also significantly increased by live as well as heatkilled C. albicans. Next, we focused on DEFB118, and found that GT1, primary fibroblasts, and RT7 (oral immortalized keratinocytes) constitutively expressed DEFB118 mRNA expression in RT-PCR. Furthermore, C. albicans b-GPs significantly increased the expression of DEFB118 mRNA in GT1 and primary fibroblasts. Although DEFB118 mRNA expression in RT7 was significantly induced by both live and heat-killed C. albicans, C. albicans b-GPs failed to have an effect on that expression. Finally, recombinant DEFB118 significantly decreased the survival of both strains of C. albicans in a dosedependent manner, whereas no effects were seen for both C. glabrata strains. Conclusion: DEFB118, induced by C. albicans b-GPs from oral fibroblasts, may play an important role in oral immune responses against C. albicans infection.

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The immunomodulatory function of the porcine β-defensin 129: Alleviate inflammatory response induced by LPS in IPEC-J2 cells

Cited by 12 publications

References 38 publications

Transcriptome Analysis Reveals the Multiple Functions of pBD2 in IPEC-J2 Cells against E. coli

Transcriptome Analysis Reveals the Multiple Functions of pBD2 in IPEC-J2 Cells against E. coli

Involvement of Porcine β-Defensin 129 in Sperm Capacitation and Rescue of Poor Sperm in Genital Tract Infection

Expression of anti-fungal peptide, β-defensin 118 in oral fibroblasts induced by C. albicans β-glucan-containing particles

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