Cecropin P1 inhibits porcine reproductive and respiratory syndrome virus by blocking attachment

Guo, Chunhe; Yu-mao, Huang; Peng, Cong; Liu, Xiaohong; Chen, Yaosheng; He, Zuyong

doi:10.1186/s12866-014-0273-8

Cited by 28 publications

(20 citation statements)

References 31 publications

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“…Cecropin P1 also shows a significant inhibitory effect on human fungal pathogen C. albicans [ 74 ]. Cecropin P1 inhibits PRRSV by blocking attachment [ 75 ]. Cecropin P1 inhibits viral particle release and attenuates virus-induced apoptosis [ 75 ].…”

Section: Insect Antimicrobial Peptidesmentioning

confidence: 99%

“…Cecropin P1 inhibits PRRSV by blocking attachment [ 75 ]. Cecropin P1 inhibits viral particle release and attenuates virus-induced apoptosis [ 75 ]. Currently, biosensors using cecropin P1 have been developed, and the peptide has been immobilized through different termini results in different functions and activities [ 76 ].…”

Section: Insect Antimicrobial Peptidesmentioning

confidence: 99%

See 1 more Smart Citation

Insect Antimicrobial Peptides, a Mini Review

Patočka

Kuča

2018

Toxins

363

271

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Antimicrobial peptides (AMPs) are crucial effectors of the innate immune system. They provide the first line of defense against a variety of pathogens. AMPs display synergistic effects with conventional antibiotics, and thus present the potential for combined therapies. Insects are extremely resistant to bacterial infections. Insect AMPs are cationic and comprise less than 100 amino acids. These insect peptides exhibit an antimicrobial effect by disrupting the microbial membrane and do not easily allow microbes to develop drug resistance. Currently, membrane mechanisms underlying the antimicrobial effects of AMPs are proposed by different modes: the barrel-stave mode, toroidal-pore, carpet, and disordered toroidal-pore are the typical modes. Positive charge quantity, hydrophobic property and the secondary structure of the peptide are important for the antibacterial activity of AMPs. At present, several structural families of AMPs from insects are known (defensins, cecropins, drosocins, attacins, diptericins, ponericins, metchnikowins, and melittin), but new AMPs are frequently discovered. We reviewed the biological effects of the major insect AMPs. This review will provide further information that facilitates the study of insect AMPs and shed some light on novel microbicides.

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Section: Insect Antimicrobial Peptidesmentioning

confidence: 99%

Section: Insect Antimicrobial Peptidesmentioning

confidence: 99%

Insect Antimicrobial Peptides, a Mini Review

Patočka

Kuča

2018

Toxins

363

271

View full text Add to dashboard Cite

show abstract

“…Porcine alveolar macrophages (PAMs) were obtained from lung lavage samples from the lungs of 3-to 8-week-old PRRSV-negative piglets (37,38) and cultured in RPMI 1640 medium supplemented with 10% heat-inactivated fetal bovine serum (FBS; PAA, Pasching, Austria), 100 U/ml penicillin, and 100 g/ml streptomycin sulfate at 37°C in 5% CO 2 . All animal experiments were approved by the Institutional Animal Care and Use Committee of Sun Yat-sen University.…”

Section: Cells and Virusesmentioning

confidence: 99%

Heparanase Upregulation Contributes to Porcine Reproductive and Respiratory Syndrome Virus Release

Guo

Zhu

Guo

et al. 2017

J Virol

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Porcine reproductive and respiratory syndrome virus (PRRSV) continues to cause substantial economic losses to the pig industry worldwide. Heparan sulfate (HS) is used by PRRSV for initial attachment to target cells. However, the role of HS in the late phase of PRRSV infection and the mechanism of virus release from host cells remain largely unknown. In this study, we showed that PRRSV infection caused a decrease in HS expression and upregulated heparanase, the only known enzyme capable of degrading HS. We subsequently demonstrated that the NF-B signaling pathway and cathepsin L protease were involved in regulation of PRRSV infectioninduced heparanase. In addition, we found that ablation of heparanase expression using small interfering RNA duplexes increased cell surface expression of HS and suppressed PRRSV replication and release, whereas overexpression of heparanase reduced HS surface expression and enhanced PRRSV replication and release. These data suggest that PRRSV activates NF-B and cathepsin L to upregulate and process heparanase, and then the active heparanase cleaves HS, resulting in viral release. Our findings provide new insight into the molecular mechanism of PRRSV egress from host cells, which might help us to further understand PRRSV pathogenesis.IMPORTANCE Porcine reproductive and respiratory syndrome virus (PRRSV) causes great economic losses each year to the pig industry worldwide. The molecular mechanism of PRRSV release from host cells largely remains a mystery. In this study, we demonstrate that PRRSV activates NF-B and cathepsin L to upregulate and process heparanase, and then the active heparanase is released to the extracellular space and exerts enzymatic activity to cleave heparan sulfate, resulting in viral release. Our findings provide new insight into the molecular mechanism of PRRSV egress from host cells, which might help us to further understand PRRSV pathogenesis.KEYWORDS PRRSV, heparan sulfate, heparanase, viral release, porcine reproductive and respiratory syndrome virus P orcine reproductive and respiratory syndrome (PRRS) has become one of the most important diseases of intensive pig production worldwide since its emergence in the late 1980s (1, 2). This disease is characterized by respiratory disease, weight loss, and poor growth performance, as well as by late-term abortions (3). The causative agent, PRRS virus (PRRSV), is a small, enveloped, positive-sense, single-stranded RNA virus of the genus Arterivirus, in the family Arteriviridae within the order Nidovirales (4, 5). The PRRSV genome is approximately 15 kb in length and consists of at least 12 overlapping open reading frames (6, 7). Due to the genetic and antigenic differences, PRRSV can be divided into European genotype 1 and North American genotype 2, with Lelystad and VR-2332 as prototypical strains, respectively, which share about 60% nucleotide sequence identity (8). In 2006, highly pathogenic PRRSV (HP-PRRSV)

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“…et al, 2004). We previously have reported that Cecropin P1 inhibits the replication of PRRSV by blocking its attachment (Guo et al, 2014). In this study, the molecular mechanisms of CD-mediated inhibition against Li11 were characterized during the attachment and the entry stage of virus life cycle.…”

Section: Discussionmentioning

confidence: 97%