Induced expression of melittin, an antimicrobial peptide, inhibits infection by Chlamydia trachomatis and Mycoplasma hominis in a HeLa cell line

Лазарев, В. Н.; Parfenova, T. M.; Gularyan, S.K; Misyurina, O. Yu.; Akopian, T. A.; Govorun, Vadim M.

doi:10.1016/s0924-8579(01)00479-4

Cited by 40 publications

(31 citation statements)

References 18 publications

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“…This mode of action is responsible for its hemolytic, anti-microbial (Blondelle and Houghten 1991a;Bechinger 1997), anti-fungal (Lazarev et al 2002), anti-tumor ) and leishmanicidal (Diaz-Achirica et al 1998) activities of melittin. The protozoan mammalian parasite Leishmania is the causative agent of leishmaniasis, which afflicts 12-14 million people worldwide (Herwaldt 1999).…”

Section: Leishmanicidal Activity Of Melittinmentioning

confidence: 99%

Melittin: a Membrane-active Peptide with Diverse Functions

2007

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Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid-protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin-membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.

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Section: Leishmanicidal Activity Of Melittinmentioning

confidence: 99%

Melittin: a Membrane-active Peptide with Diverse Functions

2007

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“…The AMPs are among the compounds under investigation for their general antimicrobial potency, and several of them are undergoing clinical evaluation (29,30). Regarding the Mollicutes, a recombinant plasmid expressing a gene for an AMP, melittin, was introduced into cell line and animal models, and the results suggested efficacy in the treatment of infections caused by Mycoplasma hominis and Mycoplasma gallisepticum (31)(32)(33)(34). Our study may provide another promising new strategy for treating ureaplasma infections.…”

Section: Discussionmentioning

confidence: 85%

Suppression of Antimicrobial Peptide Expression by Ureaplasma Species

et al. 2014

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Ureaplasma species commonly colonize the adult urogenital tract and are implicated in invasive diseases of adults and neonates. Factors that permit the organisms to cause chronic colonization or infection are poorly understood. We sought to investigate whether host innate immune responses, specifically, antimicrobial peptides (AMPs), are involved in determining the outcome of Ureaplasma infections. THP-1 cells, a human monocytoid tumor line, were cocultured with Ureaplasma parvum and U. urealyticum. Gene expression levels of a variety of host defense genes were quantified by real-time PCR. In vitro antimicrobial activities of synthetic AMPs against Ureaplasma spp. were determined using a flow cytometry-based assay. Chromosomal histone modifications in host defense gene promoters were tested by chromatin immunoprecipitation (ChIP). DNA methylation status in the AMP promoter regions was also investigated. After stimulation with U. parvum and U. urealyticum, the expression of cell defense genes, including the AMP genes (DEFB1, DEFA5, DEFA6, and CAMP), was significantly downregulated compared to that of TNFA and IL-8, which were upregulated. In vitro flow cytometry-based antimicrobial assay revealed that synthetic peptides LL-37, hBD-3, and hBD-1 had activity against Ureaplasma spp. Downregulation of the AMP genes was associated with chromatin modification alterations, including the significantly decreased histone H3K9 acetylation with U. parvum infection. No DNA methylation status changes were detected upon Ureaplasma infection. In conclusion, AMPs have in vitro activity against Ureaplasma spp., and suppression of AMP expression might be important for the organisms to avoid this aspect of the host innate immune response and to establish chronic infection and colonization.

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“…We previously showed inhibition of M. hominis infection in HeLa/Tet-On and HeLa/Tet-Off cells transfected with rPV expressing melittin gene under the control of tetracycline CMV promoter [8]. However, the gene encoding transactivator protein rtTA in this case was constitutively expressed in HeLa/Tet-On and HeLa/Tet-Off cells.…”

Section: Resultsmentioning

confidence: 94%

“…Moreover, previous experiments showed [2] that in vitro treatment of various mycoplasma strains with amphipathic peptides (cecropin A, melittin, magainin 2) leads to depolarization of their plasma membranes, changes in cell morphology, and inhibition of their mobility. We previously showed that expression of melittin gene in HeLa cell culture reduced transmembrane potential of transfected cells [8], which, in turn, disturbs the process of mycoplasma adhesion to cells and normal cycle of their development.…”

Section: Resultsmentioning

confidence: 99%

Recombinant plasmid constructs expressing gene for antimicrobial peptide melittin for the therapy of mycoplasma and chlamydia infections

et al. 2007

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In view of growing number of pathogenic microbial strain resistant to routine antibiotics, antimicrobial peptides become promising agents for the therapy of infectious diseases. We studied in vivo effects of melittin, an antimicrobial peptide expressed in a recombinant plasmid vector, on infection with urogenital pathogens Chlamydia trachomatis, Mycoplasma hominis, and Mycoplasma gallisepticum. We obtained recombinant plasmid constructs, where melittin gene is under the control of tetracycline-dependent human cytomegalovirus promoter. Inhibition of experimental C. trachomatis, M. hominis, and M. gallisepticum infection after administration of recombinant plasmid vectors expressing melittin gene to BALB/c mice was demonstrated.

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Induced expression of melittin, an antimicrobial peptide, inhibits infection by Chlamydia trachomatis and Mycoplasma hominis in a HeLa cell line

Cited by 40 publications

References 18 publications

Melittin: a Membrane-active Peptide with Diverse Functions

Melittin: a Membrane-active Peptide with Diverse Functions

Suppression of Antimicrobial Peptide Expression by Ureaplasma Species

Recombinant plasmid constructs expressing gene for antimicrobial peptide melittin for the therapy of mycoplasma and chlamydia infections

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