Relevant bibliographies by topics / Anti-virulence peptides

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Academic literature on the topic 'Anti-virulence peptides'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Anti-virulence peptides"

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Castillo-Juárez, Israel, Blanca Esther Blancas-Luciano, Rodolfo García-Contreras, and Ana María Fernández-Presas. "Antimicrobial peptides properties beyond growth inhibition and bacterial killing." PeerJ 10 (January 21, 2022): e12667. http://dx.doi.org/10.7717/peerj.12667.

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Antimicrobial peptides (AMPs) are versatile molecules with broad antimicrobial activity produced by representatives of the three domains of life. Also, there are derivatives of AMPs and artificial short peptides that can inhibit microbial growth. Beyond killing microbes, AMPs at grow sub-inhibitory concentrations also exhibit anti-virulence activity against critical pathogenic bacteria, including ESKAPE pathogens. Anti-virulence therapies are an alternative to antibiotics since they do not directly affect viability and growth, and they are considered less likely to generate resistance. Bacterial biofilms significantly increase antibiotic resistance and are linked to establishing chronic infections. Various AMPs can kill biofilm cells and eradicate infections in animal models. However, some can inhibit biofilm formation and promote dispersal at sub-growth inhibitory concentrations. These examples are discussed here, along with those of peptides that inhibit the expression of traits controlled by quorum sensing, such as the production of exoproteases, phenazines, surfactants, toxins, among others. In addition, specific targets that are determinants of virulence include secretion systems (type II, III, and VI) responsible for releasing effector proteins toxic to eukaryotic cells. This review summarizes the current knowledge on the anti-virulence properties of AMPs and the future directions of their research.
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Artini, Marco, Esther Imperlini, Francesco Buonocore, Michela Relucenti, Fernando Porcelli, Orlando Donfrancesco, Vanessa Tuccio Guarna Assanti, Ersilia Vita Fiscarelli, Rosanna Papa, and Laura Selan. "Anti-Virulence Potential of a Chionodracine-Derived Peptide against Multidrug-Resistant Pseudomonas aeruginosa Clinical Isolates from Cystic Fibrosis Patients." International Journal of Molecular Sciences 23, no. 21 (November 4, 2022): 13494. http://dx.doi.org/10.3390/ijms232113494.

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Pseudomonas aeruginosa is an opportunistic pathogen causing several chronic infections resistant to currently available antibiotics. Its pathogenicity is related to the production of different virulence factors such as biofilm and protease secretion. Pseudomonas communities can persist in biofilms that protect bacterial cells from antibiotics. Hence, there is a need for innovative approaches that are able to counteract these virulence factors, which play a pivotal role, especially in chronic infections. In this context, antimicrobial peptides are emerging drugs showing a broad spectrum of antibacterial activity. Here, we tested the anti-virulence activity of a chionodracine-derived peptide (KHS-Cnd) on five P. aeruginosa clinical isolates from cystic fibrosis patients. We demonstrated that KHS-Cnd impaired biofilm development and caused biofilm disaggregation without affecting bacterial viability in nearly all of the tested strains. Ultrastructural morphological analysis showed that the effect of KHS-Cnd on biofilm could be related to a different compactness of the matrix. KHS-Cnd was also able to reduce adhesion to pulmonary cell lines and to impair the invasion of host cells by P. aeruginosa. A cytotoxic effect of KHS-Cnd was observed only at the highest tested concentration. This study highlights the potential of KHS-Cnd as an anti-biofilm and anti-virulence molecule against P. aeruginosa clinical strains.
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Kamli, Majid, Jamal Sabir, Maqsood Malik, and Aijaz Ahmad. "Characterization of Defensin-Like Protein 1 for Its Anti-Biofilm and Anti-Virulence Properties for the Development of Novel Antifungal Drug against Candida auris." Journal of Fungi 8, no. 12 (December 14, 2022): 1298. http://dx.doi.org/10.3390/jof8121298.

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Candida auris has emerged as a pan-resistant pathogenic yeast among immunocompromised patients worldwide. As this pathogen is involved in biofilm-associated infections with serious medical manifestations due to the collective expression of pathogenic attributes and factors associated with drug resistance, successful treatment becomes a major concern. In the present study, we investigated the candidicidal activity of a plant defensin peptide named defensin-like protein 1 (D-lp1) against twenty-five clinical strains of C. auris. Furthermore, following the standard protocols, the D-lp1 was analyzed for its anti-biofilm and anti-virulence properties. The impact of these peptides on membrane integrity was also evaluated. For cytotoxicity determination, a hemolytic assay was conducted using horse blood. The minimum inhibitory concentration (MIC) and minimum fungicidal concentration (MFC) values ranged from 0.047–0.78 mg/mL and 0.095–1.56 mg/mL, respectively. D-lp1 at sub-inhibitory concentrations potentially abrogated both biofilm formation and 24-h mature biofilms. Similarly, the peptide severely impacted virulence attributes in the clinical strain of C. auris. For the insight mechanism, D-lp1 displayed a strong impact on the cell membrane integrity of the test pathogen. It is important to note that D-lp1 at sub-inhibitory concentrations displayed minimal hemolytic activity against horse blood cells. Therefore, it is highly useful to correlate the anti-Candida property of D-lp1 along with anti-biofilm and anti-virulent properties against C. auris, with the aim of discovering an alternative strategy for combating serious biofilm-associated infections caused by C. auris.
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Augustyniak, Daria, Eliza Kramarska, Paweł Mackiewicz, Magdalena Orczyk-Pawiłowicz, and Fionnuala T. Lundy. "Mammalian Neuropeptides as Modulators of Microbial Infections: Their Dual Role in Defense versus Virulence and Pathogenesis." International Journal of Molecular Sciences 22, no. 7 (April 1, 2021): 3658. http://dx.doi.org/10.3390/ijms22073658.

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The regulation of infection and inflammation by a variety of host peptides may represent an evolutionary failsafe in terms of functional degeneracy and it emphasizes the significance of host defense in survival. Neuropeptides have been demonstrated to have similar antimicrobial activities to conventional antimicrobial peptides with broad-spectrum action against a variety of microorganisms. Neuropeptides display indirect anti-infective capacity via enhancement of the host’s innate and adaptive immune defense mechanisms. However, more recently concerns have been raised that some neuropeptides may have the potential to augment microbial virulence. In this review we discuss the dual role of neuropeptides, perceived as a double-edged sword, with antimicrobial activity against bacteria, fungi, and protozoa but also capable of enhancing virulence and pathogenicity. We review the different ways by which neuropeptides modulate crucial stages of microbial pathogenesis such as adhesion, biofilm formation, invasion, intracellular lifestyle, dissemination, etc., including their anti-infective properties but also detrimental effects. Finally, we provide an overview of the efficacy and therapeutic potential of neuropeptides in murine models of infectious diseases and outline the intrinsic host factors as well as factors related to pathogen adaptation that may influence efficacy.
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Abril, Ana G., Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, José-Luis R. Rama, Pilar Calo-Mata, Angeles Sánchez-Pérez, and Tomás G. Villa. "Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?" Antibiotics 9, no. 6 (June 4, 2020): 302. http://dx.doi.org/10.3390/antibiotics9060302.

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Streptococcus spp. are major mastitis pathogens present in dairy products, which produce a variety of virulence factors that are involved in streptococcal pathogenicity. These include neuraminidase, pyrogenic exotoxin, and M protein, and in addition they might produce bacteriocins and antibiotic-resistance proteins. Unjustifiable misuse of antimicrobials has led to an increase in antibiotic-resistant bacteria present in foodstuffs. Identification of the mastitis-causing bacterial strain, as well as determining its antibiotic resistance and sensitivity is crucial for effective therapy. The present work focused on the LC–ESI–MS/MS (liquid chromatography–electrospray ionization tandem mass spectrometry) analysis of tryptic digestion peptides from mastitis-causing Streptococcus spp. isolated from milk. A total of 2706 non-redundant peptides belonging to 2510 proteins was identified and analyzed. Among them, 168 peptides were determined, representing proteins that act as virulence factors, toxins, anti-toxins, provide resistance to antibiotics that are associated with the production of lantibiotic-related compounds, or play a role in the resistance to toxic substances. Protein comparisons with the NCBI database allowed the identification of 134 peptides as specific to Streptococcus spp., while two peptides (EATGNQNISPNLTISNAQLNLEDKNK and DLWC*NM*IIAAK) were found to be species-specific to Streptococcus dysgalactiae. This proteomic repository might be useful for further studies and research work, as well as for the development of new therapeutics for the mastitis-causing Streptococcus strains.
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Abril, Ana G., Mónica Carrera, Karola Böhme, Jorge Barros-Velázquez, Pilar Calo-Mata, Angeles Sánchez-Pérez, and Tomás G. Villa. "Proteomic Characterization of Antibiotic Resistance in Listeria and Production of Antimicrobial and Virulence Factors." International Journal of Molecular Sciences 22, no. 15 (July 29, 2021): 8141. http://dx.doi.org/10.3390/ijms22158141.

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Some Listeria species are important human and animal pathogens that can be found in contaminated food and produce a variety of virulence factors involved in their pathogenicity. Listeria strains exhibiting multidrug resistance are known to be progressively increasing and that is why continuous monitoring is needed. Effective therapy against pathogenic Listeria requires identification of the bacterial strain involved, as well as determining its virulence factors, such as antibiotic resistance and sensitivity. The present study describes the use of liquid chromatography–electrospray ionization tandem mass spectrometry (LC–ESI–MS/MS) to do a global shotgun proteomics characterization for pathogenic Listeria species. This method allowed the identification of a total of 2990 non-redundant peptides, representing 2727 proteins. Furthermore, 395 of the peptides correspond to proteins that play a direct role in Listeria pathogenicity; they were identified as virulence factors, toxins and anti-toxins, or associated with either antibiotics (involved in antibiotic-related compounds production or resistance) or resistance to toxic substances. The proteomic repository obtained here can be the base for further research into pathogenic Listeria species and facilitate the development of novel therapeutics for these pathogens.
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O'Brien-Simpson, Neil M., Rita A. Paolini, and Eric C. Reynolds. "RgpA-Kgp Peptide-Based Immunogens Provide Protection againstPorphyromonas gingivalis Challenge in a Murine Lesion Model." Infection and Immunity 68, no. 7 (July 1, 2000): 4055–63. http://dx.doi.org/10.1128/iai.68.7.4055-4063.2000.

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ABSTRACT Porphyromonas gingivalis, a gram-negative bacterium, has been linked to the onset and progression of periodontitis, a chronic inflammatory disease of the supporting tissues of the teeth. A major virulence factor ofP. gingivalis is an extracellular complex of Arg- and Lys-specific proteinases and adhesins designated the RgpA-Kgp complex (formerly the PrtR-PrtK complex). In this study we show that the RgpA-Kgp complex, when used as an immunogen with incomplete Freund adjuvant (IFA), protects against challenge with invasive and noninvasive strains of P. gingivalis in the murine lesion model. We identified a variety of peptide vaccine candidates from the RgpA and Kgp polyprotein sequences that involved the putative active site histidine of both proteinases and five repeat motifs in the adhesin domains of both polyproteins implicated in aggregation and binding to host substrates, designated adhesin-binding motif (ABM) peptides. These peptides were synthesized using standard, solid-phase protocols for 9-fluorenylmethoxy carbonyl chemistry withS-acetylmercaptoacetic acid (SAMA) as the N-terminal residue. The SAMA-peptides were then conjugated to diphtheria toxoid and used with IFA to immunize BALB/c mice. Both active-site peptides and three of the five ABM peptides gave protection (P< 0.005) against challenge with P. gingivalis in the murine lesion model. The three ABM peptide sequences that conferred protection exist within a 100-residue span in the RgpA44 and Kgp39 adhesins of the RgpA-Kgp complex. Protective anti-RgpA-Kgp complex mouse antisera recognized the RgpA27, Kgp39, and RgpA44 adhesins in an immunoblot. Epitope mapping of the RgpA27 adhesin using the protective anti-RgpA-Kgp antisera identified a major protective epitope that mapped immediately N terminal to one of the protective ABM peptides in the 100-residue span in RgpA44 and Kgp39. This identified protective epitope contains clusters of basic residues spatially surrounded by hydrophobic amino acids, a finding which is characteristic of a heparin binding motif.
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Åkesson, Per, Heiko Herwald, Magnus Rasmussen, Katarina HÅkansson, Magnus Abrahamson, Ahmed A. K. Hasan, Alvin H. Schmaier, Werner Müller-Esterl, and Lars Björck. "Streptococcal inhibitor of complement-mediated lysis (SIC): an anti-inflammatory virulence determinant." Microbiology 156, no. 12 (December 1, 2010): 3660–68. http://dx.doi.org/10.1099/mic.0.039578-0.

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Since the late 1980s, a worldwide increase of severe Streptococcus pyogenes infections has been associated with strains of the M1 serotype, strains which all secrete the streptococcal inhibitor of complement-mediated lysis (SIC). Previous work has shown that SIC blocks complement-mediated haemolysis, inhibits the activity of antibacterial peptides and has affinity for the human plasma proteins clusterin and histidine-rich glycoprotein; the latter is a member of the cystatin protein family. The present work demonstrates that SIC binds to cystatin C, high-molecular-mass kininogen (HK) and low-molecular-mass kininogen, which are additional members of this protein family. The binding sites in HK are located in the cystatin-like domain D3 and the endothelial cell-binding domain D5. Immobilization of HK to cellular structures plays a central role in activation of the human contact system. SIC was found to inhibit the binding of HK to endothelial cells, and to reduce contact activation as measured by prolonged blood clotting time and impaired release of bradykinin. These results suggest that SIC modifies host defence systems, which may contribute to the virulence of S. pyogenes strains of the M1 serotype.
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Pacios, Olga, Lucia Blasco, Inès Bleriot, Laura Fernandez-Garcia, Mónica González Bardanca, Antón Ambroa, María López, German Bou, and Maria Tomás. "Strategies to Combat Multidrug-Resistant and Persistent Infectious Diseases." Antibiotics 9, no. 2 (February 6, 2020): 65. http://dx.doi.org/10.3390/antibiotics9020065.

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Antibiotic failure is one of the most worrying health problems worldwide. We are currently facing an international crisis with several problematic facets: new antibiotics are no longer being discovered, resistance mechanisms are occurring in almost all clinical isolates of bacteria, and recurrent infections caused by persistent bacteria are hampering the successful treatment of infections. In this context, new anti-infectious strategies against multidrug-resistant (MDR) and persistent bacteria, as well as the rescue of Food and Drug Administration (FDA)-approved compounds (drug repurposing), are being explored. Among the highlighted new anti-infectious strategies, in this review, we focus on antimicrobial peptides, anti-virulence compounds, phage therapy, and new molecules. As drugs that are being repurposed, we highlight anti-inflammatory compounds, anti-psychotics, anti-helminthics, anti-cancerous drugs, and statins.
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El-Dirany, Rima, Celia Fernández-Rubio, José Peña-Guerrero, Esther Moreno, Esther Larrea, Socorro Espuelas, Fadi Abdel-Sater, Klaus Brandenburg, Guillermo Martínez-de-Tejada, and Paul Nguewa. "Repurposing the Antibacterial Agents Peptide 19-4LF and Peptide 19-2.5 for Treatment of Cutaneous Leishmaniasis." Pharmaceutics 14, no. 11 (November 20, 2022): 2528. http://dx.doi.org/10.3390/pharmaceutics14112528.

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The lack of safe and cost-effective treatments against leishmaniasis highlights the urgent need to develop improved leishmanicidal agents. Antimicrobial peptides (AMPs) are an emerging category of therapeutics exerting a wide range of biological activities such as anti-bacterial, anti-fungal, anti-parasitic and anti-tumoral. In the present study, the approach of repurposing AMPs as antileishmanial drugs was applied. The leishmanicidal activity of two synthetic anti-lipopolysaccharide peptides (SALPs), so-called 19-2.5 and 19-4LF was characterized in Leishmania major. In vitro, both peptides were highly active against intracellular Leishmania major in mouse macrophages without exerting toxicity in host cells. Then, q-PCR-based gene profiling, revealed that this activity was related to the downregulation of several genes involved in drug resistance (yip1), virulence (gp63) and parasite proliferation (Cyclin 1 and Cyclin 6). Importantly, the treatment of BALB/c mice with any of the two AMPs caused a significant reduction in L. major infective burden. This effect was associated with an increase in Th1 cytokine levels (IL-12p35, TNF-α, and iNOS) in the skin lesion and spleen of the L. major infected mice while the Th2-associated genes were downregulated (IL-4 and IL-6). Lastly, we investigated the effect of both peptides in the gene expression profile of the P2X7 purinergic receptor, which has been reported as a therapeutic target in several diseases. The results showed significant repression of P2X7R by both peptides in the skin lesion of L. major infected mice to an extent comparable to that of a common anti-leishmanial drug, Paromomycin. Our in vitro and in vivo studies suggest that the synthetic AMPs 19-2.5 and 19-4LF are promising candidates for leishmaniasis treatment and present P2X7R as a potential therapeutic target in cutaneous leishmaniasis (CL).
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Dissertations / Theses on the topic "Anti-virulence peptides"

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HIMOUDI, NOURREDINE. "Developpement d'un modele general de vaccins conjugues polyosides-peptides comportant des epitopes b et t : application a la vaccination anti-pneumococcique (doctorat : pharmacologie)." Strasbourg 1, 2000. http://www.theses.fr/2000STR15056.

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BIANCALANI, CAROLA. "Anti-infective environmentally friendly molecules against plant pathogenic Gram-negative bacteria." Doctoral thesis, 2017. http://hdl.handle.net/2158/1087786.

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The market globalisation and the climate change are contributing substantially to the possible and rapid spread of alien and invasive plant pathogens in areas where they were previously absent, or are intensifying the incidence and severity of endemic pathogens, thus contributing significantly to increase the possible threats to the agricultural sector. Moreover, the lack of effective alternative molecules to copper compounds in plant protection, whose negative effects on both human health and environmental protection, have been neglected for far too long, and the need to adapt to European legislation, have led the operators in plant protection sector to reflect about the urgent need to implement a cultural revolution in which major innovation efforts are required. The study was carried out in order to achieve the following main aims: I) analysing pathogenic and virulence systems of phytopathogenic Gram-negative bacteria such as the Type Three Secretion System (TTSS), and in particular the main structural protein of TTSS pilus, i.e. “HrpA”, in order to design molecules able to block the pathogenicity and virulence of these bacteria without undermining their viability; II) verifying the in vitro and in vivo efficacy of anti-infective molecules, such as small oligopeptides and polyphenolic extracts obtained in a circular economy framework, to reduce or to block symptoms development caused by plant pathogenic bacteria; finally, as a future objective to analyse a possible correlation among virulence systems, fitness and efflux pumps related to xenobiotic compounds extrusion in phytopathogenic bacteria, in order to identify underdeveloped targets, against which innovative molecules can be designed.
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Book chapters on the topic "Anti-virulence peptides"

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Kalra, Aakanksha, Sakshi Piplani, and Ravi Ranjan Kumar Niraj. "Current Therapeutic Options and Challenges for MDR." In Current Developments in the Detection and Control of Multi Drug Resistance, 66–78. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815049879122010009.

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Multiple-Drug Resistance (MDR) against many antibiotics and other therapeutic agents is a major concern for health care providers and researchers in the field. Due to tremendous rise in MDR cases, researchers are in search of potent therapeutic options or alternatives to overcome MDR. Here, in this chapter, we will discuss the current status of the common as well as advanced methods which have been developed so far for the treatment of MDR and also the challenges and opportunities in each of those methods. This chapter discusses common methods used for the treatment of MDR, i.e., major antibiotics used for the treatment of MDR bacteria and synergistic approaches by the combination of different antibiotics. Along with common treatments used against MDR bacteria, this chapter also discusses current treatments like anti microbial peptides, anti-virulence compounds, phage therapy and drug repurposing approaches for MDR treatment.
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