Antimicrobial Peptides

Total Page:16

File Type:pdf, Size:1020Kb

Antimicrobial Peptides Antimicrobial peptides Innate Immunity · Acute phase proteins · Western blot · Antimicrobial peptides · Complement Research · LPS, Microbial toxins · Flow cytometry · Scavenger receptors · TLR · Assays · Inflammation · Adhesion molecules · Immunohistochemistry · Coagulation molecules · Cytokines · Chemokines · Antibodies · Cell & Tissue damage · Functional studies · Lipid binding proteins · Immunoprecipitation · Oxidative stress · Organ & Tissue related research · Proteins · www.hycultbiotech.com Leukocytes/ Lungs Neutrophils • TAP • Calprotectin • HBD-1 • LL-37 • HBD-2 • HNP1-3 • LL-37 • SLPI • Elastase • NGAL • HNP1-3 • Azurocidin • BPI • MPO • Arginase • Elastase • SLPI • Lactoferrin • RNAse7 • BPI • Arginase Intestine • HD6 Kidney • HD5 • β-defensin-2 • β-defensin-2 • HD5 • Calprotectin • LL-37 • S100A4 • S100A8 • S100A9 Skin • S100A12 • LL-37 • HBD-1 • HBD-2 Reproductive Tract • RNAse7 • β-defensin-1 • Elan • HD5 • S100A7 • LL-37 Antimicrobial peptides and proteins are Abbreviations in this brochure: important means of innate host defense FC: Flow Cytometry in eukaryotes. They have a broad ability FS: Functional studies F: Frozen sections to kill microbes. Beside their role as endo- P: Paraffin sections genous antibiotics, antimicrobial peptides IA: Immunoassays ELISA kits are involved in cytokine release, chemo- IF: Immunofluorescence taxis, angiogenesis, wound repair and IP: Immunoprecipitation Product Cat.# regulation of the adaptive immune system. W: Western Blot We offer a broad range in the field of BPI, Human, ELISA kit HK314 Calprotectin, Human, ELISA kit HK325 antimicrobial peptides, from antibodies Elafin, Human, ELISA kit HK318 and proteins to specific, sensitive and Elastase, Human, ELISA kit HK319 robust ELISA kits. HNP1-3, Human, ELISA kit HK317 Lactoferrin, Human, ELISA kit HK329 LBP, Human, ELISA kit HK315 LBP, Mouse, ELISA kit HK205 LBP, of various species, ELISA kit HK503 LL-37, Human, ELISA kit HK321 MPO, Human, ELISA kit HK324 MPO, Mouse, ELISA kit HK210 MPO, Rat, ELISA kit HK105 NGAL, Human, ELISA kit HK330 S100A9/Calprotectin, Mouse, ELISA kit HK214 SLPI, Human, ELISA kit HK316 HD5 in human ileum tissue. Staining of paraffin embedded Human Kidney paraffin sections with mAb All ELISA kits are available in 1- and 2-plate format, section with antibody to human HD5 (Cat.# HM2228). 3D11 (Cat.# HM2070) with exception of HK503. Antibodies Antibodies Product Cat.# Product Cat.# Azurocidin, Human, mAb #z6721, 100µg HM2310 LL37/CAP18, Human, mAb 1-1C12, 100µg HM2071 Azurocidin, Human, mAb #z6733, 100µg HM2311 Lysozyme, Human, pAb, 100µg HP9035 Azurocidin, Human, mAb #z6718, 100µg HM2312 Mannose Receptor, Human, mAb 15-2, 100µg HM2056 BPI, Human, mAb 3F9, 100µg HM2041 Mannose Receptor, Human, mAb 15-2, biotinylated, 50µg HM2057 BPI, Human, mAb 4H5, 100µg HM2042 Mannose Receptor, Mouse, mAb MR5D3, 100µg HM1049 BPI, Human, mAb 4E3, 100µg HM2170 MPO, Human, mAb 266-6K1, 100µg HM2164 BPI, Human, pAb, 100µg HP9022 MPO, Human, mAb B7, 100µg HM2288 Calprotectin, Human, mAb 27E10, 100µg HM2156 MPO, Human, mAb 266-6K1, biotinylated, 50µg HM2164BT Calprotectin, Human, mAb 27E10, biotinylated, 50µg HM2156BT MPO, Human, mAb 266-6K1, FITC, 100µg HM2164F Calprotectin, Human, mAb 27E10, FITC, 100µg HM2156F MPO, Mouse, mAb 8F4 , 100µg HM1051 CHIPS, mAb JCC1, 100µg HM6003 MPO, Mouse, mAb B7, 100µg HM1135 CHIPS , mAb JNC1, 100µg HM6004 MPO, Mouse, mAb 8F4, biotinylated, 50µg HM1051BT CRISP-3, Human, pAb, 100µg HP9033 MPO, Mouse, mAb 8F4, FITC, 100µg HM1051F Defensin 5, Human, mAb 8C8, 100µg HM2228 MPO, Mouse, mAb 8F4, R-PE, 25 tests HM1051PE-25 Dermcidin, Human, mAb G-81, >200µg HM2040 MPO, Mouse, mAb 8F4, R-PE, 100 tests HM1051PE-100 Elafin, Human, mAb TRAB2O, 100µg HM2062 MPO, Rat, mAb 2D4, 100µg HM3030 Elafin, Human, mAb TRAB2F, 100µg HM2063 MPO, Rat, mAb B7, 100µg HM3039 Elafin, Human, pAb, 1ml HP9025 MPO, Rat, mAb 2D4, biotinylated, 50µg HM3030BT Elastase, Human, mAb 265-3K1, 100µg HM2174 MPO, Rat, mAb 2D4, FITC, 100µg HM3030F Elastase, Human, pAb, 100µg HP9027 MPO, Rat, mAb 2D4, R-PE, 25 tests HM3030PE-25 EphB1, B2, B3, Mouse, mAb Efb1-3, 100µg HM1113 MPO, Rat, mAb 2D4, R-PE, 100 tests HM3030PE-100 EphB1, Mouse, mAb EfrnB1, 100µg HM1114 Neutrophil defensin 5, Rabbit, mAb R3, 100µg HM4008 Galectin-2, Human , mAb H3F3D1, 100µg HM2306 NGAL, Human, mAb 697, 100µg HM2193 Galectin-3, Human, mAb B2C10, 100µg HM2186 Pentraxin 3, Human, mAb MNB1, 100µg HM2241 Galectin-8, Human, mAb 106.1, 100µg HM2278 Pentraxin 3, Human, mAb MNB4, 100µg HM2242 HNP1-3, Human, mAb D21 , 100µg HM2058 Pentraxin 3, Human, mAb MNB4, FITC, 100µg HM2242F HNP1-3, Human, mAb D21, biotinylated, 50µg HM2059 Pentraxin 3, Mouse, mAb 2C3, 100µg HM1130 Lactoferrin, Bovine, mAb 5F12.1.2, 100µg HM4012 Pentraxin 3, Mouse, mAb 6B11, 100µg HM1131 Lactoferrin, Bovine, mAb a-bC-lobe, 100µg HM4013 Pentraxin 3, Mouse, mAb 6B11, biotinylated, 50µg HM1131BT Lactoferrin, Bovine, pAb, 100µg HP7001 Polymyxin B, mAb 45, >200µg HM2047 Lactoferrin, Human, mAb 265-1K1, 100µg HM2173 Proteinase 3, Human, mAb WGM2, 100µg HM2171 Lactoferrin, Human, pAb, 100µg HP9034 Proteinase 3, Human, mAb PR3G-2, 100µg HM2172 Lactoferrin, Mouse, mAb 1A10, 100µg HM1132 Proteinase 3, Human, mAb WGM2, FITC, 100µg HM2171F Lactoferrin, Mouse, mAb 1E4, 100µg HM1133 Proteinase 3, Human, mAb PR3G-2, FITC, 100µg HM2172F LBP, Human, mAb 6G3, 100µg HM2043 RBC, Mouse, mAb 34-3C, 100µg HM1120 LBP, Human, mAb 1C7, 100µg HM2044 RBC, Mouse, mAb 34-3C, FITC, 100µg HM1120F LBP, Human, pAb, 100µg HP9023 S100A9, Mouse, mAb MU14-2A5, 100µg HM1102 LBP, Mouse, mAb M330-19, 100µg HM1026 S100A9, Mouse, mAb MU14-2A5, biotinylated, 50µg HM1102BT LBP, Mouse, mAb RR433-8, 100µg HM1027 SLPI, Human, mAb 31, 100µg HM2037 LBP, Mouse, mAb M392-2, 100µg HM1028 SLPI, Human, pAb, 100µg HP9024 LL37/CAP18, Human, mAb 3D11, 100µg HM2070 SLPI, Human, mAb 31, biotinylated, 50µg HM2038 Flow cytometric detection of mouse MPO in Wehi 3BD+ cells (mAb B7, Cat.# HM1135). Red represents the isotype control, black the negative control and the blue line represents HM1135 10µg/ml. Flow cytometric detection of human Galectin-3 in Huvec cells (mAb B2C10, Cat.# HM2186). Red represents the isotype control, black the negative control and the blue line represents HM2186 20µg/ml. Antibodies B Product Cat.# a n d T Defensin 5, Human, mAb 8C8, 0.5mg HM2228-IA cytotoxicity and cells Elastase, Human, mAb 265-3K1, 0.5mg HM2174-IA growth promotion LL37/CAP18, Human, mAb 3D11, 0.5mg HM2070-FS α-defensins ACTH antagonist a d NP-3A re Mannose Receptor, Human, mAb 15-2, no cyte 0.5mg HM2056-FS MPO, Human, mAb 266-6K1, 0.5mg HM2164-IA MPO, Rat, mAb 2D4, 0.5mg HM3030-IA histamine release opsonization l Pentraxin 3, Human, mAb MNB1, 0.5mg HM2241-IA mast cel α-defensins NP-1 Pentraxin 3, Human, mAb MNB1, 0.5mg HM2241-FS HBD-2 NP-2 K Pentraxin 3, Human, mAb MNB4, 0.5mg HM2242-IA leb α- and β- siell iae S100A9, Mouse, mAb MU14-2A5, 0.5mg HM1102-IA a pneumon defensins SLPI, Human, mAb 31, 0.5mg HM2037-IA m interaction with o complement Proteins and peptides n o c y t -2 e P Name Cat.# s N HN H chemotaxis P-1 wound repair, c y Alpha-Defensin 5, Human, peptide HC2121 2 cell migration t - o D Calprotectin, Human, Recombinant HC2120 k HNP1-3 i B n EGF receptor H CCR6 e CHIPS HC4012 - a il c h Elafin, Human, Recombinant HC4011 t p iv ro T at t ed neu HNP1-3, Human, Natural HC4014 c e LBP, Human, Peptide HC4030-01 lls HBD-2 LBP, Human, Peptide HC4030-05 ll s e n LBP, Human, Peptide HC4030-10 c c si dendriti n LBP, Human, Purified, Natural HC4010 efe HBD-2 α-d LL37, Human, Peptide HC4013 Why scientists buy our products: · Unique products · Sensitivity · Specificity · Easy to use · Value for money · 1- & 2-plate kits · Functional studies · Technical support · · Standardized assays · Quality control · Inter/intra variation <10% · Well documented products · Broad in applications · Hycult Biotech is distributed by: www.hycultbiotech.com Hycult Biotech BV Hycult Biotech Inc P.O. Box 30 600 West Germantown Pike 5400 AA Uden Suite 110 The Netherlands Plymouth Meeting, PA 19462 USA T +31 413 25 13 35 T: 1-484-534-3566 Toll Free: 855-2-HYCULT (855 249 2858) F +31 413 24 83 53 F: 1-484-368-3558 E [email protected] E: [email protected].
Recommended publications
  • Antimicrobial Activity of Cathelicidin Peptides and Defensin Against Oral Yeast and Bacteria JH Wong, TB Ng *, RCF Cheung, X Dan, YS Chan, M Hui
    RESEARCH FUND FOR THE CONTROL OF INFECTIOUS DISEASES Antimicrobial activity of cathelicidin peptides and defensin against oral yeast and bacteria JH Wong, TB Ng *, RCF Cheung, X Dan, YS Chan, M Hui KEY MESSAGES Mycosphaerella arachidicola, Saccharomyces cerevisiae and C albicans with an IC value of 1. Human cathelicidin LL37 and its fragments 50 3.9, 4.0, and 8.4 μM, respectively. The peptide LL13-37 and LL17-32 were equipotent in increased fungal membrane permeability. inhibiting growth of Candida albicans. 6. LL37 did not show obvious antibacterial activity 2. LL13-37 permeabilised the membrane of yeast below a concentration of 64 μM and its fragments and hyphal forms of C albicans and adversely did not show antibacterial activity below a affected mitochondria. concentration of 128 μM. Pole bean defensin 3. Reactive oxygen species was detectable in the exerted antibacterial activity on some bacterial yeast form after LL13-37 treatment but not in species. untreated cells suggesting that the increased membrane permeability caused by LL13-37 might also lead to uptake of the peptide, which Hong Kong Med J 2016;22(Suppl 7):S37-40 might have some intracellular targets. RFCID project number: 09080432 4. LL37 and its fragments also showed antifungal 1 JH Wong, 1 TB Ng, 1 RCF Cheung, 1 X Dan, 1 YS Chan, 2 M Hui activity against C krusei, and C tropicalis. 5. A 5447-Da antifungal peptide with sequence The Chinese University of Hong Kong: 1 School of Biomedical Sciences homology to plant defensins was purified from 2 Department of Microbiology king pole beans by chromatography on Q- Sepharose and FPLC-gel filtration on Superdex * Principal applicant and corresponding author: 75.
    [Show full text]
  • Human Peptides -Defensin-1 and -5 Inhibit Pertussis Toxin
    toxins Article Human Peptides α-Defensin-1 and -5 Inhibit Pertussis Toxin Carolin Kling 1, Arto T. Pulliainen 2, Holger Barth 1 and Katharina Ernst 1,* 1 Institute of Pharmacology and Toxicology, Ulm University Medical Center, 89081 Ulm, Germany; [email protected] (C.K.); [email protected] (H.B.) 2 Institute of Biomedicine, Research Unit for Infection and Immunity, University of Turku, FI-20520 Turku, Finland; arto.pulliainen@utu.fi * Correspondence: [email protected] Abstract: Bordetella pertussis causes the severe childhood disease whooping cough, by releasing several toxins, including pertussis toxin (PT) as a major virulence factor. PT is an AB5-type toxin, and consists of the enzymatic A-subunit PTS1 and five B-subunits, which facilitate binding to cells and transport of PTS1 into the cytosol. PTS1 ADP-ribosylates α-subunits of inhibitory G-proteins (Gαi) in the cytosol, which leads to disturbed cAMP signaling. Since PT is crucial for causing severe courses of disease, our aim is to identify new inhibitors against PT, to provide starting points for novel therapeutic approaches. Here, we investigated the effect of human antimicrobial peptides of the defensin family on PT. We demonstrated that PTS1 enzyme activity in vitro was inhibited by α-defensin-1 and -5, but not β-defensin-1. The amount of ADP-ribosylated Gαi was significantly reduced in PT-treated cells, in the presence of α-defensin-1 and -5. Moreover, both α-defensins decreased PT-mediated effects on cAMP signaling in the living cell-based interference in the Gαi- mediated signal transduction (iGIST) assay.
    [Show full text]
  • Innate Immune System of Mallards (Anas Platyrhynchos)
    Anu Helin Linnaeus University Dissertations No 376/2020 Anu Helin Eco-immunological studies of innate immunity in Mallards immunity innate of studies Eco-immunological List of papers Eco-immunological studies of innate I. Chapman, J.R., Hellgren, O., Helin, A.S., Kraus, R.H.S., Cromie, R.L., immunity in Mallards (ANAS PLATYRHYNCHOS) Waldenström, J. (2016). The evolution of innate immune genes: purifying and balancing selection on β-defensins in waterfowl. Molecular Biology and Evolution. 33(12): 3075-3087. doi:10.1093/molbev/msw167 II. Helin, A.S., Chapman, J.R., Tolf, C., Andersson, H.S., Waldenström, J. From genes to function: variation in antimicrobial activity of avian β-defensin peptides from mallards. Manuscript III. Helin, A.S., Chapman, J.R., Tolf, C., Aarts, L., Bususu, I., Rosengren, K.J., Andersson, H.S., Waldenström, J. Relation between structure and function of three AvBD3b variants from mallard (Anas platyrhynchos). Manuscript I V. Chapman, J.R., Helin, A.S., Wille, M., Atterby, C., Järhult, J., Fridlund, J.S., Waldenström, J. (2016). A panel of Stably Expressed Reference genes for Real-Time qPCR Gene Expression Studies of Mallards (Anas platyrhynchos). PLoS One. 11(2): e0149454. doi:10.1371/journal. pone.0149454 V. Helin, A.S., Wille, M., Atterby, C., Järhult, J., Waldenström, J., Chapman, J.R. (2018). A rapid and transient innate immune response to avian influenza infection in mallards (Anas platyrhynchos). Molecular Immunology. 95: 64-72. doi:10.1016/j.molimm.2018.01.012 (A VI. Helin, A.S., Wille, M., Atterby, C., Järhult, J., Waldenström, J., Chapman, N A S J.R.
    [Show full text]
  • Antimicrobial Peptides in Reptiles
    Pharmaceuticals 2014, 7, 723-753; doi:10.3390/ph7060723 OPEN ACCESS pharmaceuticals ISSN 1424-8247 www.mdpi.com/journal/pharmaceuticals Review Antimicrobial Peptides in Reptiles Monique L. van Hoek National Center for Biodefense and Infectious Diseases, and School of Systems Biology, George Mason University, MS1H8, 10910 University Blvd, Manassas, VA 20110, USA; E-Mail: [email protected]; Tel.: +1-703-993-4273; Fax: +1-703-993-7019. Received: 6 March 2014; in revised form: 9 May 2014 / Accepted: 12 May 2014 / Published: 10 June 2014 Abstract: Reptiles are among the oldest known amniotes and are highly diverse in their morphology and ecological niches. These animals have an evolutionarily ancient innate-immune system that is of great interest to scientists trying to identify new and useful antimicrobial peptides. Significant work in the last decade in the fields of biochemistry, proteomics and genomics has begun to reveal the complexity of reptilian antimicrobial peptides. Here, the current knowledge about antimicrobial peptides in reptiles is reviewed, with specific examples in each of the four orders: Testudines (turtles and tortosises), Sphenodontia (tuataras), Squamata (snakes and lizards), and Crocodilia (crocodilans). Examples are presented of the major classes of antimicrobial peptides expressed by reptiles including defensins, cathelicidins, liver-expressed peptides (hepcidin and LEAP-2), lysozyme, crotamine, and others. Some of these peptides have been identified and tested for their antibacterial or antiviral activity; others are only predicted as possible genes from genomic sequencing. Bioinformatic analysis of the reptile genomes is presented, revealing many predicted candidate antimicrobial peptides genes across this diverse class. The study of how these ancient creatures use antimicrobial peptides within their innate immune systems may reveal new understandings of our mammalian innate immune system and may also provide new and powerful antimicrobial peptides as scaffolds for potential therapeutic development.
    [Show full text]
  • The Unusual Resistance of Avian Defensin
    The unusual resistance of avian defensin AvBD7 to proteolytic enzymes preserves its antibacterial activity Geoffrey Bailleul, Amanda Kravtzoff, Alix Joulin-Giet, Fabien Lecaille, Valérie Labas, Hervé Meudal, Karine Loth, Ana-Paula Teixeira-Mechin, Florence B. Gilbert, Laurent Coquet, et al. To cite this version: Geoffrey Bailleul, Amanda Kravtzoff, Alix Joulin-Giet, Fabien Lecaille, Valérie Labas, et al..The unusual resistance of avian defensin AvBD7 to proteolytic enzymes preserves its antibacterial activity. PLoS ONE, Public Library of Science, 2016, 11 (8), pp.1-20. 10.1371/journal.pone.0161573. hal- 01594888 HAL Id: hal-01594888 https://hal.archives-ouvertes.fr/hal-01594888 Submitted on 26 Sep 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License RESEARCH ARTICLE The Unusual Resistance of Avian Defensin AvBD7 to Proteolytic Enzymes Preserves Its Antibacterial Activity Geoffrey Bailleul1, Amanda Kravtzoff2, Alix Joulin-Giet1, Fabien Lecaille2, Valérie Labas3, Hervé Meudal4,
    [Show full text]
  • Vitamin D-Cathelicidin Axis: at the Crossroads Between Protective Immunity and Pathological Inflammation During Infection
    Immune Netw. 2020 Apr;20(2):e12 https://doi.org/10.4110/in.2020.20.e12 pISSN 1598-2629·eISSN 2092-6685 Review Article Vitamin D-Cathelicidin Axis: at the Crossroads between Protective Immunity and Pathological Inflammation during Infection Chaeuk Chung 1, Prashanta Silwal 2,3, Insoo Kim2,3, Robert L. Modlin 4,5, Eun-Kyeong Jo 2,3,6,* 1Division of Pulmonary and Critical Care, Department of Internal Medicine, Chungnam National University School of Medicine, Daejeon 35015, Korea Received: Oct 27, 2019 2Infection Control Convergence Research Center, Chungnam National University School of Medicine, Revised: Jan 28, 2020 Daejeon 35015, Korea Accepted: Jan 30, 2020 3Department of Microbiology, Chungnam National University School of Medicine, Daejeon 35015, Korea 4Division of Dermatology, Department of Medicine, David Geffen School of Medicine at the University of *Correspondence to California, Los Angeles, Los Angeles, CA 90095, USA Eun-Kyeong Jo 5Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Department of Microbiology, Chungnam Los Angeles, CA 90095, USA National University School of Medicine, 282 6Department of Medical Science, Chungnam National University School of Medicine, Daejeon 35015, Korea Munhwa-ro, Jung-gu, Daejeon 35015, Korea. E-mail: [email protected] Copyright © 2020. The Korean Association of ABSTRACT Immunologists This is an Open Access article distributed Vitamin D signaling plays an essential role in innate defense against intracellular under the terms of the Creative Commons microorganisms via the generation of the antimicrobial protein cathelicidin. In addition Attribution Non-Commercial License (https:// to directly binding to and killing a range of pathogens, cathelicidin acts as a secondary creativecommons.org/licenses/by-nc/4.0/) messenger driving vitamin D-mediated inflammation during infection.
    [Show full text]
  • The Human Cathelicidin LL-37 — a Pore-Forming Antibacterial Peptide and Host-Cell Modulator☆
    Biochimica et Biophysica Acta 1858 (2016) 546–566 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbamem The human cathelicidin LL-37 — A pore-forming antibacterial peptide and host-cell modulator☆ Daniela Xhindoli, Sabrina Pacor, Monica Benincasa, Marco Scocchi, Renato Gennaro, Alessandro Tossi ⁎ Department of Life Sciences, University of Trieste, via Giorgeri 5, 34127 Trieste, Italy article info abstract Article history: The human cathelicidin hCAP18/LL-37 has become a paradigm for the pleiotropic roles of peptides in host de- Received 7 August 2015 fence. It has a remarkably wide functional repertoire that includes direct antimicrobial activities against various Received in revised form 30 October 2015 types of microorganisms, the role of ‘alarmin’ that helps to orchestrate the immune response to infection, the Accepted 5 November 2015 capacity to locally modulate inflammation both enhancing it to aid in combating infection and limiting it to pre- Available online 10 November 2015 vent damage to infected tissues, the promotion of angiogenesis and wound healing, and possibly also the elimi- Keywords: nation of abnormal cells. LL-37 manages to carry out all its reported activities with a small and simple, Cathelicidin amphipathic, helical structure. In this review we consider how different aspects of its primary and secondary LL-37 structures, as well as its marked tendency to form oligomers under physiological solution conditions and then hCAP-18 bind to molecular surfaces as such, explain some of its cytotoxic and immunomodulatory effects. We consider CRAMP its modes of interaction with bacterial membranes and capacity to act as a pore-forming toxin directed by our Host defence peptide organism against bacterial cells, contrasting this with the mode of action of related peptides from other species.
    [Show full text]
  • Avian Antimicrobial Host Defense Peptides: from Biology to Therapeutic Applications
    Pharmaceuticals 2014, 7, 220-247; doi:10.3390/ph7030220 OPEN ACCESS pharmaceuticals ISSN 1424-8247 www.mdpi.com/journal/pharmaceuticals Review Avian Antimicrobial Host Defense Peptides: From Biology to Therapeutic Applications Guolong Zhang 1,2,3,* and Lakshmi T. Sunkara 1 1 Department of Animal Science, Oklahoma State University, Stillwater, OK 74078, USA 2 Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA 3 Department of Physiological Sciences, Oklahoma State University, Stillwater, OK 74078, USA * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +1-405-744-6619; Fax: +1-405-744-7390. Received: 6 February 2014; in revised form: 18 February 2014 / Accepted: 19 February 2014 / Published: 27 February 2014 Abstract: Host defense peptides (HDPs) are an important first line of defense with antimicrobial and immunomoduatory properties. Because they act on the microbial membranes or host immune cells, HDPs pose a low risk of triggering microbial resistance and therefore, are being actively investigated as a novel class of antimicrobials and vaccine adjuvants. Cathelicidins and β-defensins are two major families of HDPs in avian species. More than a dozen HDPs exist in birds, with the genes in each HDP family clustered in a single chromosomal segment, apparently as a result of gene duplication and diversification. In contrast to their mammalian counterparts that adopt various spatial conformations, mature avian cathelicidins are mostly α-helical. Avian β-defensins, on the other hand, adopt triple-stranded β-sheet structures similar to their mammalian relatives. Besides classical β-defensins, a group of avian-specific β-defensin-related peptides, namely ovodefensins, exist with a different six-cysteine motif.
    [Show full text]
  • Plasma Elafin, Cathelicidin, and Α-Defensins Are Increased in Paediatric Inflammatory Crohn’S Disease and Reflect Disease Location
    Research letter Gastroenterology Plasma elafin, cathelicidin, and α-defensins are increased in paediatric inflammatory Crohn’s disease and reflect disease location Andrzej Wędrychowicz1, Przemysław Tomasik2, Kinga Kowalska-Duplaga1, Stanisław Pieczarkowski1, Krzysztof Fyderek1 1Department of Paediatrics, Gastroenterology, and Nutrition, Jagiellonian University Corresponding author: Medical College, Krakow, Poland Prof. Andrzej Wędrychowicz 2Department of Clinical Biochemistry, Jagiellonian University Medical College, Krakow, Department of Paediatrics, Poland Gastroenterology, and Nutrition Submitted: 10 April 2021, Accepted: 1 June 2021 Jagiellonian University Online publication: 11 June 2021 Medical College Krakow, Poland Arch Med Sci 2021; 17 (4): 1114–1117 Phone: +48 12 3339330 DOI: https://doi.org/10.5114/aoms/138349 E-mail: Copyright © 2021 Termedia & Banach [email protected] Abstract Introduction: The aim of our study was to assess antimicrobial peptides in children with Crohn’s disease (CD). Methods: Plasma elafin, cathelicidin, and α- and β-defensins were assessed in 35 children with CD using immunoassays. Phenotype and location of CD were assessed based on the results of endoscopic and radiological studies. Results: We found increased elafin, cathelicidin, and α-defensins in children with inflammatory phenotype as compared to stricturing and penetrating phenotypes of CD. Additionally, we found increased elafin and cathelicidin in colonic location and α-defensins in ileal CD locations. Conclusions: Assessing antimicrobial
    [Show full text]
  • Neutrophil Products Inhibit LLO Secretion and Activity, and Listeria Monocytogenes Intracellular Growth
    Neutrophil products inhibit LLO secretion and activity, and Listeria monocytogenes intracellular growth Dissertation Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Eusondia Arnett Graduate Program in Microbiology The Ohio State University 2013 Dissertation Committee: Dr. Stephanie Seveau, Advisor Dr. John Gunn Dr. Mike Ibba Dr. Larry Schlesinger Copyright by Eusondia Arnett 2013 Abstract Listeria monocytogenes is a facultative intracellular pathogen that infects a large variety of host cells, including macrophages and diverse non-phagocytic cells. To avoid the phagosome microbicidal environment, L. monocytogenes secretes a pore-forming toxin (listeriolysin O; LLO) that releases the bacterium into the cytoplasm. Once in the cytosol, L. monocytogenes proliferates and infects adjacent cells through cell-to-cell spreading. Innate immune cells like neutrophils play an important role in the control of infection, yet the interaction between neutrophils, other host cells, and L. monocytogenes is not well understood. Neutrophils produce a high concentration and variety of antimicrobial molecules, including defensins and proteases; thus it is likely that these cells enhance the anti-listerial response of other host cells. This dissertation addresses if: i) human defensins, which can be released into the extracellular milieu by neutrophils, enable macrophages to control intracellular replication of L. monocytogenes; ii) L. monocytogenes is able to replicate in human neutrophils in a LLO-dependent manner as observed in macrophages; and iii) human neutrophils cooperate with macrophages to prevent L. monocytogenes replication in human macrophages. Addressing i), we found that the α-defensin HNP-1 (one of the most abundant proteins in neutrophil primary granules) cooperates with macrophages to inhibit L.
    [Show full text]
  • Structure, Function, and Evolution of Gga-Avbd11, the Archetype of the Structural Avian-Double- Β-Defensin Family
    Structure, function, and evolution of Gga-AvBD11, the archetype of the structural avian-double- β-defensin family Nicolas Guyota, Hervé Meudalb, Sascha Trappc, Sophie Iochmannd, Anne Silvestrec, Guillaume Joussetb, Valérie Labase,f, Pascale Reverdiaud, Karine Lothb,g, Virginie Hervéd, Vincent Aucagneb, Agnès F. Delmasb, Sophie Rehault-Godberta,1, and Céline Landonb,1 aBiologie des Oiseaux et Aviculture, Institut National de la Recherche Agronomique, Université de Tours, 37380 Nouzilly, France; bCentre de Biophysique Moléculaire, CNRS, 45071 Orléans, France; cInfectiologie et Santé Publique, Institut National de la Recherche Agronomique, Université de Tours, 37380 Nouzilly, France; dCentre d’Etude des Pathologies Respiratoires, INSERM, Université de Tours, 37032 Tours, France; ePhysiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, CNRS, Institut Français du Cheval et de l’Equitation, Université de Tours 37380 Nouzilly, France; fPôle d’Analyse et d’Imagerie des Biomolécules, Chirurgie et Imagerie pour la Recherche et l’Enseignement, Institut National de la Recherche Agronomique, Centre Hospitalier Régional Universitaire, Université de Tours, 37380 Nouzilly, France; and gUnité de Formation et de Recherche Sciences et Techniques, Université d’Orléans, 45100 Orléans, France Edited by Akiko Iwasaki, Yale University, New Haven, CT, and approved November 26, 2019 (received for review July 26, 2019) Outofthe14avianβ-defensins identified in the Gallus gallus genome, The sequence of Gga-AvBD11 contains 2 predicted β-defensin only 3 are present in the chicken egg, including the egg-specific avian motifs (Fig. 1) (7) and represents the sole double-sized defensin β-defensin 11 (Gga-AvBD11). Given its specific localization and its (9.3 kDa) among all 14 AvBDs reported in the chicken species.
    [Show full text]
  • Expression and Function of Host Defense Peptides at Inflammation
    International Journal of Molecular Sciences Review Expression and Function of Host Defense Peptides at Inflammation Sites Suhanya V. Prasad, Krzysztof Fiedoruk , Tamara Daniluk, Ewelina Piktel and Robert Bucki * Department of Medical Microbiology and Nanobiomedical Engineering, Medical University of Bialystok, Mickiewicza 2c, Bialystok 15-222, Poland; [email protected] (S.V.P.); krzysztof.fi[email protected] (K.F.); [email protected] (T.D.); [email protected] (E.P.) * Correspondence: [email protected]; Tel.: +48-85-7485483 Received: 12 November 2019; Accepted: 19 December 2019; Published: 22 December 2019 Abstract: There is a growing interest in the complex role of host defense peptides (HDPs) in the pathophysiology of several immune-mediated inflammatory diseases. The physicochemical properties and selective interaction of HDPs with various receptors define their immunomodulatory effects. However, it is quite challenging to understand their function because some HDPs play opposing pro-inflammatory and anti-inflammatory roles, depending on their expression level within the site of inflammation. While it is known that HDPs maintain constitutive host protection against invading microorganisms, the inducible nature of HDPs in various cells and tissues is an important aspect of the molecular events of inflammation. This review outlines the biological functions and emerging roles of HDPs in different inflammatory conditions. We further discuss the current data on the clinical relevance of impaired HDPs expression in inflammation and selected diseases. Keywords: host defense peptides; human antimicrobial peptides; defensins; cathelicidins; inflammation; anti-inflammatory; pro-inflammatory 1. Introduction The human body is in a constant state of conflict with the unseen microbial world that threatens to disrupt the host cell function and colonize the body surfaces.
    [Show full text]