اخبار و اعلانات

 آمار

تعداد نشریات286
تعداد نشریات سازمان84
تعداد شماره‌ها2,829
تعداد مقالات32,098
تعداد مشاهده مقاله40,864,084
تعداد دریافت فایل اصل مقاله18,113,701
Forouharmehr, Ali, Banan, A, Mousavi, S. M, Jaydari, A. (1400). Development of a Novel Multi-Epitope Vaccine Candidate against Streptococcus Iniae Infection in Fish: An Immunoinformatics Study. سامانه مدیریت نشریات علمی, 77(1), 45-56. doi: 10.22092/ari.2021.353377.1601
Ali Forouharmehr; A Banan; S. M Mousavi; A Jaydari. "Development of a Novel Multi-Epitope Vaccine Candidate against Streptococcus Iniae Infection in Fish: An Immunoinformatics Study". سامانه مدیریت نشریات علمی, 77, 1, 1400, 45-56. doi: 10.22092/ari.2021.353377.1601
Forouharmehr, Ali, Banan, A, Mousavi, S. M, Jaydari, A. (1400). 'Development of a Novel Multi-Epitope Vaccine Candidate against Streptococcus Iniae Infection in Fish: An Immunoinformatics Study', سامانه مدیریت نشریات علمی, 77(1), pp. 45-56. doi: 10.22092/ari.2021.353377.1601
Forouharmehr, Ali, Banan, A, Mousavi, S. M, Jaydari, A. Development of a Novel Multi-Epitope Vaccine Candidate against Streptococcus Iniae Infection in Fish: An Immunoinformatics Study. سامانه مدیریت نشریات علمی, 1400; 77(1): 45-56. doi: 10.22092/ari.2021.353377.1601

Development of a Novel Multi-Epitope Vaccine Candidate against Streptococcus Iniae Infection in Fish: An Immunoinformatics Study

Archives of Razi Institute
مقاله 8، دوره 77، شماره 1، فروردین و اردیبهشت 2022، صفحه 45-56    اصل مقاله (1.39 M)
نوع مقاله: Original Articles
شناسه دیجیتال (DOI): 10.22092/ari.2021.353377.1601
نویسندگان
Ali Forouharmehr* 1؛ A Banan2؛ S. M Mousavi3؛ A Jaydari4
1Department of animal science, Faculty of agriculture, Lorestan university, Khorramabad, Iran
2Department of Marine Science, Faculty of Agriculture, Lorestan University, Khorramabad, Iran
3Department of Animal Science, Faculty of Agriculture, Lorestan University, Khorramabad, Iran
4Department of Pathobiology, Faculty of Veterinary Medicine, Lorestan University, Khorramabad, Iran
چکیده
Streptococcus iniae infection is recognized as a disease with substantial economic losses, infecting a wide range of fish species. The limitations of current vaccines and strategies have led to the identification of new methods to control this disease. Multi-epitope vaccines which employ various immunogenic proteins can be promising. The current research project aimed to design an efficient multi-epitope vaccine against Streptococcus iniae infection in fish. To this end, six immunogenic proteins of Streptococcus iniae, including FBA, ENO, Sip11, GAPDH, MtsB, and SCPI proteins, were applied for epitope prediction. The best B cell, T cell, and IFNγ epitopes of the immunogenic proteins, as well as interleukin-8, were used to construct a multi-epitope vaccine. Thereafter, different parameters of the designed vaccine, including physicochemical features, antigenicity, secondary structure, and tertiary structure, were evaluated. Moreover, the interaction of the interleukin-8 domain of the designed vaccine and its receptor was investigated by molecular docking strategy. Finally, nucleotide sequence of the vaccine was adapted to express in Escherichia coli. The results of the present study pointed out that the designed vaccine was a stable vaccine with molecular weight and antigenicity score of 45 kDa and 0.936, respectively. Furthermore, the structure analysis results revealed that the designed vaccine contained 23.49% alpha helix, with 90.5% residues in favored region. Finally, it was demonstrated that the interleukin-8 domain of the designed vaccine could be successfully docked to its receptor with the lowest energy of -1020.9. Based on the obtained results, it seems that the designed vaccine can be an efficient candidate to prevent Streptococcus iniae infection in fish.
کلیدواژه‌ها
Multi-epitope scaffold؛ Streptococcus iniae؛ Immunoinformatics؛ Immunogenic proteins
عنوان مقاله [English]
توسعه یک واکسن چند اپیتوپی جدید علیه عفونت استرپتوکوکوس اینیایی در ماهی: یک مطالعه ایمنوانفورماتیک
چکیده [English]
استرپتوکوکوس اینیایی به عنوان یک عامل عفونی سبب ایجاد خسارات اقتصادی زیادی می‌شود که می‌تواند طیف وسیعی از گونه‌های ماهی را آلوده کند. محدودیت‌ها که در مورد واکسن های رایج و استراتژی‌های موجود وجود دارد منجر به شناسایی روش‌های جدیدی برای کنترل این بیماری می‌شود. در این رابطه، واکسن‌های مبتنی بر چند اپی توپ که بر پایه استفاده از پروتئین‌های مختلف ایمنوژنیک هستند می‌توانند امیدوار کننده باشند. مطالعه حاضر در مورد مهندسی یک واکسن چند اپی-توپی کارآمد علیه عامل استرپتوکوکوس اینیایی است. در این ارتباط، شش پروتئین ایمنوژنیک از استرپتوکوکوس اینیایی که شامل پروتئین هایFBA ، ENO، Sip11،GAPDH ، MtsB و SCPI بود برای پیش بینی اپی توپ استفاده شد. برای ساخت واکسن چند اپی توپی از بهترین اپی‌توپ‌های سلول B ، سلول T و IFNγ پروتئین های مذکور به همراه اینترلوکین-8 استفاده شد. سپس، پارامترهای مختلفی از واکسن طراحی شده از جمله ویژگی‌های فیزیکوشیمیایی، آنتی ژنسیتی، ساختارهای ثانویه و ساختار سوم مورد ارزیابی قرار گرفت. علاوه بر این، تعامل بین دمین اینترلوکین-8 از واکسن مهندسی شده و گیرنده آن توسط فرایند داکینگ مولکولی بررسی شد. سرانجام، توالی نوکلئوتیدی واکسن طراحی شده برای بیان در باکتری اشرشیاکلی سازگار شد. نتایج بدست امده از این پژوهش نشان داد که واکسن طراحی شده با وزن مولکولی 45 کیلو دالتون و اسکور آنتی ژنسیتی 936/0، یک واکسن پایدار است. همچنین، نتایج تجزیه و تحلیل ساختار نشان داد که واکسن طراحی شده شامل 49/23٪ مارپیچ آلفا است که 5/90٪ اسید آمینه‌ها در منطقه مطلوب واقع شده‌اند. در نهایت نیز نتایج داکینگ مولکولی نشان دادکه دمین اینترلوکین-8 از واکسن مهندسی شده می‌تواند با کمترین انرژی( 9/1020- ) به گیرنده خود متصل شود. بر اساس نتایج مستخرج از این مطالعه به نظر می‌رسد که واکسن طراحی شده می-تواند کاندید کارآمدی برای جلوگیری از عفونت استرپتوکوکوس اینیایی باشد
کلیدواژه‌ها [English]
سازه چند اپیتوپی, استرپتوکوکوس اینیایی, ایمنوانفورماتیک, پروتئین‌های ایمنوژنیک
سایر فایل های مرتبط با مقاله
مراجع
  1. Sheng X, Liu M, Liu H, Tang X, Xing J, Zhan W. Identification of immunogenic proteins and evaluation of recombinant PDHA1 and GAPDH as potential vaccine candidates against Streptococcus iniae infection in flounder (Paralichthys olivaceus). PloS One. 2018;13(5):0195450.
  2. El Aamri F, Padilla D, Acosta F, Caballero M, Roo J, Bravo J, et al. First report of Streptococcus iniae in red porgy (Pagrus pagrus, L.). J Fish Dis. 2010;33(11):901-5.
  3. Eldar A, Frelier PF, Assenta L, Varner PW, Lawhon S, Bercovier H, et al. Streptococcus shiloi, the name for an agent causing septicemic infection in fish, is a junior synonym of Streptococcus iniae. Int J Syst Evol Microbiol. 1995;45(4):840-2.
  4. Facklam R, Elliott J, Shewmaker L, Reingold A. Identification and characterization of sporadic isolates of Streptococcus iniae isolated from humans. J Clin Microbiol. 2005;43(2):933-7.
  5. Agnew W, Barnes AC. Streptococcus iniae: an aquatic pathogen of global veterinary significance and a challenging candidate for reliable vaccination. Vet Microbiol. 2007;122(1-2):1-15.
  6. Goh SH, Driedger D, Gillett S, Low DE, Hemmingsen SM, Amos M, et al. Streptococcus iniae, a human and animal pathogen: specific identification by the chaperonin 60 gene identification method. J Clin Microbiol. 1998;36(7):2164-6.
  7. Bromage Ea, Owens L. Infection of barramundi Lates calcarifer with Streptococcus iniae: effects of different routes of exposure. Dis Aquat Organ. 2002;52(3):199-205.
  8. Evans JJ, Shoemaker CA, Klesius PH. Experimental Streptococcus iniae infection of hybrid striped bass (Morone chrysops× Morone saxatilis) and tilapia (Oreochromis niloticus) by nares inoculation. Aquaculture. 2000;189(3-4):197-210.
  9. Perera RP, Fiske RA, Johnson SK. Histopathology of Hybrid Tilapias Infected witha Biotype of Streptococcus iniae. J Aquat Anim Health. 1998;10(3):294-9.
  10. Ma J, Bruce TJ, Jones EM, Cain KD. A review of fish vaccine development strategies: Conventional methods and modern biotechnological approaches. Microorganisms. 2019;7(11):569.
  11. Sneeringer S, Bowman M, Clancy M. The US and EU Animal Pharmaceutical Industries in the Age of Antibiotic Resistance. 2019.
  12. Horzinek M, Schijns V, Denis M, Desmettre P, Babiuk L. General description of vaccines. Vet Vaccine. 1997:131-52.
  13. Gudding R, Goodrich T. The history of fish vaccination. Fish Vaccine. 2014:1-11.
  14. Snieszko S, Friddle S. Prophylaxis of furunculosis in brook trout (Salvelinus fontinalis) by oral immunization and sulfamerazine. Progress Fish Cult. 1949;11(3):161-8.
  15. Hansson M, Nygren PAk, Sta˚ hl S, biochemistry a. Design and production of recombinant subunit vaccines. Biotechnol Appl Biochem. 2000;32(2):95-107.
  16. Shams N, Gandabeh ZS, Nazifi N, Forouharmehr A, Jaydari A, Rashidian E, et al. Computational Design of Different Epitope-Based Vaccines Against Salmonella typhi. Int J Pept Res Ther. 2019:1-13.
  17. Slingluff Jr CL. The present and future of peptide vaccines for cancer: single or multiple, long or short, alone or in combination? J Cancer. 2011;17(5):343.
  18. Nazifi N, Mousavi SM, Moradi S, Jaydari A, Jahandar MH, Forouharmehr A. In silico B cell and T cell epitopes evaluation of lipL32 and OmpL1 proteins for designing a recombinant multi-epitope vaccine against leptospirosis. Int J Infect. 2018;5(2).
  19. Jebastin T, Narayanan S, Chemistry. In silico epitope identification of unique multidrug resistance proteins from Salmonella Typhi for vaccine development. Comput Biol Chem. 2019;78:74-80.
  20. Saadi M, Karkhah A, Nouri HR, Genetics, Evolution. Development of a multi-epitope peptide vaccine inducing robust T cell responses against brucellosis using immunoinformatics based approaches. Infect Genet Evol. 2017;51:227-34.
  21. Rashidian E, Gandabeh ZS, Forouharmehr A, Nazifi N, Shams N, Jaydari A, et al. Immunoinformatics Approach to Engineer a Potent Poly-epitope Fusion Protein Vaccine Against Coxiella burnetii. Int J Pept Res. 2020:1-11.
  22. Hajissa K, Zakaria R, Suppian R, Mohamed Z. Immunogenicity of Multiepitope Vaccine Candidate against Toxoplasma gondii Infection in BALB/c Mice. Iran J Parasitol. 2018;13(2):215.
  23. Zhang L, immunology m. Multi-epitope vaccines: a promising strategy against tumors and viral infections. Cell Mol Immunol. 2018;15(2):182-4.
  24. Jaydari A, Forouharmehr A, Nazifi N. Determination of immunodominant scaffolds of Com1 and OmpH antigens of Coxiella burnetii. Microb Pathog. 2019;126:298-309.
  25. Secombes C, Zou J, Bird S. Fish cytokines: discovery, activities and potential applications. Fish Defenses. 2009;1:1-36.
  26. Consortium U. UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019;47(1):506-15.
  27. Vita R, Mahajan S, Overton JA, Dhanda SK, Martini S, Cantrell JR, et al. The immune epitope database (IEDB): 2018 update. Nucleic Acids Res. 2019;47(1): 339-43.
  28. Saha S, Raghava GPS. Prediction of continuous B‐cell epitopes in an antigen using recurrent neural network. Proteins: Struct, Funct, Bioinf. 2006;65(1):40-8.
  29. Doytchinova IA, Flower DR. VaxiJen: a server for prediction of protective antigens, tumour antigens and subunit vaccines. BMC Bioinf. 2007;8(1):1-7.
  30. Dhanda SK, Vir P, Raghava GP. Designing of interferon-gamma inducing MHC class-II binders. Biol Direct. 2013;8(1):1-15.
  31. Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. The proteomics protocols handbook. 2005:571-607.
  32. Molero-Abraham M, Lafuente EM, Flower DR, Reche PA. Selection of conserved epitopes from hepatitis C virus for pan-populational stimulation of T-cell responses. Clin Dev Immunol. 2013;2013.
  33. Sen TZ, Jernigan RL, Garnier J, Kloczkowski A. GOR V server for protein secondary structure prediction. Bioinformatics. 2005;21(11):2787-8.
  34. Yang J, Zhang Y. I-TASSER server: new development for protein structure and function predictions. Nucleic Acids Res. 2015;43(1):174-81.
  35. Heo L, Park H, Seok C. GalaxyRefine: Protein structure refinement driven by side-chain repacking. Nucleic Acids Res. 2013;41(1):384-8.
  36. Williams CJ, Headd JJ, Moriarty NW, Prisant MG, Videau LL, Deis LN, et al. MolProbity: More and better reference data for improved all‐atom structure validation. Protein Sci. 2018;27(1):293-315.
  1. Wiederstein M, Sippl MJ. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 2007;35(2):407-10.
  2. Eisenberg D, Lüthy R, Bowie J. VERIFY3D: assessment of protein models with three-dimensional profiles. InMethods in enzymology 1997 Jan 1 (Vol. 277, pp. 396-404). Academic Press DOI.10:s0076-6879.
  3. Kozakov D, Hall DR, Xia B, Porter KA, Padhorny D, Yueh C, et al. The ClusPro web server for protein–protein docking. Nat Protoc. 2017;12(2):255.
  4. Grote A, Hiller K, Scheer M, Münch R, Nörtemann B, Hempel DC, et al. JCat: a novel tool to adapt codon usage of a target gene to its potential expression host. Nucleic Acids Res. 2005;33(2):526-31.
  5. Schrodinger L. The PyMOL molecular graphics system. Version. 2010;1(5).
  6. Wang E, Long B, Wang K, Wang J, He Y, Wang X, et al. Interleukin-8 holds promise to serve as a molecular adjuvant in DNA vaccination model against Streptococcus iniae infection in fish. Oncotarget. 2016;7(51):83938.
  7. Evensen Ø, Leong J-AC, immunology s. DNA vaccines against viral diseases of farmed fish. Fish Shellfish Immunol. 2013;35(6):1751-8.
  8. Goumari MM, Farhani I, Nezafat N, Mahmoodi S. Multi-Epitope Vaccines (MEVs), as a Novel Strategy Against Infectious Diseases. Curr Proteomics. 2020;17(5):354-64.
  1. Alspach E, Lussier DM, Schreiber RD. Interferon γ and its important roles in promoting and inhibiting spontaneous and therapeutic cancer immunity. Cold Spring Harb Perspect Biol. 2019;11(3):028480.
  2. Jaydari A, Nazifi N, Forouharmehr A. Computational design of a novel multi-epitope vaccine against Coxiella burnetii. Hum Immunol. 2020.
  3. Validi M, Karkhah A, Prajapati VK, Nouri HR. Immuno-informatics based approaches to design a novel multi epitope-based vaccine for immune response reinforcement against Leptospirosis. Mol Immunol. 2018;104:128-38.
  4. Gamage DG, Gunaratne A, Periyannan GR, Russell TG. Applicability of instability index for in vitro protein stability prediction. Protein Pept Lett. 2019;26(5):339-47.
  5. Guruprasad K, Reddy BB, Pandit MW. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. Des. Sel. 1990;4(2):155-61.
50.          Forouharmehr A, Nassiri M, Ghovvati S, Javadmanesh A. Evaluation of different signal peptides for secretory production of recombinant bovine pancreatic ribonuclease A in gram negative bacterial system: an in silico study. Curr Proteomics. 2018;15(1):24-33.

آمار
تعداد مشاهده مقاله: 1,920
تعداد دریافت فایل اصل مقاله: 674


counter
سامانه مدیریت نشریات علمی. قدرت گرفته از سیناوب