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Issue:ISSN 1000-7083
          CN 51-1193/Q
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Your Position :Home->Past Journals Catalog->2018 Vol.37 No.6

Synergistic Effect of Recombinant Yeast Co-Expressing Porcine Interleukin-2 and Fusion Antimicrobial Peptide Gene on Immunity and Growth of Mice
Author of the article:HU Bing1#, WU Xueying1#, MA Changjun1#, WAN Xiaoping1, XIAO Yongle1, CHEN Jianlin1, LI Jiangling2, LYU Xuebin2*, WANG Zezhou3*, GAO Rong1*
Author's Workplace:1. Key Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, Key Laboratory of Animal Disease Prevention and Food Safety of Sichuan Province, College of Life Sciences, Sichuan University, Chengdu 610065, China;
2. Sichuan Academy of Animal Science, Chengdu 610066, China;
3. Center for Animal Disease Control of Sichuan Province, Chengdu 610035, China
Key Words:porcine interleukin-2; fusion antimicrobial peptide; recombinant Pichiapastoris; mice; immunity
Abstract:To develop a novel and practicable immunomodulator, the recombinant Pichiapastoris to co-express porcine interleukin-2 and fusion antimicrobial peptide gene were constructed by 2A self-cleavage technique, and then fermented to feed ICR mice by gavage to evaluate its effects on the immunity and growth of mice via real time fluorescent quantitative PCR, ELISA and flow-cytometry. It was found that the expressed molecules of recombinant yeasts not only showed remarkable immunological bioactivity but also manifested obvious antimicrobial activity in vitro. The feeding of the yeast relatively improved the growth of mice in comparison to the control group (P<0.05). The contents of IgG, IgG1 and IgG2a were significantly increased in the yeast-treated groups (P<0.05), and the expression levels of the TLR1, TLR4, TLR6, TLR9, IL-7, IL-15, IL-23, CD62L, IL-2, IL-4, IL-6, IL-12, CRP4 and CAMP genes significantly increased in comparison to the control (P<0.05). Similarly, significant increases of the leukocytes, Th and Tc cells were detected in the blood of yeast-treated mice (P<0.05). Meanwhile, the mice of yeast-treated groups displayed markedly higher levels of immunity and survival rates than those of the control after challenged with virulent bacteria Escherichia coli and Staphylococcus aureus (P<0.05). These results suggest that the recombinant yeast can effectively enhance the immunity and growth of mice, and thus can be further developed as a promising safe and effective immunomodulator for livestock.
2018,37(6): 609-619 收稿日期:2017-11-16
分类号:Q78;Q95-33
基金项目:四川省科技项目(2016RZ0034,2017HH0023);四川省国际科技合作项目(2010HH0003);成都市科技攻关项目(2015NY-02-0028-NC);四川省重点动物育种项目(2016NYZ0042);科技部国际合作项目(2011DFA10101103)
作者简介:胡冰,女,硕士研究生,主要从事新型抗感染免疫分子制剂方面的研究,E-mail:578077613@qq.com;吴雪颖,女,硕士,医学遗传与分子生物学;马常俊,女,硕士,医学遗传与分子生物学
*通信作者:吕学斌,王泽洲,主要从事动物表观遗传学、动物分子免疫、疫苗研制、免疫应答调节和新型抗感染免疫分子制剂的研究,E-mail:lake96@qq.com;高荣,主要从事动物表观遗传学、动物分子免疫、疫苗研制、免疫应答调节和新型抗感染免疫分子制剂的研究,E-mail:gaorong96@163.com
参考文献:
Bals R, Wilson JM. 2003. Cathelicidins-a family of multifunctional antimicrobial peptides[J]. Cellular and Molecular Life Sciences, 60(4): 711-720.
Collins RA, Tayton HK, Gelder KI, et al. 1994. Cloning and expression of bovine and porcine interleukin-2 in baculovirus and analysis of species cross-reactivity[J]. Veterinary Immunology and Immunopathology, 40(4): 313-324.
Gordon YJ, Romanowski EG, Mcdermott AM. 2005. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs[J]. Current Eye Research, 30(7): 505-515.
Hsieh CS, Macatonia SE, Tripp CS, et al. 1993. Development of TH1 CD4+ cells through IL-12 produced by Listeria-induced macrophages[J]. Science, 260(5107): 547-549.
Isabel HP, Rüdiger K, Doris H, et al. 2012. PR-39, a porcine host defence peptide, is prominent in mucosa and lymphatic tissue of the respiratory tract in healthy pigs and pigs infected with Actinobacillus pleuropneumoniae[J]. BMC Research Notes, 5(1): 539.
Jenson AB, Ghim SJ, Sundberg JP. 2016. An inquiry into the causes and effects of the variolae vaccinae[J]. Experimental Dermatology, 25(3): 178-180.
Kawai T, Akira S. 2010. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors[J]. Nature Immunology, 11(5): 373-384.
Kayamuro H, Yoshioka Y, Abe Y, et al. 2010. Interleukin-1 family cytokines as mucosal vaccine adjuvants for induction of protective immunity against influenza virus[J]. Journal of Virology, 84(24): 12703-12712.
Kumar H, Kawai T, Akira S. 2009. Toll-like receptors and innate immunity[J]. Biochemical and Biophysical Research Communications, 388(4): 621-625.
Lawyer C, Pai S, Watabe M, et al. 1996. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from putative porcine precursor protein of a novel family of antibacterial peptides[J]. FEBS Letters, 390(1): 95-98.
Medzhitov R. 2001. Toll-like receptors and innate immunity[J]. Nature Reviews Immunology, 1: 135-145.
Niyonsaba F, Nagaoka I, Ogawa H, et al. 2009. Multifunctional antimicrobial proteins and peptides: natural activatorsof immune systems[J]. Current Pharmaceutical Design, 15(21): 2393-2413.
Park K, Oh D, Shin SY, et al. 2002. Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy[J]. Biochemical and Biophysical Research Communications, 290(1): 204-212.
Parronchi P, Macchia D, Piccinni MP, et al. 1991. Allergen- and bacterial antigen-specific T-cell clones established from atopic donors show a different profile of cytokine production[J]. Proceedings of the National Academy of Sciences of the United States of America, 88(10): 4538-4542.
Playfair JH, Souza JBD. 1987. Recombinant gamma interferon is a potent adjuvant for a malaria vaccine in mice[J]. Clinical and Experimental Immunology, 67(1): 5-10.
Plotkin SL, Plotkin SA. 1999. A short history of vaccination[M]//Plotkin SA, Orenstein WA, Offit PA. 2013. Vaccines 6th edition. Philadelphia, USA: Saunders: 1-12.
Romagnani. 1991. Human Th1 and Th2 subsets: doubt no more[J]. Immunology Today, 12(8): 256-257.
Sereti I, Anthony KB, Martinez-Wilson H, et al. 2004. IL-2 induced CD4+ T cell expansion in HIV-infected patients is associated with long-term decreases in T cell proliferation[J]. Blood, 104(3): 775-780.
Sher A, Coffman RL. 1992. Regulation of immunity to parasites by T cells and T cell-derived cytokines[J]. Annual Review of Immunology, 10(1): 385-409.
Shin MK, Kang ML, Jung MH, et al. 2013. Induction of protective immune responses against challenge of Actinobacillus pleuropneumoniae by oral administration with Saccharomyces cerevisiae expressing Apx toxins in pigs[J]. Veterinary Immunology and Immunopathology, 151(1-2): 132-139.
Smith KA. 1988. Interleukin-2: inception, impact, and implications[J]. Science, 240(4856): 1169-1176.
Stevceva L, Moniuszko M, Ferrari MG. 2006. Utilizing IL-12, IL-15 and IL-7 as mucosal vaccine adjuvants[J]. Letters in Drug Design & Discovery, 3(8): 586-592.
Szymczak AL, Vignali DA. 2005. Development of 2A peptide-based strategies in the design of multicistronic vectors[J]. Expert Opinion on Biological Therapy, 5(5): 627-638.
Tagliabue A, Boraschi D. 1993. Cytokines as vaccine adjuvants: interleukin 1 and its synthetic peptide 163-171[J]. Vaccine, 11(5): 594-595.
Thorne PS. 2007. The potential role of concentrated animal feeding operations in infectious disease epidemics andantibiotic resistance[J]. Environmental Health Perspectives, 115(2): 313-316.
Wuerth K, Hancock REW. 2011. New insights into cathelicidin modulation of adaptive immunity[J]. European Journal of Immunology, 41(10): 2817-2819.
Yang D, Chertov O, Oppenheim JJ. 2001. The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity[J]. Cellular and Molecular Life Sciences, 58(7): 978-989.
Yang ST, Shin SY, Kim YC, et al. 2002. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide[J]. Biochemical and Biophysical Research Communications, 296(5): 1044-1050.
Yang ST, Song YS, Lee CW, et al. 2003. Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure[J]. FEBS Letters, 540(1): 229-233.
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