全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...
PLOS ONE  2012 

A Cucumber Mosaic Virus Based Expression System for the Production of Porcine Circovirus Specific Vaccines

DOI: 10.1371/journal.pone.0052688

Full-Text   Cite this paper   Add to My Lib

Abstract:

Potential porcine circovirus type 2 (PCV2) capsid protein epitopes, suitable for expression on the surface of cucumber mosaic virus (CMV) particles were determined by a thorough analysis of the predicted PCV capsid protein structure. The ab initio protein structure prediction was carried out with fold recognition and threading methods. The putative PCV epitopes were selected on the basis of PCV virion models and integrated into the plant virus coat protein, after amino acid position 131. The recombinants were tested for infectivity and stability on different Nicotiana species and stable recombinant virus particles were purified. The particles were tested for their ability to bind to PCV induced porcine antibodies and used for specific antibody induction in mice and pigs. The results showed that PCV epitopes expressed on the CMV surface were recognized by the porcine antibodies and they were also able to induce PCV specific antibody response. Challenge experiment with PCV2 carried out in immunized pigs showed partial protection against the infection. Based on these results it was concluded that specific antiviral vaccine production for the given pathogen was feasible, offering an inexpensive way for the mass production of such vaccines.

References

[1]  Brun A, Barcena J, Blanco E, Borrego B, Dory D, et al. (2011) Current strategies for subunit and genetic viral veterinary vaccine development. Virus Research 157: 1–12.
[2]  Mason HS, Lam DMK, Arntzen CJ (1992) Expression of hepatitis B surface antigen in transgenic plants. Proceedings of the National Academy of Sciences of the United States of America 89: 11745–11749.
[3]  Richter LJ, Thanavala Y, Arntzen CJ, Mason HS (2000) Production of hepatitis B surface antigen in transgenic plants for oral immunization. Nat Biotechnol 18: 1167–1171.
[4]  Mason HS, Ball JM, Shi JJ, Jiang X, Estes MK, et al. (1996) Expression of Norwalk virus capsid protein in transgenic tobacco and potato and its oral immunogenicity in mice. P Natl Acad Sci USA 96: 5335–5340.
[5]  Carrillo C, Wigdorovitz A, Oliveros JC, Zamorano PI, Sadir AM, et al. (1998) Protective immune response to foot-and-mouth disease virus with VP1 expressed in transgenic plants. J Virol 72: 1688–1690.
[6]  Tuboly T, Yu W, Bailey A, Degrandis S, Du S, et al. (2000) Immunogenicity of porcine transmissible gastroenteritis virus spike protein expressed in plants. Vaccine 18: 2023–2028.
[7]  Gil F, Titarenko E, Terrada E, Arcalis E, Escribano JM (2006) Successful oral prime-immunization with VP60 from rabbit haemorrhagic disease virus produced in transgenic plants using different fusion strategies. Plant Biotechnol J 4: 135–143.
[8]  Loza-Rubio E, Rojas-Anaya E (2010) Vaccine production in plant systems – an aid to the control of viral diseases in domestic animals: a review. Acta Veterinaria Hungarica 58: 511–522.
[9]  Streatfield SJ, Jilka JM, Hood EE, Turner DD, Bailey MR, et al. (2001) Plant-based vaccines: unique advantages. Vaccine 19: 2742–2748.
[10]  Streatfield SJ (2005) Plant-based vaccines for animal health. Revue Scientifique Et Technique-Office International Des Epizooties 24: 189–199.
[11]  Santi L (2009) Plant derived veterinary vaccines. Veterinary Research Communications 33: S61–S66.
[12]  Porta C, Spall VE, Loveland J, Johnsosn JE, Barker PJ, et al. (1994) Development of cowpea mosaic virus as a high yielding system for the presentation of foreign peptides. Virology 202: 949–955.
[13]  Dalsgaard K, Uttenhalt á, Jones TD, Xu F, Merryweather A, et al. (1997) Plant derived vaccine projects target animals against a virus disease. Nat Biotechnol 15: 248–252.
[14]  Gopinath K, Wellink J, Porta C, Taylor KM, Lomonossoff GP, et al. (2000) Engineering Cowpea mosaic virus RNA-2 into a vector to express heterologous proteins in plants. Virology 267: 159–173.
[15]  Lomonossoff GP, Johnson JE (1991) The synthesis and structure of comovirus capsids. Prog Biophys Mol Bio 55: 107–137.
[16]  Stauffacher CV, Usha R, Harrington M, Schmidt T, Hosur M, et al. (1987) The structure of cowpea mosaic virus at 3.5 ?. In: Moras D, Drenth J, Strandberg B, Suck D, Wilson K, editors. Crystallography in Molecular biology. New York: Plenum Press. 293–308.
[17]  Lin T, Chen Z, Usha R, Stauffacher CV, Dai JB, et al. (1999) The refined crystal structure of cowpea mosaic virus at 2.8 ? resolution. Virology 265: 20–34.
[18]  Awram P, Gardner RC, Forster RL, Bellamy AR (2002) The potential of plant virus vectors and transgenic plants for subunit vaccine production. Adv Virus Res 58: 81–124.
[19]  Nuzzaci M, Piazzolla G, Vitti A, Lapelosa M, Tortorella C, et al. (2007) Cucumber mosaic virus as a presentation system for a double hepatitis C virus-derived epitope. Archives Of Virology 152: 915–928.
[20]  Vitti A, Piazzolla G, Condelli V, Nuzzaci M, Lanorte MT, et al. (2010) Cucumber mosaic virus as the expression system for a potential vaccine against Alzheimer’s disease. 169: 332–340.
[21]  Mahé D, Blanchard P, Truong C, Arnauld C, Le Cann P, et al. (2000) Differential recognition of ORF2 protein from type 1 and type 2 porcine circoviruses and identification of immunorelevant epitopes. J Gen Virol 1: 1815–1824.
[22]  Lekcharoensuk P, Morozov I, Paul PS, Thangthumniyom N, Wajjawalku W, et al. (2004) Epitope mapping of the major capsid protein of type 2 porcine circovirus (PCV2) by using chimeric PCV1 and PCV2. J Virol 78: 8135–8145.
[23]  Shang SB, Jin JL, Jiang X, Zhoua JY, Zhanga X, et al. (2009) Fine mapping of antigenic epitopes on capsid proteins of porcine circovirus and antigenic phenotype of porcine circovirus Type 2. Res Vet Sci 84: 150–157.
[24]  Tischer I, Rasch R, Tochtermann G (1974) Characterization of papovavirus- and picornavirus-like particles in permanent pig kidney cell lines. Zentralbl Bakteriol Org A 226: 153–176.
[25]  Segalés J, Allan GM, Domingo M (2005) Porcine circovirus diseases. Anim Health Res Rev 6: 119–142.
[26]  Kristensen CS, Baadsgaard NP, Toft N (2011) A meta-analysis comparing the effect of PCV2vaccines on average daily weight gain and mortality rate in pigs from weaning to slaughter. Prev Vet Med 98: 250–258.
[27]  Gellért á, Salánki K, Náray-Szabó G, Balázs E (2006) Homology modelling and protein structure based functional analysis of five cucumovirus coat proteins. Journal of Molecular Graphics and Modelling 24: 319–327.
[28]  Llamas S, Moreno IM, García-Arénal F (2006) Analysis of the viability of coat-protein hybrids between Cucumber mosaic virus and Tomato aspermy virus. J Gen Virol 87: 2085–2088.
[29]  Pacios LF, García-Arénal F (2006) Comparison of properties of particles of Cucumber mosaic virus and Tomato aspermy virus based on the analysis of molecular surfaces of capsids. Journal of General Virology 87: 2073–2083.
[30]  Thompson JR, Doun S, Perry KL (2006) Compensatory Capsid Protein Mutations in Cucumber Mosaic Virus Confer Systemic Infectivity in Squash (Cucurbitapepo). J Virol 80: 7740–7743.
[31]  Salánki K, Kiss L, Gellért á, Balázs E (2011) Identification a coat protein region of Cucumber mosaic virus (CMV) essential for long-distance movement in cucumber Arch Virol. 156: 2279–2283.
[32]  Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40.
[33]  Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols 5: 725–738.
[34]  Schneidman-Duhovny D, Inbar Y, Nussinov R, Wolfson HJ (2005) Geometry based flexible and symmetric protein docking. Proteins 60: 224–231.
[35]  Humphrey W, Dalke A, Schulten K (1996) VMD - Visual Molecular Dynamics. Journal of Molecular Graphics 14: 33–38.
[36]  Salánki K, Carrère I, Jacquemond M, Balázs E, Tepfer M (1997) Biological properties of pseudorecombinant and recombinant strains created with cucumber mosaic virus and tomato aspermy virus. J Virol 71: 3597–3602.
[37]  Shankarappa B, Vijayananda K, Ehrlich GD (1992) SILMUT: a computer program for the identification of regions suitable for silent mutagenesis to introduce restriction enzyme recognition sequences. Biotechniques 12: 882–884.
[38]  White JL, Kaper JM (1989) A simple method for detection of viral satellite RNAs in small tissue samples. Journal of Virological Methods 23: 83–94.
[39]  Peden KW, Symons RH (1973) Cucumber mosaic virus contains a functionally divided genome. Virology 53: 487–492.
[40]  Sambrook J, Fritsch EF, Maniatis T (1989) Molecular Cloning: a laboratory manual: Cold Spring Harbor Laboratory Press.
[41]  Lot H, Marrou J, Quiot JB, Esvan C (1972) Contribution á l’étude du virus de la mosaique du concombre (CMV). I. Méthode de purification rapide du virus. Ann Phytopath 4: 25–38.
[42]  Cságola A (2009) Epidemiological examination of porcine circoviruses: Szent István University, Faculty of Veterinary Science.
[43]  Patterson AR, Ramamoorthy S, Madson DM, Meng XJ, Halbur PG, et al. (2011) Shedding and infection dynamics of porcine circovirus type 2 (PCV2) after experimental infection. Veterinary Microbiology 149: 91–98.
[44]  Khayat R, Brunn N, Speir JA, Hardham JM, Ankenbauer RG, et al. (2011) The 2.3-Angstrom Structure of Porcine Circovirus 2. J Virol 85: 7856–7862.
[45]  Segalés J (2012) Porcine circovirus type 2 (PCV2) infections: Clinical signs, pathology and laboratory diagnosis. Virus Research 164: 10–19.
[46]  Truong C, Mahé D, Blanchard P, Le Dimna M, Madec F, et al. (2011) Identification of an immunorelevant ORF2 epitope from porcine circovirus type 2 as a serological marker for experimental and natural infection. Arch Virol 46: 1197–1211.
[47]  Gilpin DF, McCullough K, Meehan BM, McNeilly F, McNair I, et al. (2003) In vitro studies on the infection and replication of porcine circovirus type 2 in cells of the porcine immune system. Veterinary Immunology and Immunopathology 94: 149–161.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133