A molecular assembly system for presentation of antigens on the surface of HBc virus-like particles

Virology

Volumn 435, Issue 2, 2013, Pages 293-300

  Blokhina, Elena A ^a   Kuprianov, Victor V ^a   Stepanova, Ludmila A ^b   Tsybalova, Ludmila M ^b   Kiselev, Oleg I ^b,c   Ravin, Nikolai V ^a,c   Skryabin, Konstantin G ^a,c  

^a INSTITUTE OF BIOENGINEERING   (Russian Federation)

^b N N BLOKHIN NATIONAL MEDICAL RESEARCH CENTER OF ONCOLOGY   (Russian Federation)

^c GenNanotech Ltd   (Russian Federation)

Author keywords

Hepatitis B virus; In vitro assembly; Influenza A virus; M2 protein; Vaccine; Virus like particle

Indexed keywords

3 MP HEPATITIS B CORE PROTEIN COMPLEX; ANTIGEN; EPITOPE; GLYCYLSERYLLEUCYLLEUCYLGLYCYLARGINYLMETHIONYLLYSYLGLYCYLALANINE; HYBRID PROTEIN; INFLUENZA VACCINE; INTERLEUKIN 2; PEPTIDE; PROTEIN M2; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN BINDING; ANTIGEN PRESENTATION; ARTICLE; CONTROLLED STUDY; HEPATITIS B VIRUS; IMMUNOGENICITY; IN VITRO STUDY; INFLUENZA; INFLUENZA VIRUS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN TARGETING; VIRUS PARTICLE;

AMINO ACID SEQUENCE; ANIMALS; ANTIGEN PRESENTATION; EPITOPES; HEPATITIS B CORE ANTIGENS; HEPATITIS B VIRUS; IMMUNIZATION; INFLUENZA VACCINES; MICE; MICE, INBRED BALB C; MOLECULAR SEQUENCE DATA; ORTHOMYXOVIRIDAE INFECTIONS; PEPTIDES; RECOMBINANT FUSION PROTEINS; VIRAL MATRIX PROTEINS; VIRION;

HEPATITIS B VIRUS; INFLUENZA A VIRUS; MUS;

EID: 84871690916     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2012.09.014     Document Type: Article

References (31)

1. Bachmann M.F., Rohrer U.H., Kundig T.M., Burki K., Hengartner H., Zinkernagel R.M. The influence of antigen organization on B cell responsiveness. Science 1993, 262(5138):1448-1451.
2. Bessa J., Schmitz N., Hinton H.J., Schwarz K., Jegerlehner A., Bachmann M.F. Efficient induction of mucosal and systemic immune responses by virus-like particles administered intranasally: implications for vaccine design. Eur. J. Immunol. 2008, 38:114-126.
3. Böttcher B., Tsuji N., Takahashi H., Dyson M.R., Zhao S., Crowther R.A., Murray K. Peptides that block hepatitis B virus assembly: analysis by cryomicroscopy, mutagenesis and transfection. EMBO J. 1998, 17:6839-6845.
4. De Filette M., Min Jou W., Birkett A., Lyons K., Schultz B., Tonkyro A., Resch S., Fiers W. Universal influenza A vaccine: optimization of M2-based constructs. Virology 2005, 337:149-161.
5. Denis J., Acosta-Ramirez E., Zhao Y., Hamelin M.E., Koukavica I., Baz M., Abed Y., Savard C., Pare C., Lopez Macias C., Boivin G., Leclerc D. Development of a universal influenza A vaccine based on the M2e peptide fused to the papaya mosaic virus (PapMV) vaccine platform. Vaccine 2008, 26:3395-3403.
6. Dyson M.R., Murray K. Selection of peptide inhibitors of interactions involved in complex protein assemblies: association of the core and surface antigens of hepatitis B virus. Proc. Natl. Acad. Sci. USA 1995, 92:2194-2198.
7. Fan J., Liang X., Horton M.S., Perry H.C., Citron M.P., Heidecker G.J., Fu T.M., Joyce J., Przysiecki C.T., Keller P.M., Garsky V.M., Ionescu R., Rippeon Y., Shi L., Chastain M.A., Condra J.H., Davies M.E., Liao J., Emini E.A., Shiver J.W. Preclinical study of influenza virus A M2 peptide conjugate vaccines in mice, ferrets, and rhesus monkeys. Vaccine 2004, 22(23-24):2993-3003.
8. Feng Zhang J.Q, Zhang M., Mozdzanowska K., Zharikova D., Hoff H., Wunner W., Couch R., Gerhard W. Influenza A virus infection engenders a poor antibody response against the ectodomain of matrix protein 2. Virol J. 2006, 3:102.
9. Fiers W., De Filette M., El Bakkouri K., Schepens B., Roose K., Schotsaert M., Birkett A., Saelens X. M2e-based universal influenza A vaccine. Vaccine 2009, 27:6280-6283.
10. Ganem D. Assembly of Hepadnaviral virions and subviral particles. Curr. Topics Microbiol. Immunol. 1991, 168:61-63.
11. Holsinger L.J., Lamb R.A. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 1991, 183:32-43.
12. Ionescu R.M., Przysiecki C.T., Liang X., Garsky V.M., Fan J., Wang B., Troutman R., Rippeon Y., Flanagan E., Shiver J., Shi L. Pharmaceutical and immunological evaluation of human papillomavirus virus like particle as an antigen carrier. J. Pharm. Sci. 2006, 95:70-79.
13. Ito T., Gorman O.T., Kawaoka Y., Bean W.J., Webster R.G. Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins. J. Virol. 1991, 65:5491-5498.
14. Jegerlehner A., Tissot A., Lechner F., Sebbel P., Erdmann I., Kundig T., Bachi T., Storni T., Jennings G., Pumpens P., Renner W.A., Bachmann M.F. A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses. Vaccine 2002, 20:3104-3112.
15. Karpenko L.I., Ivanisenko V.A., Pika I.A., Chikaev N.A., Eroshkin A.M., Veremeiko T.A., Ilyichev A.A. Insertion of foreign epitopes in HBcAg: how to make the chimeric particle assemble. Amino Acids 2000, 18:329-337.
16. Kawamura H., Rosenberg S., Berzofsky J.A. Immunization with antigen and interleukin-2 in vivo overcomes Ir gene low responsiveness. J. Exp. Med. 1985, 162:381-386.
17. Kotlyarov R.Yu., Kupriyanov V.V., Migunov A.I., Stepanova L.A., Tsybalova L.M., Kiselev O.I., Ravin N.V., Skryabin K.G. Development of recombinant vaccine against A(H1N1) 2009 influenza based on virus-like nanoparticles carrying the extracellular domain of M2 protein. Acta Naturae 2010, 2(5):75-80.
18. Kratz P.A., Bottcher B., Nassal M. Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc. Natl. Acad. Sci. USA 1999, 96:1915-1920.
19. Lane L.C. A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Anal. Biochem. 1978, 86(2):655-664.
20. Matić S., Rinaldi R., Masenga V., Noris E. Efficient production of chimeric human papillomavirus 16 L1 protein bearing the M2e influenza epitope in Nicotiana benthamiana plants. BMC Biotechnol. 2011, 11:106.
21. Meshcheryakova Y.A., El'darov M.A., Migunov A.I., Stepanova L.A., Repko I.A., Kiselev O.I., Lomonosov D.P., Skryabin K.G. Cowpea mosaic virus chimeric particles bearing ectodomain of matrix protein 2 (M2E) of influenza A virus: production and characteristics. Mol. Biol. (Moscow) 2009, 43:741-750.
22. Nakao M., Hazama M., Mayumi-Aono A., Hinuma S., Fujisawa Y. Immunotherapy of acute and recurrent herpes simplex virus type-2 infection with an adjuvant-free form of recombinant glycoprotein D-interleukin-2 fusion protein. J. Infect. Dis. 1994, 169:787-791.
23. Neirynck S., Deroo T., Saelens X., Vanlandschoot P., Min Jou W., Fiers W. A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat. Med. 1999, 5:1157-1163.
24. Pumpens P., Grens E. HBV core particles as a carrier for B cell/T cell epitopes. Intervirology 2001, 44:98-114.
25. Ravin N.V., Kotlyarov R.Y., Mardanova E.S., Kuprianov V.V., Migunov A.I., Stepanova L.A., Tsybalova L.M., Kiselev O.I., Skryabin K.G. Plant-produced recombinant influenza vaccine based on virus-like HBc particles carrying an extracellular domain of M2 protein. Biochemistry (Moscow) 2012, 77:33-40.
26. Salfeld J., Pfaff E., Noah M., Schaller H. Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J. Virol. 1989, 63:798-808.
27. Skamel C., Ploss M., Böttcher B., Stehle T., Wallich R., Simon M.M., Nassal M. Hepatitis B virus capsid-like particles can display the complete, dimeric outer surface protein C and stimulate production of protective antibody responses against Borrelia burgdorferi infection. J. Biol. Chem. 2006, 281(25):17474-17481.
28. Schotsaert M., De Filette M., Fiers W., Saelens X. Universal M2 ectodomain-based influenza A vaccines: preclinical and clinical developments. Expert Rev. Vaccines 2009, 8(4):499-508.
29. Taylor C.E. Cytokines as adjuvants for vaccines: antigen-specific responses differ from polyclonal responses. Infect. Immun. 1995, 63:3241-3244.
30. Vogel M., Vorreiter J., Nassal M. Quaternary structure is critical for protein display on capsid-like particles (CLPs): efficient generation of hepatitis B virus CLPs presenting monomeric but not dimeric and tetrameric fluorescent proteins. Proteins 2005, 58:478-488.
31. Wynne S.A., Crowther R.A., Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell. 1999, 3:771-780.