Highly effective soluble and bacteriophage T4 nanoparticle plague vaccines against Yersinia pestis

Methods in Molecular Biology

Volumn 1403, Issue , 2016, Pages 499-518

  Tao, Pan ^a   Mahalingam, Marthandan ^a   Rao, Venigalla B ^a  

^a NONE

Author keywords

Bacteriophage T4; F1V; Nanoparticle vaccine; Yersinia pestis

Indexed keywords

ANTIGEN; CAPSID PROTEIN; HYBRID PROTEIN; NANOPARTICLE; PLAGUE VACCINE; SUBUNIT VACCINE; BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

CD4+ T LYMPHOCYTE; CELLULAR IMMUNITY; DRUG EFFICACY; ENTEROBACTERIA PHAGE T4; ESCHERICHIA COLI; IMMUNIZATION; IMMUNOGENICITY; MUTATION; NONHUMAN; PLAGUE; PROTEIN PURIFICATION; VIRUS CAPSID; WILD TYPE; YERSINIA PESTIS; ANIMAL; BETA SHEET; CHEMISTRY; GENETICS; IMMUNOLOGY; MOLECULAR MODEL; MOUSE; PROTEIN ENGINEERING; SOLUBILITY;

ANIMALS; BACTERIAL PROTEINS; BACTERIOPHAGE T4; MICE; MODELS, MOLECULAR; MUTATION; NANOPARTICLES; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SOLUBILITY; YERSINIA PESTIS;

EID: 84963811974     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-3387-7_28     Document Type: Chapter

References (31)

1. Wagner DM et al (2014) Yersinia pestis and the plague of Justinian 541–543 AD: a genomic analysis. Lancet Infect Dis 14:319–326
2. Guernier V et al (2014) Fleas of small mammals on Reunion Island: diversity, distribution and epidemiological consequences. PLoS Negl Trop Dis 8(9), e3129
3. Smiley ST (2008) Current challenges in the development of vaccines for pneumonic plague. Expert Rev Vaccines 7:209–221
4. Zilinskas RA (2006) The anti-plague system and the Soviet biological warfare program. Crit Rev Microbiol 32:47–64
5. Sha J et al (2013) Deletion of Braun lipoprotein encoding gene and altering the function of lipopolysaccharide attenuate plague bacterium. Infect Immun 81:815–828
6. Rosenzweig JA et al (2011) Progress on plague vaccine development. Appl Microbiol Biotechnol 91:265–286
7. Zavialov AV et al (2003) Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113:587–596
8. Stenseth NC et al (2008) Plague: past, present, and future. PLoS Med 5(1), e3
9. Derewenda U et al (2004) The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure 12:301–306
10. Williamson ED et al (1995) A new improved sub-unit vaccine for plague: the basis of protection. FEMS Immunol Med Microbiol 12: 223–230
11. Anderson GW Jr, Heath DG, Bolt CR, Welkos SL, Friedlander AM (1998) Short- and longterm efficacy of single-dose subunit vaccines against Yersinia pestis in mice. Am J Trop Med Hyg 58:793–799
12. Heath DG et al (1998) Protection against experimental bubonic and pneumonic plague by a recombinant capsular F1-V antigen fusion protein vaccine. Vaccine 16:1131–1137
13. Goodin JL et al (2007) Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague. Protein Expr Purif 53:63–79
14. Goodin JL et al (2011) Purification and characterization of a recombinant Yersinia pestis V-F1 “Reversed” fusion protein for use as a new subunit vaccine against plague. Protein Expr Purif 76:136–144
15. Mizel SB et al (2009) Flagellin-F1-V fusion protein is an effective plague vaccine in mice and two species of nonhuman primates. Clin Vaccine Immunol 16:21–28
16. Powell BS et al (2005) Design and testing for a nontagged F1-V fusion protein as vaccine antigen against bubonic and pneumonic plague. Biotechnol Prog 21:1490–1510
17. Parent MA et al (2005) Cell-mediated protection against pulmonary Yersinia pestis infection. Infect Immun 73:7304–7310
18. Tao P et al (2013) Mutated and bacteriophage T4 nanoparticle arrayed F1-V immunogens from Yersinia pestis as next generation plague vaccines. PLoS Pathog 9(7), e1003495
19. Li Q, Shivachandra SB, Leppla SH, Rao VB (2006) Bacteriophage T4 capsid: a unique platform for efficient surface assembly of macromolecular complexes. J Mol Biol 363: 577–588
20. Sathaliyawala T et al (2006) Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: a novel in vitro approach to construct multicomponent HIV vaccines. J Virol 80:7688–7698
21. Andrews GP, Heath DG, Anderson GW Jr, Welkos SL, Friedlander AM (1996) Fraction 1 capsular antigen (F1) purification from Yersinia pestis CO92 and from an Escherichia coli recombinant strain and efficacy against lethal plague challenge. Infect Immun 64:2180–2187
22. Miller J et al (1998) Macromolecular organisation of recombinant Yersinia pestis F1 antigen and the effect of structure on immunogenicity. FEMS Immunol Med Microbiol 21:213–221
23. Musson JA et al (2006) Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes. J Biol Chem 281:26129–26135
24. Li Q, Shivachandra SB, Zhang Z, Rao VB (2007) Assembly of the small outer capsid protein, Soc, on bacteriophage T4: a novel system for high density display of multiple large anthrax toxins and foreign proteins on phage capsid. J Mol Biol 370:1006–1019
25. Shivachandra SB et al (2007) Multicomponent anthrax toxin display and delivery using bacteriophage T4. Vaccine 25:1225–1235
26. Black LW, Rao VB (2012) Structure, assembly, and DNA packaging of the bacteriophage T4 head. Adv Virus Res 82:119–153
27. Fokine A et al (2004) Molecular architecture of the prolate head of bacteriophage T4. Proc Natl Acad Sci U S A 101:6003–6008
28. Ishii T, Yanagida M (1977) The two dispensable structural proteins (soc and hoc) of the T4 phage capsid; their purification and properties, isolation and characterization of the defective mutants, and their binding with the defective heads in vitro. J Mol Biol 109:487–514
29. Qin L, Fokine A, O’Donnell E, Rao VB, Rossmann MG (2009) Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages. J Mol Biol 395:728–741
30. Sathaliyawala T et al (2010) Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages. Mol Microbiol 77:444–455
31. Tao P et al (2013) In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine. Proc Natl Acad Sci U S A 110:5846–5851