Delivery of epitopes by the Salmonella type III secretion system for vaccine development

Science

Volumn 281, Issue 5376, 1998, Pages 565-568

  Rüssmann, Holger ^a,c   Shams, Homayoun ^b   Poblete, Fernando ^b   Fu, Yixin ^a   Galán, Jorge E ^a   Donis, Ruben O ^b  

^a STONY BROOK UNIVERSITY   (United States)

^b UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^c UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; EPITOPE;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; BACTERIAL TRANSLOCATION; BACTERIUM MUTANT; CONTROLLED STUDY; CYTOTOXIC T LYMPHOCYTE; IMMUNE RESPONSE; LYMPHOCYTIC CHORIOMENINGITIS VIRUS; MOUSE; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; STRAIN DIFFERENCE; TARGET CELL; VACCINATION; VIRUS MENINGITIS;

ANIMALS; ANTIGEN PRESENTATION; ANTIGENS, VIRAL; BACTERIAL PROTEINS; CYTOSOL; ENDOPLASMIC RETICULUM; EPITOPES; HISTOCOMPATIBILITY ANTIGENS CLASS I; HYBRIDOMAS; LYMPHOCYTIC CHORIOMENINGITIS; LYMPHOCYTIC CHORIOMENINGITIS VIRUS; MICE; MICE, INBRED C57BL; NUCLEOPROTEINS; PEPTIDE FRAGMENTS; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT FUSION PROTEINS; SALMONELLA TYPHIMURIUM; T-LYMPHOCYTES; T-LYMPHOCYTES, CYTOTOXIC; TUMOR CELLS, CULTURED; VACCINES, SYNTHETIC; VIRAL CORE PROTEINS; VIRAL VACCINES;

ANIMALIA; BACTERIA (MICROORGANISMS); CHORIOMENINGITIS VIRUS; LYMPHOCYTIC CHORIOMENINGITIS VIRUS; SALMONELLA; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 2642703408     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.281.5376.565     Document Type: Article

References (46)

1. Anonymous, Report WHO/VRD/GEN/97.01 (World Health Organization, Global Programme For Vaccines And Immunization, Geneva, 1997) (http://www. who.cn/gpv-documents/DoxRpts/word9744.doc); S. L. Katz, Lancet 350, 1767 (1997), P. H. Lambert, Dev. Biol. Stand. 87, 45 (1996).
2. Anonymous, Report WHO/VRD/GEN/97.01 (World Health Organization, Global Programme For Vaccines And Immunization, Geneva, 1997) (http://www. who.cn/gpv-documents/DoxRpts/word9744.doc); S. L. Katz, Lancet 350, 1767 (1997), P. H. Lambert, Dev. Biol. Stand. 87, 45 (1996).
3. Anonymous, Report WHO/VRD/GEN/97.01 (World Health Organization, Global Programme For Vaccines And Immunization, Geneva, 1997) (http://www. who.cn/gpv-documents/DoxRpts/word9744.doc); S. L. Katz, Lancet 350, 1767 (1997), P. H. Lambert, Dev. Biol. Stand. 87, 45 (1996).
4. R. Curtiss III et al., Dev. Biol. Stand. 82, 23 (1994); E. Paoletti, Proc. Natl. Acad. Sci. U.S.A. 93, 11349 (1996); L. M. Weiskirch and Y. Paterson, Immunol. Rev. 158, 159 (1997); M. S. Rolph and I. A. Ramshaw, Curr. Opin. Immunol. 9, 517 (1997).
5. R. Curtiss III et al., Dev. Biol. Stand. 82, 23 (1994); E. Paoletti, Proc. Natl. Acad. Sci. U.S.A. 93, 11349 (1996); L. M. Weiskirch and Y. Paterson, Immunol. Rev. 158, 159 (1997); M. S. Rolph and I. A. Ramshaw, Curr. Opin. Immunol. 9, 517 (1997).
6. R. Curtiss III et al., Dev. Biol. Stand. 82, 23 (1994); E. Paoletti, Proc. Natl. Acad. Sci. U.S.A. 93, 11349 (1996); L. M. Weiskirch and Y. Paterson, Immunol. Rev. 158, 159 (1997); M. S. Rolph and I. A. Ramshaw, Curr. Opin. Immunol. 9, 517 (1997).
7. R. Curtiss III et al., Dev. Biol. Stand. 82, 23 (1994); E. Paoletti, Proc. Natl. Acad. Sci. U.S.A. 93, 11349 (1996); L. M. Weiskirch and Y. Paterson, Immunol. Rev. 158, 159 (1997); M. S. Rolph and I. A. Ramshaw, Curr. Opin. Immunol. 9, 517 (1997).
8. F. Schodel and R. Curtiss III, Dev. Biol. Stand. 84, 245 (1995); A. Kantele et al., J. Immunol. 158, 574 (1997); M. M. Levine et al., J. Biotechnol. 44, 193 (1996).
9. F. Schodel and R. Curtiss III, Dev. Biol. Stand. 84, 245 (1995); A. Kantele et al., J. Immunol. 158, 574 (1997); M. M. Levine et al., J. Biotechnol. 44, 193 (1996).
10. F. Schodel and R. Curtiss III, Dev. Biol. Stand. 84, 245 (1995); A. Kantele et al., J. Immunol. 158, 574 (1997); M. M. Levine et al., J. Biotechnol. 44, 193 (1996).
11. J. E. Galán, Mol. Microbiol. 20, 263 (1996); J. E. Galán and J. B. Bliska, Annu. Rev. Cell Dev. Biol. 12, 221 (1996).
12. J. E. Galán, Mol. Microbiol. 20, 263 (1996); J. E. Galán and J. B. Bliska, Annu. Rev. Cell Dev. Biol. 12, 221 (1996).
13. J. E. Galán and P. J. Sansonetti, in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, F. C. Neidhardt, Ed. (American Society for Microbiology Press, Washington, DC, ed. 2, 1996), pp. 2757-2763.
14. X. M. Gao et al., Infect. Immun. 60, 3780 (1992); J. H. Ringrose, B. A. Yard, G. M. Verjans, C. J. Boog, Clin. Rheumatol. 15, 79 (1996); D. M. Yang et al., J. Immunol. 145, 2281 (1990).
15. X. M. Gao et al., Infect. Immun. 60, 3780 (1992); J. H. Ringrose, B. A. Yard, G. M. Verjans, C. J. Boog, Clin. Rheumatol. 15, 79 (1996); D. M. Yang et al., J. Immunol. 145, 2281 (1990).
16. X. M. Gao et al., Infect. Immun. 60, 3780 (1992); J. H. Ringrose, B. A. Yard, G. M. Verjans, C. J. Boog, Clin. Rheumatol. 15, 79 (1996); D. M. Yang et al., J. Immunol. 145, 2281 (1990).
17. A. Darji et al., Cell 91, 765 (1997).
18. K. Kaniga, J. Uralil, J. B. Bliska, J. E. Galán, Mol. Microbiol. 21, 633 (1996); Y. Fu and J. E. Galán, ibid. 27, 359 (1998).
19. K. Kaniga, J. Uralil, J. B. Bliska, J. E. Galán, Mol. Microbiol. 21, 633 (1996); Y. Fu and J. E. Galán, ibid. 27, 359 (1998).
20. A. Vitiello et al., J. Immunol. 157, 5555 (1996); O. Rotzschke et al., Nature 348, 252 (1990).
21. A. Vitiello et al., J. Immunol. 157, 5555 (1996); O. Rotzschke et al., Nature 348, 252 (1990).
22. Plasmid pSB762, which encodes a chimeric protein consisting of SptP fused to a region of the influenza virus NP comprising residues 366 to 374 (ASNENMETM) (24) of the influenza virus nucleoprotein, was constructed by inserting a double-stranded oligonucleotide (5′-AAATTGCTTCCAATGAAAACATGGAGACTATGGAATCAAGTACCCTTGAACTGAGAAGCA-3′) into the unique Pvu II site of sptP. A double-stranded oligonucleotide (5′-AACGTAGCGAACGGCCGCAAGCATCAGGCGTTTATATGGGAAATA-3′) was inserted into the unique Pvu II site of sptP to construct plasmid pSB775, which encodes a protein fusion between SptP and residues 118 to 126 of the LCMV nucleoprotein. Both plasmids are derived from the low-copy plasmid pWSK-II [R. F. Wang and S. Kushner, Gene 100, 195 (1991)]. Plasmid pSB776, which encodes a fusion between the first 179 amino acids of InvJ and residues 335 to 498 of the influenza virus nucleoprotein, was constructed by polymerase chain reaction (PCR). This plasmid is derived from the low-copy plasmid pYA292 [J. E. Galán, K. Nakayama, R. Curtiss III, Gene 94, 29 (1990)]. Strain SB824 was constructed by introducing the sptP::kan mutant allele from strain SB237 (8) into the ΔaroA strain SL3261 [S. K. Hoiseth and B. A. Stocker, Nature 291, 238 (1981)] by P22HTint transduction.
23. Plasmid pSB762, which encodes a chimeric protein consisting of SptP fused to a region of the influenza virus NP comprising residues 366 to 374 (ASNENMETM) (24) of the influenza virus nucleoprotein, was constructed by inserting a double-stranded oligonucleotide (5′-AAATTGCTTCCAATGAAAACATGGAGACTATGGAATCAAGTACCCTTGAACTGAGAAGCA-3′) into the unique Pvu II site of sptP. A double-stranded oligonucleotide (5′-AACGTAGCGAACGGCCGCAAGCATCAGGCGTTTATATGGGAAATA-3′) was inserted into the unique Pvu II site of sptP to construct plasmid pSB775, which encodes a protein fusion between SptP and residues 118 to 126 of the LCMV nucleoprotein. Both plasmids are derived from the low-copy plasmid pWSK-II [R. F. Wang and S. Kushner, Gene 100, 195 (1991)]. Plasmid pSB776, which encodes a fusion between the first 179 amino acids of InvJ and residues 335 to 498 of the influenza virus nucleoprotein, was constructed by polymerase chain reaction (PCR). This plasmid is derived from the low-copy plasmid pYA292 [J. E. Galán, K. Nakayama, R. Curtiss III, Gene 94, 29 (1990)]. Strain SB824 was constructed by introducing the sptP::kan mutant allele from strain SB237 (8) into the ΔaroA strain SL3261 [S. K. Hoiseth and B. A. Stocker, Nature 291, 238 (1981)] by P22HTint transduction.
24. Plasmid pSB762, which encodes a chimeric protein consisting of SptP fused to a region of the influenza virus NP comprising residues 366 to 374 (ASNENMETM) (24) of the influenza virus nucleoprotein, was constructed by inserting a double-stranded oligonucleotide (5′-AAATTGCTTCCAATGAAAACATGGAGACTATGGAATCAAGTACCCTTGAACTGAGAAGCA-3′) into the unique Pvu II site of sptP. A double-stranded oligonucleotide (5′-AACGTAGCGAACGGCCGCAAGCATCAGGCGTTTATATGGGAAATA-3′) was inserted into the unique Pvu II site of sptP to construct plasmid pSB775, which encodes a protein fusion between SptP and residues 118 to 126 of the LCMV nucleoprotein. Both plasmids are derived from the low-copy plasmid pWSK-II [R. F. Wang and S. Kushner, Gene 100, 195 (1991)]. Plasmid pSB776, which encodes a fusion between the first 179 amino acids of InvJ and residues 335 to 498 of the influenza virus nucleoprotein, was constructed by polymerase chain reaction (PCR). This plasmid is derived from the low-copy plasmid pYA292 [J. E. Galán, K. Nakayama, R. Curtiss III, Gene 94, 29 (1990)]. Strain SB824 was constructed by introducing the sptP::kan mutant allele from strain SB237 (8) into the ΔaroA strain SL3261 [S. K. Hoiseth and B. A. Stocker, Nature 291, 238 (1981)] by P22HTint transduction.
25. K. Kaniga, D. Trollinger, J. E. Galán, J. Bacteriol. 177, 7078 (1995).
26. A. Deckhut et al., J. Immunol. 151, 2658 (1993); H. G. Ljunggren and K. Karre, J. Exp. Med. 162, 1745 (1985).
27. A. Deckhut et al., J. Immunol. 151, 2658 (1993); H. G. Ljunggren and K. Karre, J. Exp. Med. 162, 1745 (1985).
28. 5 cells ) was added to the treated RMA or RMA-S cultures (12). Culture medium was collected after incubation for 44 hours at 37°C to determine the IL-2 concentration by a capture ELISA (Pharmingen).
29. 366-374 coding sequence of pSB762 by PCR. The resulting mutant protein is secreted from the bacteria at levels indistinguishable from those of wild type but it is not translocated into host cells (Y. Fu and J. E. Galán, unpublished results).
30. 366-374 coding sequence of pSB762 by PCR. The resulting mutant protein is secreted from the bacteria at levels indistinguishable from those of wild type but it is not translocated into host cells (Y. Fu and J. E. Galán, unpublished results).
31. C. M. Collazo and J. E. Galán, Mol. Microbiol. 24, 747 (1996).
32. C. M. Collazo, M. K. Zierler, J. E. Galán, ibid. 15, 25 (1995).
33. M. Attaya et al., Nature 355, 647 (1992).
34. 51Cr release after cocultivation for 4 hours. Target lysis was calculated as [(experimental release - spontaneous release)/ (maximum release - spontaneous release)] × 100. Maximum release was determined by Triton X-100 cell lysis. Spontaneous release was always <10% of maximum release. Data are presented as percent specific lysis, with the percent lysis of unsensitized target cells subtracted from the percent lysis of cognate peptide-sensitized target cells.
35. L. S. Klavinskis, A. Tishon, M. B. Oldstone, J. Immunol. 143, 2013 (1989); J. L. Whitton et al., J. Virol. 63, 4303 (1989).
36. L. S. Klavinskis, A. Tishon, M. B. Oldstone, J. Immunol. 143, 2013 (1989); J. L. Whitton et al., J. Virol. 63, 4303 (1989).
37. 4 PFU of LCMV strain Armstrong 4 weeks before assessment of immunity.
38. 4 PFU of LCMV strain Armstrong 4 weeks before intracerebral inoculation with LCMV, survived.
39. J. Hackett, Curr. Opin. Biotechnol. 4, 611 (1993): K. L Karem, J. N. Bowen, B. T. Rouse, J. Gen. Virol. 78, 427 (1997).
40. J. Hackett, Curr. Opin. Biotechnol. 4, 611 (1993): K. L Karem, J. N. Bowen, B. T. Rouse, J. Gen. Virol. 78, 427 (1997).
41. W. Schmidt et al., Proc. Natl. Acad. Sci. U.S.A. 94, 3262 (1997); M. A. Ossevoort, M. C. Feltkamp, K. J. van Veen, C. J. Melief, W. M. Kast, J. Immunother. Emphasis Tumor Immunol. 18, 86 (1995); J. Schlom et al., Breast Cancer Res. Treat. 38, 27 (1996).
42. W. Schmidt et al., Proc. Natl. Acad. Sci. U.S.A. 94, 3262 (1997); M. A. Ossevoort, M. C. Feltkamp, K. J. van Veen, C. J. Melief, W. M. Kast, J. Immunother. Emphasis Tumor Immunol. 18, 86 (1995); J. Schlom et al., Breast Cancer Res. Treat. 38, 27 (1996).
43. W. Schmidt et al., Proc. Natl. Acad. Sci. U.S.A. 94, 3262 (1997); M. A. Ossevoort, M. C. Feltkamp, K. J. van Veen, C. J. Melief, W. M. Kast, J. Immunother. Emphasis Tumor Immunol. 18, 86 (1995); J. Schlom et al., Breast Cancer Res. Treat. 38, 27 (1996).
44. Abbreviations for amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp, Y, Tyr.
45. G. L. Smith, J. Z. Levin, P. Palese, B. Moss, Virology 160, 336 (1987).
46. We thank P. Doherty for T cell hybridoma 12.164. Supported by grants from the NIH (J.E.G. and R.O.D.) and the American Heart Association (J.E.G.) and a fellowship from the German Bundesministerium für Forschung und Technologie-Aids Stipendienprogramm (H.R.).