Efficient secretion of the model antigen M6-gp41E in Lactobacillus plantarum NCIMB 8826

Microbiology

Volumn 143, Issue 8, 1997, Pages 2733-2741

  Hols, Pascal ^a   Slos, Philippe ^b   Dutot, Philippe ^b   Reymund, Jacqueline ^b   Chabot, Paul ^b   Delplace, Brigitte ^a   Delcour, Jean ^a   Mercenier, Annick ^b,c  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

^b TRANSGENE S A   (France)

^c INSTITUT PASTEUR DE LILLE   (France)

Author keywords

Lactobacillus; M6 protein; Mucosal vaccines; Secretion; amylase

Indexed keywords

AMYLASE; ANTIGEN; BACTERIAL ANTIGEN; EPITOPE; GLYCOPROTEIN GP 41; LACTIC ACID; VIRUS FUSION PROTEIN; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; HUMAN IMMUNODEFICIENCY VIRUS 1; LACTIC ACID BACTERIUM; LACTOBACILLUS PLANTARUM; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN SECRETION; STREPTOCOCCUS PYOGENES;

BACTERIA (MICROORGANISMS); HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; LACTOBACILLUS; LACTOBACILLUS PLANTARUM; STREPTOCOCCUS PYOGENES;

EID: 0030816521     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-8-2733     Document Type: Article

References (48)

1. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
2. Casadaban, M. J. & Cohen, S. (1980). Analysis of gene control signals by DNA fusion cloning in E. coli. J Mol Biol 138, 179-207.
3. Chassy, B. M. (1987). Prospects for the genetic manipulation of lactobacilli. FEMS Microbiol Rev 46, 297-312.
4. van Dijl, J. M., Smith, H., Bron, S. & Venema, G. (1988). Synthesis and processing of Escherichia coli TEM β-lactamase and Bacillus licheniformis α-amylase in E. coli: the role of signal peptidase I. Mol Gen Genet 214, 55-61.
5. Dutot, P. (1996). Evaluation des lactobacilles comme vecteurs vivants de vaccination. PhD thesis, Université Louis-Pasteur de Strasbourg.
6. Fernandes, C. F., Shahani, K. M. & Amer, M. A. (1987). Therapeutic role of dietary lactobacilli and lactobacillic fermented dairy products. FEMS Microbiol Rev 46, 343-356.
7. Fischetti, V. A., Medaglini, D., Oggioni, M. & Pozzi, G. (1993). Expression of foreign proteins on Gram-positive commensal bacteria for mucosal vaccine delivery. Curr Opin Biotechnol 4, 603-610.
8. Fitzsimons, A., Hols, P., Jore, J., Leer, R. J., O'Connell, M. & Delcour, J. (1994). Development of an amylolytic Lactobacillus plantarum silage strain expressing the Lactobacillus amylovorus α-amylase gene. Appl Environ Microbiol 60, 3529-3535.
9. Gibson, S. A. W. & Conway, P. L. (1992). Recovery of a probiotic organism from human faeces after oral dosing. In Human Health: the Contribution of Microorganisms, pp. 119-141. Edited by S. A. W. Gibson. New York: Springer.
10. Hollingshead, S. K., Fischetti, V. A. & Scott, J. R. (1986). Complete nucleotide sequence of type 6 M protein of the group A Streptococcus: repetitive structure and membrane anchor. J Biol Chem 261, 1677-1686.
11. Hols, P., Baulard, A., Garmyn, D., Delplace, B., Hogan, S. & Delcour, J. (1992). Isolation and characterization of genetic expression and secretion signals from Enterococcus faecalis through the use of broad-host-range α-amylase probe vectors. Gene 118, 21-30.
12. Hols, P., Ferain, T., Garmyn, D., Bernard, N. & Delcour, J. (1994). Use of homologous expression-secretion signals and vector-free stable chromosomal integration in engineering of Lactobacillus plantarum for α-amylase and levanase expression. Appl Environ Microbiol 60, 1401-1413.
13. Josson, K., Scheirlinck, T., Michiels, F., Plateeuw, C., Stanssens, P., Joos, H., Dhaese, P., Zabeau, M. & Mahillon, J. (1989). Characterization of a Gram-positive broad-host-range plasmid isolated from Lactobacillus hilgardii. Plasmid 21, 9-20.
14. Klijn, N., Weerkamp, A. H. & de Vos, W. M. (1995). Genetic marking of Lactococcus lactis shows its survival in the human gastrointestinal tract. Appl Environ Microbiol 61, 2771-2774.
15. Kok, J., van der Vossen, J. M. B. M. & Venema, G. (1984). Construction of plasmid cloning vectors for lactic streptococci which also replicate in Bacillus subtilis and Escherichia coli. Appl Environ Microbiol 48, 726-731.
16. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 27, 680-685.
17. Leclerc, C., Charbit, A., Martineau, P., Deriaud, E. & Hofnung, M. (1991). The cellular location of foreign B cell epitope expressed by recombinant bacteria determines its T cell-independent or T cell-dependent characteristics. J Immunol 147, 3545-3552.
18. Link-Amster, H., Rochat, F., Saudan, K. Y., Mignot, O. & Aeschlimann, J. M. (1994). Modulation of a specific humoral immune response and changes in intestinal flora mediated through fermented milk intake. FEMS Immunol Med Microbiol 10, 55-64.
19. Marteau, P. & Rambaud, J.-C. (1993). Potential of using lactic acid bacteria for therapy and immunomodulation in man. FEMS Microbiol Rev 12, 207-220.
20. Mercenier, A., Pouwels, P. H. & Chassy, B. M. (1994). Genetic engineering of lactobacilli, leuconostocs and Streptococcus thermophilus. In Genetics and Biotechnology of Lactic Acid Bacteria, pp. 252-293. Edited by M. J. Gasson & W. M. de Vos. Glasgow: Blackie Academic & Professional.
21. Muster, T., Guinea, R., Trkola, A., Purtscher, M., Klima, A., Steindl, F., Palese, P. & Katinger, H. (1994). Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by gp41 sequence ELDKWAS. J Virol 68, 4031-4034.
22. Nguyen, T. N., Hansson, M., Ståhl, S., Bächi, T., Robert, A., Domzig, W., Binz, H. & Uhlén, M. (1993). Cell-surface display of heterologous epitopes on Staphylococcus xylosus as a potential delivery system for oral vaccination. Gene 128, 89-94.
23. Norton, P. M., Brown, H. W. G. & Le Page, R. W. F. (1994). The immune response to Lactococcus lactis: implications for its use as vaccine delivery vehicle. FEMS Microbiol Lett 120, 249-256.
24. Oggioni, M. R., Manganelli, R., Contorni, M., Tommasino, M. & Pozzi, G. (1995). Immunization of mice by oral colonization with live recombinant commensal streptococci. Vaccine 13, 775-779.
25. O'Sullivan, D. J. & Klaenhammer, T. R. (1993). Rapid mini-prep isolation of high quality plasmid DNA from Lactococcus and Lactobacillus spp. Appl Environ Microbiol 59, 2730-2733.
26. Perdigon, G., de Macias, M. E. N., Alvarez, S., Oliver, G. & de Ruiz Holgado, A. P. (1988). Systemic augmentation of the immune response in mice by feeding fermented milks with Lactobacillus casei and Lactobacillus acidophilus. Immunology 63, 17-23.
27. Perez-Martinez, G., Kok, J., Venema, G., van Dijl, J. M., Smith, H. & Bron, S. (1992). Protein export elements from Lactococcus lactis. Mol Gen Genet 234, 401-411.
28. Posno, M., Leer, R. J., van Luik, K., van Giezen, N. M. J. F., Heuvelmans, B. C., Lokman, P. T. H. M. & Pouwels, P. H. (1991). Incompatibility of Lactobacillus vectors with replicons derived from small cryptic Lactobacillus plasmids and segregational instability of the introduced vectors. Appl Environ Microbiol 57, 1822-1828.
29. Pouwels, P. H. & Leer, R. J. (1993). Genetics of lactobacilli: plasmids and gene expression. Antonie Leeuwenhoek 64, 85-107.
30. Pouwels, P. H., Leer, R. J. & Boersma, W. J. A. (1996). The potential of Lactobacillus as a carrier for oral immunization: development and preliminary characterization of vector systems for targeted delivery of antigens. J Biotechnol 44, 183-192.
31. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
32. Samuelson, P., Hansson, M., Ahlborg, N., Andréoni, C., Götz, F., Bächi, T., Nguyen, T. N., Binz, H., Uhlén, M. & Ståhl, S. (1995). Cell surface display of recombinant proteins on Staphylococcus carnosus. J Bacteriol 177, 1470-1476.
33. Saunders, C. W., Schmidt, B. J., Mallonee, R. L. & Guyer, M. S. (1987). Secretion of human serum albumin from Bacillus subtilis. J Bacteriol 169, 2917-2925.
34. Schauder, B. & McCarthy, J. E. G. (1989). The role of bases upstream of the Shine-Dalgarno region and in the coding sequence in the control of gene expression in Escherichia coli: translation and stability of mRNAs in vivo. Gene 78, 59-72.
35. Schneewind, O., Fowler, A. & Faull, K. F. (1995). Structure of the cell wall anchor of surface protein in Staphylococcus aureus. Science 268, 103-106.
36. Schorr, J., Knapp, B., Hundt, E., Küpper, H. A. & Amann, E. (1991). Surface expression of malarial antigens in Salmonella typhimurium: induction of serum antibody response upon oral vaccination of mice. Vaccine 9, 675-681.
37. Simonen, M. & Palva, I. (1993). Protein secretion in Bacillus species. Microbiol Rev 57, 109-137.
38. Slos, P. (1990). Développement de systèmes de transfert de gènes et de vecteurs d'expression chez Streptococcus thermophilus. PhD thesis, Université Louis-Pasteur de Strasbourg.
39. Slos, P., Bourquin, J.-C., Lemoine, Y. & Mercenier, A. (1991). Isolation and characterization of chromosomal promoters of Streptococcus salivarius subsp. thermophilus. Appl Environ Microbiol 57, 1333-1339.
40. de Smit, M. H. & van Duin, J. (1990). Secondary structure of the ribosome binding site determines translation efficiency: a quantitative analysis. Proc Natl Acad Sci USA 87, 7668-7672.
41. Steidler, L., Wells, J. M., Raeymaekers, A., Vandekerckhove, J., Fiers, W. & Remaut, E. (1995). Secretion of biologically active murine interleukin-2 by Lactococcus lactis subsp. lactis. Appl Environ Microbiol 61, 1627-1629.
42. Taguchi, H. & Ohta, T. (1991). D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: cloning, sequencing and expression in Escherichia coli of the L-lactate dehydrogenase gene of Lactobacillus plantarum. J Biol Chem 266, 12588-12594.
43. Tinoco, I., Jr, Borer, P. N., Dengler, B., Levine, M. D., Uhlenbeck, O. C., Crothers, D. M. & Gralla, J. (1973). Improved estimation of secondary structure in ribonucleic acids. Nature New Biol 246, 40-41.
44. Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76, 4350-4354.
45. Van Asseldonk, M. (1993). Production and secretion of heterologous proteins by Lactococcus lactis. PhD thesis, Agricultural University of Wageningen.
46. Van Asseldonk, M., de Vos, W. M. & Simons, G. (1993). Functional analysis of the Lactococcus lactis usp45 secretion signal in the secretion of a homologous proteinase and a heterologous α-amylase. Mol Gen Genet 240, 428-434.
47. Wells, J. M., Wilson, P. W., Norton, P. M., Gasson, M. J. & Le Page, R. W. F. (1993a). Lactococcus lactis: high-level expression of tetanus toxin fragment C and protection against lethal challenge. Mol Microbiol 8, 1155-1162.
48. Wells, J. M., Wilson, P. W., Norton, P. M. & Le Page, R. W. F. (1993b). A model system for the investigation of heterologous protein secretion pathways in Lactococcus lactis. Appl Environ Microbiol 59, 3954-3959.