Fimbriae assisted bacterial surface display of heterologous peptides

Abstract The display of peptide segments on the surface of bacteria offers many new and exciting applications in biotechnology and medical research. Fimbria-assisted display of heterologous sequences is a paradigm for chimeric organelle display on bacteria. Fimbriae are particularly attractive candidates for epitope display for several reasons: (1) they are present in extremely high numbers at the cell surface, (2) they are strong immunogens, (3) they possess inherent adhesive properties, and (4) they can be easily purified. The majority of work dealing with fimbria-assisted peptide display has been focused on the development of recombinant vaccines. A number of different fimbrial types have been used to display immune-relevant sectors of various foreign proteins. Chimeric fimbrial vaccines can be used in the context of purified proteins, however the potential also exists to exploit this technology for the development of live recombinant vaccines. Work has also been performed demonstrating the amenability of fimbriae towards the powerful technology of random peptide display. This review summarises the current state of research in this field.

[1]  P. Klemm,et al.  Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences. , 1989, Gene.

[2]  M. Sela,et al.  Antibodies against synthetic peptides of the B subunit of cholera toxin: crossreaction and neutralization of the toxin. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[3]  H. Laude,et al.  CS31A capsule-like antigen as an exposure vector for heterologous antigenic determinants , 1994, Infection and immunity.

[4]  H. Moon,et al.  Vaccines for preventing enterotoxigenic Escherichia coli infections in farm animals , 1993, Vaccine.

[5]  C. Brinton The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria. , 1965, Transactions of the New York Academy of Sciences.

[6]  R. Marre,et al.  Reciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities , 1994, Journal of bacteriology.

[7]  M. Schembri,et al.  Bacterial adhesins: function and structure. , 2000, International journal of medical microbiology : IJMM.

[8]  S. Mishiro,et al.  A synthetic peptide vaccine involving the product of the pre-S(2) region of hepatitis B virus DNA: protective efficacy in chimpanzees. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[9]  H. Laude,et al.  An Escherichia coli CS31A fibrillum chimera capable of inducing memory antibodies in outbred mice following booster immunization with the entero-pathogenic coronavirus transmissible gastroenteritis virus , 1997, Vaccine.

[10]  Structural diversity in a conserved cholera toxin epitope involved in ganglioside binding , 1995, Protein science : a publication of the Protein Society.

[11]  J. Martial,et al.  Crystal structure of cholera toxin B‐pentamer bound to receptor GM1 pentasaccharide , 1994, Protein science : a publication of the Protein Society.

[12]  M. Der Vartanian,et al.  The major subunit ClpG of Escherichia coli CS31A fibrillae as an expression vector for different combinations of two TGEV coronavirus epitopes , 1996, Gene.

[13]  C. Wray,et al.  Escherichia coli infections in farm animals , 1997 .

[14]  F. V. van Zijderveld,et al.  K88 fimbriae as carriers of heterologous antigenic determinants. , 1990, Microbial pathogenesis.

[15]  P. Orndorff,et al.  Lesions in two Escherichia coli type 1 pilus genes alter pilus number and length without affecting receptor binding , 1992, Journal of bacteriology.

[16]  H. van den Bosch,et al.  P-fimbriae of Escherichia coli as carriers for gonadotropin releasing hormone: development of a recombinant contraceptive vaccine. , 1995, Vaccine.

[17]  P. Klemm FimC, a chaperone-like periplasmic protein of Escherichia coli involved in biogenesis of type 1 fimbriae. , 1992, Research in microbiology.

[18]  Linker insertion analysis of the FimH adhesin of type 1 fimbriae in an Escherichia coli fimH-null background. , 1996, FEMS microbiology letters.

[19]  K. Krogfelt,et al.  Investigation of minor components of Escherichia coli type 1 fimbriae: protein chemical and immunological aspects. , 1988, Microbial pathogenesis.

[20]  M. Schembri,et al.  Heterobinary Adhesins Based on theEscherichia coli FimH Fimbrial Protein , 1998, Applied and Environmental Microbiology.

[21]  L. Poulsen,et al.  Chimeric FimH adhesin of type 1 fimbriae: a bacterial surface display system for heterologous sequences. , 1995, Microbiology.

[22]  M. Méchin,et al.  Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences , 1994, Gene.

[23]  J. Mattick,et al.  Fimbriae of Bacteroides nodosus: protein engineering of the structural subunit for the production of an exogenous peptide. , 1989, Protein engineering.

[24]  Christos Stathopoulos,et al.  Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines , 1997, Nature Biotechnology.

[25]  E. Beachey,et al.  Identification of two ancillary subunits of Escherichia coli type 1 fimbriae by using antibodies against synthetic oligopeptides of fim gene products , 1987, Journal of bacteriology.

[26]  M. Der Vartanian,et al.  CS31A, a new K88-related fimbrial antigen on bovine enterotoxigenic and septicemic Escherichia coli strains , 1988, Infection and immunity.

[27]  J. Pinkner,et al.  FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[28]  M. Schembri,et al.  Bioaccumulation of heavy metals by fimbrial designer adhesins. , 1999, FEMS microbiology letters.

[29]  M. Wauben,et al.  Genetic manipulation of major P-fimbrial subunits and consequences for formation of fimbriae , 1988, Journal of bacteriology.

[30]  P. Klemm Fimbriae Adhesion, Genetics, Biogenesis, and Vaccines , 1994 .

[31]  L. Jensen,et al.  Authentic display of a cholera toxin epitope by chimeric type 1 fimbriae: effects of insert position and host background. , 1997, Microbiology.

[32]  A. Clippe,et al.  Cloning of DNA sequences encoding foreign peptides and their expression in the K88 pili , 1989, Applied and environmental microbiology.

[33]  V. Stojanoff,et al.  X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. , 1999, Science.

[34]  M. Bayer,et al.  Polymeric Display of Immunogenic Epitopes from Herpes Simplex Virus and Transmissible Gastroenteritis Virus Surface Proteins on an Enteroadherent Fimbria , 1999, Clinical Diagnostic Laboratory Immunology.

[35]  K. Krogfelt,et al.  Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae , 1990, Infection and immunity.

[36]  M. Schembri,et al.  Sequestration of Zinc Oxide by Fimbrial Designer Chelators , 2000, Applied and Environmental Microbiology.