Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences

Hedegaard, L.; Klemm, Per

doi:10.1016/0378-1119(89)90471-x

Cited by 58 publications

(30 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gram-negative bacteria, such as Escherichia coli and Salmonella spp. [3][4][5][6][7][8], and more recently certain Gram-positive bacteria have been investigated for surface display purposes. The Mycobacterium bovis strain, bacillus Calmette-Guerin (BCG) [9], as well as staphylococci [10][11][12][13][14] and streptococci [15 18] have been investigated.…”

Section: Introductionmentioning

confidence: 99%

Surface display on staphylococci: a comparative study

et al. 1996

View full text Add to dashboard Cite

Two different host-vector expression systems, designed for cell surface display of heterologous receptors on Staphylococcus xylosus and Staphylococcus carnosus, respectively, were compared for the surface display of four variants of a 101 amino acid region derived from the G glycoprotein of human respiratory syncytial virus (RSV). Surface localization of the different chimeric receptors was evaluated by a colorimetric assay and by fluorescence-activated cell sorting. It was concluded that the S. carnosus system was better both in the ability to translocate inefficiently secreted peptides and in the number of exposed hybrid receptors. The potential use of the described staphylococci as live bacterial vaccine vehicles or alternatives to filamentous phages for surface display of protein libraries is discussed.

show abstract

Section: Introductionmentioning

confidence: 99%

Surface display on staphylococci: a comparative study

et al. 1996

View full text Add to dashboard Cite

show abstract

“…Many different types of surface proteins of gram-negative bacteria have been used to display foreign peptides; these surface proteins include LamB (4,5,22), flagellin (26,29), P fimbriae (35,38), OmpA (9), PhoE (1), peptidoglycan-associated lipoprotein (7,10), OprI (6), Lpp (8), and type 1 fimbriae (13,20,30,36). Enzymes, antigenic determinants, single-chain antibodies, metal-chelating peptides, and random peptide libraries have all been displayed on the surfaces of gram-negative bacteria.…”

mentioning

confidence: 99%

Sequestration of Zinc Oxide by Fimbrial Designer Chelators

Kjærgaard

Sørensen

Schembri

et al. 2000

Appl Environ Microbiol

Self Cite

108

View full text Add to dashboard Cite

Type 1 fimbriae are surface organelles of Escherichia coli. By engineering a structural component of the fimbriae, FimH, to display a random peptide library, we were able to isolate metal-chelating bacteria. A library consisting of 4 ؋ 10 7 independent clones was screened for binding to ZnO. Sequences responsible for ZnO adherence were identified, and distinct binding motifs were characterized. The sequences selected exhibited various degrees of affinity and specificity towards ZnO. Competitive binding experiments revealed that the sequences recognized only the oxide form of Zn. Interestingly, one of the inserts exhibited significant homology to a specific sequence in a putative zinc-containing helicase, which suggests that searches such as this one may aid in identifying binding motifs in nature. The zinc-binding bacteria might have a use in detoxification of metal-polluted water.

show abstract

“…In gram-negative bacteria, different types of surface proteins have been exploited for this purpose. These include the following: (i) outer membrane proteins LamB (4), PhoE (1), and OmpA (35); (ii) lipoproteins TraT (19) and the peptidoglycan-associated lipoprotein (10); (iii) the fimbria protein fimbrillin (20,21); and (iv) the flagellar protein flagellin (32). The different surface display systems have been used extensively to express heterologous antigenic determinants on the bacterial cells for the purpose of developing live bacterial vaccine vehicles.…”

mentioning

confidence: 99%

Cell surface display of recombinant proteins on Staphylococcus carnosus

et al. 1995

View full text Add to dashboard Cite

Surface display of heterologous proteins on bacterial cells is an important objective for many applications in microbiology and molecular biology. In gram-negative bacteria, different types of surface proteins have been exploited for this purpose. These include the following: (i) outer membrane proteins LamB (4), PhoE (1), and OmpA (35); (ii) lipoproteins TraT (19) and the peptidoglycan-associated lipoprotein (10); (iii) the fimbria protein fimbrillin (20, 21); and (iv) the flagellar protein flagellin (32). The different surface display systems have been used extensively to express heterologous antigenic determinants on the bacterial cells for the purpose of developing live bacterial vaccine vehicles. Enteric bacteria, such as Escherichia coli and Salmonella typhimurium, have been studied in this context, and the cell surface presentation has been considered advantageous to induce an antibody response to the exposed antigens with live cells for immunization (11,28,41).The expression of functional single-chain antibodies on the surface of E. coli cells (7, 10) has opened the discussion of whether this strategy would be an alternative to the rapidly developing phage technology for the selection of peptides or recombinant antibody fragments from large libraries (31). An interesting application for bacterial cells exposing heterologous proteins might be the development of whole-cell adsorbents by the surface expression of suitable protein ligands. Immobilized recombinant bacteria cannot be considered for separation processes in pharmaceutical industries but might because of their low cost constitute competitive adsorbents for certain separations (3, 11). The use of enzyme-coated bacteria as novel biocatalysts has also been envisioned, because enzymes with retained activity have been surface displayed on E. coli cells (8, 9).Investigations with gram-positive bacteria for cell surface display of heterologous proteins have recently been initiated. Expression systems for the mouth commensal bacterium Streptococcus gordinii (37) and the nonpathogenic bacterium Staphylococcus xylosus (18) have been developed on the basis of the fibrillar M6 protein from Streptococcus pyogenes and protein A from Staphylococcus aureus, respectively. These cell surface display systems have been used for the surface expression of several antigenic determinants, and immunization with live recombinant bacteria induces both local and systemic antibody responses to the hybrid receptors (33, 37), suggesting that gram-positive bacteria might constitute potential live bacterial vaccine delivery systems. The surface receptors of gram-positive bacteria seem to be more permissive for the insertion of extended sequences of foreign proteins (6) than the different gram-negative systems, in which both translocation through the cytoplasmic membrane and correct integration into the outer membrane are required for proper surface exposure of the heterologous polypeptide. Considering the development of whole-cell adsorbents or bacterial biocatalysts by surface ...

show abstract

Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences

Cited by 58 publications

References 18 publications

Surface display on staphylococci: a comparative study

Surface display on staphylococci: a comparative study

Sequestration of Zinc Oxide by Fimbrial Designer Chelators

Cell surface display of recombinant proteins on Staphylococcus carnosus

Contact Info

Product

Resources

About