An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.

W.S.P. Jong, M.H. Daleke, D. Vikstrom, C.M. ten Hagen-Jongman ten, K. de Punder, N.N. van der Wel, C.E. van de Sandt, G.F. Rimmelzwaan, F. Follman, E. Agger, P. Andersen, J.-W. de Gier, J. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Background: The Autotransporter pathway, ubiquitous in Gram-negative bacteria, allows the efficient secretion of large passenger proteins via a relatively simple mechanism. Capitalizing on its crystal structure, we have engineered the Escherichia coli autotransporter Hemoglobin protease (Hbp) into a versatile platform for secretion and surface display of multiple heterologous proteins in one carrier molecule. Results: As proof-of-concept, we demonstrate efficient secretion and high-density display of the sizeable Mycobacterium tuberculosis antigens ESAT6, Ag85B and Rv2660c in E. coli simultaneously. Furthermore, we show stable multivalent display of these antigens in an attenuated Salmonella Typhimurium strain upon chromosomal integration. To emphasize the versatility of the Hbp platform, we also demonstrate efficient expression of multiple sizeable antigenic fragments from Chlamydia trachomatis and the influenza A virus at the Salmonella cell surface. Conclusions: The successful efficient cell surface display of multiple antigens from various pathogenic organisms highlights the potential of Hbp as a universal platform for the development of multivalent recombinant bacterial vector vaccines.
LanguageEnglish
Article number162
Pages1-15
Number of pages15
JournalMicrobial Cell Factories
Volume13
DOIs
Publication statusPublished - 25 Nov 2014

Fingerprint

Bacterial Vaccines
Synthetic Vaccines
Vaccines
Hemoglobin
Hemoglobins
Peptide Hydrolases
Antigens
Display devices
Salmonella
Escherichia coli
Chlamydia trachomatis
Influenza A virus
Salmonella typhimurium
Gram-Negative Bacteria
Proteins
Viruses
Bacteria
Crystal structure
Molecules
Type V Secretion Systems

Cite this

Jong, W.S.P. ; Daleke, M.H. ; Vikstrom, D. ; ten Hagen-Jongman ten, C.M. ; de Punder, K. ; van der Wel, N.N. ; van de Sandt, C.E. ; Rimmelzwaan, G.F. ; Follman, F. ; Agger, E. ; Andersen, P. ; de Gier, J.-W. ; Luirink, J. / An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines. In: Microbial Cell Factories. 2014 ; Vol. 13. pp. 1-15.
@article{0e9030b04bab4789bbc96ed49d8b7385,
title = "An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.",
abstract = "Background: The Autotransporter pathway, ubiquitous in Gram-negative bacteria, allows the efficient secretion of large passenger proteins via a relatively simple mechanism. Capitalizing on its crystal structure, we have engineered the Escherichia coli autotransporter Hemoglobin protease (Hbp) into a versatile platform for secretion and surface display of multiple heterologous proteins in one carrier molecule. Results: As proof-of-concept, we demonstrate efficient secretion and high-density display of the sizeable Mycobacterium tuberculosis antigens ESAT6, Ag85B and Rv2660c in E. coli simultaneously. Furthermore, we show stable multivalent display of these antigens in an attenuated Salmonella Typhimurium strain upon chromosomal integration. To emphasize the versatility of the Hbp platform, we also demonstrate efficient expression of multiple sizeable antigenic fragments from Chlamydia trachomatis and the influenza A virus at the Salmonella cell surface. Conclusions: The successful efficient cell surface display of multiple antigens from various pathogenic organisms highlights the potential of Hbp as a universal platform for the development of multivalent recombinant bacterial vector vaccines.",
author = "W.S.P. Jong and M.H. Daleke and D. Vikstrom and {ten Hagen-Jongman ten}, C.M. and {de Punder}, K. and {van der Wel}, N.N. and {van de Sandt}, C.E. and G.F. Rimmelzwaan and F. Follman and E. Agger and P. Andersen and {de Gier}, J.-W. and J. Luirink",
year = "2014",
month = "11",
day = "25",
doi = "10.1186/s12934-014-0162-8",
language = "English",
volume = "13",
pages = "1--15",
journal = "Microbial Cell Factories",
issn = "1475-2859",
publisher = "BioMed Central",

}

Jong, WSP, Daleke, MH, Vikstrom, D, ten Hagen-Jongman ten, CM, de Punder, K, van der Wel, NN, van de Sandt, CE, Rimmelzwaan, GF, Follman, F, Agger, E, Andersen, P, de Gier, J-W & Luirink, J 2014, 'An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.', Microbial Cell Factories, vol. 13, 162, pp. 1-15. https://doi.org/10.1186/s12934-014-0162-8

An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines. / Jong, W.S.P.; Daleke, M.H.; Vikstrom, D.; ten Hagen-Jongman ten, C.M.; de Punder, K.; van der Wel, N.N.; van de Sandt, C.E.; Rimmelzwaan, G.F.; Follman, F.; Agger, E.; Andersen, P.; de Gier, J.-W.; Luirink, J.

In: Microbial Cell Factories, Vol. 13, 162, 25.11.2014, p. 1-15.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.

AU - Jong, W.S.P.

AU - Daleke, M.H.

AU - Vikstrom, D.

AU - ten Hagen-Jongman ten, C.M.

AU - de Punder, K.

AU - van der Wel, N.N.

AU - van de Sandt, C.E.

AU - Rimmelzwaan, G.F.

AU - Follman, F.

AU - Agger, E.

AU - Andersen, P.

AU - de Gier, J.-W.

AU - Luirink, J.

PY - 2014/11/25

Y1 - 2014/11/25

N2 - Background: The Autotransporter pathway, ubiquitous in Gram-negative bacteria, allows the efficient secretion of large passenger proteins via a relatively simple mechanism. Capitalizing on its crystal structure, we have engineered the Escherichia coli autotransporter Hemoglobin protease (Hbp) into a versatile platform for secretion and surface display of multiple heterologous proteins in one carrier molecule. Results: As proof-of-concept, we demonstrate efficient secretion and high-density display of the sizeable Mycobacterium tuberculosis antigens ESAT6, Ag85B and Rv2660c in E. coli simultaneously. Furthermore, we show stable multivalent display of these antigens in an attenuated Salmonella Typhimurium strain upon chromosomal integration. To emphasize the versatility of the Hbp platform, we also demonstrate efficient expression of multiple sizeable antigenic fragments from Chlamydia trachomatis and the influenza A virus at the Salmonella cell surface. Conclusions: The successful efficient cell surface display of multiple antigens from various pathogenic organisms highlights the potential of Hbp as a universal platform for the development of multivalent recombinant bacterial vector vaccines.

AB - Background: The Autotransporter pathway, ubiquitous in Gram-negative bacteria, allows the efficient secretion of large passenger proteins via a relatively simple mechanism. Capitalizing on its crystal structure, we have engineered the Escherichia coli autotransporter Hemoglobin protease (Hbp) into a versatile platform for secretion and surface display of multiple heterologous proteins in one carrier molecule. Results: As proof-of-concept, we demonstrate efficient secretion and high-density display of the sizeable Mycobacterium tuberculosis antigens ESAT6, Ag85B and Rv2660c in E. coli simultaneously. Furthermore, we show stable multivalent display of these antigens in an attenuated Salmonella Typhimurium strain upon chromosomal integration. To emphasize the versatility of the Hbp platform, we also demonstrate efficient expression of multiple sizeable antigenic fragments from Chlamydia trachomatis and the influenza A virus at the Salmonella cell surface. Conclusions: The successful efficient cell surface display of multiple antigens from various pathogenic organisms highlights the potential of Hbp as a universal platform for the development of multivalent recombinant bacterial vector vaccines.

U2 - 10.1186/s12934-014-0162-8

DO - 10.1186/s12934-014-0162-8

M3 - Article

VL - 13

SP - 1

EP - 15

JO - Microbial Cell Factories

T2 - Microbial Cell Factories

JF - Microbial Cell Factories

SN - 1475-2859

M1 - 162

ER -