scholarly journals Novel Bacterial Surface Display System Based on the Escherichia coli Protein MipA

2020 ◽  
Vol 30 (7) ◽  
pp. 1097-1103
Author(s):  
Mee Jung Han
Keyword(s):  
Escherichia Coli ◽  
Surface Display ◽  
Display System ◽  
Bacterial Surface ◽  
Bacterial Surface Display

Development of a novel bacterial surface display system using truncated OmpT as an anchoring motif

2019 ◽  
Vol 41 (6-7) ◽  
pp. 763-777 ◽  
Author(s):  
Chang-ye Hui ◽  
Yan Guo ◽  
Lisa Liu ◽  
Hao-qu Zheng ◽  
Hong-min Wu ◽  
...  
Keyword(s):  
Surface Display ◽  
Display System ◽  
Bacterial Surface ◽  
Bacterial Surface Display ◽  
Anchoring Motif

scholarly journals An Effective Platform for Exploring Rotavirus Receptors by Bacterial Surface Display System

2019 ◽  
Vol 35 (1) ◽  
pp. 103-109
Author(s):  
Danlei Liu ◽  
Haoran Geng ◽  
Zilei Zhang ◽  
Yifan Xing ◽  
Danlu Yang ◽  
...  
Keyword(s):  
Surface Display ◽  
Display System ◽  
Bacterial Surface ◽  
Bacterial Surface Display

scholarly journals Chimeric FimH adhesin of type 1 fimbriae: a bacterial surface display system for heterologous sequences

Microbiology ◽  
1995 ◽  
Vol 141 (11) ◽  
pp. 2839-2848 ◽  
Author(s):  
L. Pallesen ◽  
L. K. Poulsen ◽  
G. Christiansen ◽  
P. Klemm
Keyword(s):  
Surface Display ◽  
Display System ◽  
Bacterial Surface ◽  
Type 1 Fimbriae ◽  
Bacterial Surface Display

scholarly journals Decorating the Surface of Escherichia Coli with Bacterial Lipoproteins: A Comparative Analysis of Different Display Systems

2020 ◽  
Author(s):  
Sonia Nicchi ◽  
Maria Giuliani ◽  
Fabiola Giusti ◽  
Laura Pancotto ◽  
Domenico Maione ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Surface Display ◽  
Display System ◽  
Experimental Conditions ◽  
Bacterial Surface ◽  
E Coli ◽  
Phenotype Heterogeneity ◽  
Passenger Proteins ◽  
Display Systems

Abstract Background: The display of recombinant proteins on cell surfaces has a plethora of applications including vaccine development, screening of peptide libraries, whole-cell biocatalysts and biosensor development for diagnostic, industrial or environmental purposes. In the last decades, a wide variety of surface display systems have been developed for the exposure of recombinant proteins on the surface of Escherichia coli, such as autotransporters and outer membrane proteins.Results: In this study, we assess three approaches for the surface display of a panel of heterologous and homologous mature lipoproteins in E. coli: four from Neisseria meningitidis and four from the host strain that are known to be localised in the inner leaflet of the outer membrane. Constructs were made carrying the sequences coding for eight mature lipoproteins, each fused to the delivery portion of three different systems: the autotransporter adhesin involved in diffuse adherence-I (AIDA-I) from enteropathogenic E. coli, the Lpp’OmpA chimaera and a truncated form of the ice nucleation protein (INP), InaK-NC (N-terminal domain fused with C-terminal one) from Pseudomonas syringae. In contrast to what was observed for the INP constructs, when fused to the AIDA-I or Lpp’OmpA, most of the mature lipoproteins were displayed on the bacterial surface both at 37°C and 25°C as demonstrated by FACS analysis, confocal and transmission electron microscopy.Conclusions: To our knowledge this is the first study that compares surface display systems using a number of passenger proteins. We have shown that the experimental conditions, including the choice of the carrier protein and the growth temperature, play an important role in the translocation of mature lipoproteins onto the bacterial surface. Despite all the optimization steps performed with the InaK-NC anchor motif, surface exposure of the passenger proteins used in this study was not achieved. For our experimental conditions, Lpp’OmpA chimaera has proved to be an efficient surface display system for the homologous passenger proteins although cell lysis and phenotype heterogeneity were observed. Finally, , AIDA-I was found to be the best surface display system for mature lipoproteins (especially heterologous ones) in the E. coli host strain with no inhibition of growth and only limited phenotype heterogeneity.

scholarly journals Ice nucleation protein as a bacterial surface display protein

2011 ◽  
Vol 63 (4) ◽  
pp. 943-948 ◽  
Author(s):  
Mohammed Sarhan
Keyword(s):  
Recombinant Proteins ◽  
Surface Display ◽  
Ice Nucleation ◽  
Display System ◽  
Ice Nucleation Protein ◽  
Bacterial Surface ◽  
Sorting Signals ◽  
Bacterial Surface Display ◽  
Display Technology ◽  
Anchoring Motif

Surface display technology can be defined as that phenotype (protein or peptide) which is linked to a genotype (DNA or RNA) through an appropriate anchoring motif. A bacterial surface display system is based on expressing recombinant proteins fused to sorting signals (anchoring motifs) that direct their incorporation on the cell surface.

scholarly journals Decorating the surface of Escherichia coli with bacterial lipoproteins: a comparative analysis of different display systems

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Sonia Nicchi ◽  
Maria Giuliani ◽  
Fabiola Giusti ◽  
Laura Pancotto ◽  
Domenico Maione ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Surface Display ◽  
Display System ◽  
Experimental Conditions ◽  
Bacterial Surface ◽  
E Coli ◽  
Phenotype Heterogeneity ◽  
Passenger Proteins ◽  
Display Systems

Abstract Background The display of recombinant proteins on cell surfaces has a plethora of applications including vaccine development, screening of peptide libraries, whole-cell biocatalysts and biosensor development for diagnostic, industrial or environmental purposes. In the last decades, a wide variety of surface display systems have been developed for the exposure of recombinant proteins on the surface of Escherichia coli, such as autotransporters and outer membrane proteins. Results In this study, we assess three approaches for the surface display of a panel of heterologous and homologous mature lipoproteins in E. coli: four from Neisseria meningitidis and four from the host strain that are known to be localised in the inner leaflet of the outer membrane. Constructs were made carrying the sequences coding for eight mature lipoproteins, each fused to the delivery portion of three different systems: the autotransporter adhesin involved in diffuse adherence-I (AIDA-I) from enteropathogenic E. coli, the Lpp’OmpA chimaera and a truncated form of the ice nucleation protein (INP), InaK-NC (N-terminal domain fused with C-terminal one) from Pseudomonas syringae. In contrast to what was observed for the INP constructs, when fused to the AIDA-I or Lpp’OmpA, most of the mature lipoproteins were displayed on the bacterial surface both at 37 and 25 °C as demonstrated by FACS analysis, confocal and transmission electron microscopy. Conclusions To our knowledge this is the first study that compares surface display systems using a number of passenger proteins. We have shown that the experimental conditions, including the choice of the carrier protein and the growth temperature, play an important role in the translocation of mature lipoproteins onto the bacterial surface. Despite all the optimization steps performed with the InaK-NC anchor motif, surface exposure of the passenger proteins used in this study was not achieved. For our experimental conditions, Lpp’OmpA chimaera has proved to be an efficient surface display system for the homologous passenger proteins although cell lysis and phenotype heterogeneity were observed. Finally, AIDA-I was found to be the best surface display system for mature lipoproteins (especially heterologous ones) in the E. coli host strain with no inhibition of growth and only limited phenotype heterogeneity.

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