A plant-produced bacteriophage tailspike protein for the control of Salmonella
The receptor binding domain of the tailspike protein Gp9 from the P22 bacteriophage was recently shown to reduce colonization in the chicken gut. In this study, we transiently expressed the receptor binding domain of the Gp9 tailspike protein in Nicotiana benthamiana, and targeted it to the endoplas...
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doaj-594e4c02e42847b6894e638f989a8aa82020-11-25T00:12:09ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-01-01610.3389/fpls.2015.01221172721A plant-produced bacteriophage tailspike protein for the control of SalmonellaSean Philip Miletic0Sean Philip Miletic1David J Simpson2David J Simpson3Christine M Szymanski4Christine M Szymanski5Michael K Deyholos6Rima eMenassa7Rima eMenassa8Agriculture and Agri-Food CanadaUniversity of Western OntarioUniversity of AlbertaUniversity of AlbertaUniversity of AlbertaUniversity of AlbertaUniversity of British ColumbiaAgriculture and Agri-Food CanadaUniversity of Western OntarioThe receptor binding domain of the tailspike protein Gp9 from the P22 bacteriophage was recently shown to reduce colonization in the chicken gut. In this study, we transiently expressed the receptor binding domain of the Gp9 tailspike protein in Nicotiana benthamiana, and targeted it to the endoplasmic reticulum (ER) or to the chloroplast. Gp9 was also fused to either an elastin-like polypeptide (ELP) or hydrophobin I (HFBI) tag, which were previously described to improve accumulation levels of recombinant proteins. The highest levels of recombinant protein accumulation occurred when unfused Gp9 was targeted to the ER. Lower levels of chloroplast-targeted Gp9 were also detected. ELP-fused Gp9 was purified and demonstrated to bind to Salmonella enterica serovar Typhimurium in vitro. Upon oral administration of lyophilized leaves expressing Gp9-ELP to newly hatched chicks, we found that this tailspike protein has the potential to be used as a prophylactic to control Salmonella contamination in chickens.http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01221/fullChickensSalmonellaplant biotechnologyNicotiana benthamianaTransient transformationbacteriophage tailspike protein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sean Philip Miletic Sean Philip Miletic David J Simpson David J Simpson Christine M Szymanski Christine M Szymanski Michael K Deyholos Rima eMenassa Rima eMenassa |
spellingShingle |
Sean Philip Miletic Sean Philip Miletic David J Simpson David J Simpson Christine M Szymanski Christine M Szymanski Michael K Deyholos Rima eMenassa Rima eMenassa A plant-produced bacteriophage tailspike protein for the control of Salmonella Frontiers in Plant Science Chickens Salmonella plant biotechnology Nicotiana benthamiana Transient transformation bacteriophage tailspike protein |
author_facet |
Sean Philip Miletic Sean Philip Miletic David J Simpson David J Simpson Christine M Szymanski Christine M Szymanski Michael K Deyholos Rima eMenassa Rima eMenassa |
author_sort |
Sean Philip Miletic |
title |
A plant-produced bacteriophage tailspike protein for the control of Salmonella |
title_short |
A plant-produced bacteriophage tailspike protein for the control of Salmonella |
title_full |
A plant-produced bacteriophage tailspike protein for the control of Salmonella |
title_fullStr |
A plant-produced bacteriophage tailspike protein for the control of Salmonella |
title_full_unstemmed |
A plant-produced bacteriophage tailspike protein for the control of Salmonella |
title_sort |
plant-produced bacteriophage tailspike protein for the control of salmonella |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2016-01-01 |
description |
The receptor binding domain of the tailspike protein Gp9 from the P22 bacteriophage was recently shown to reduce colonization in the chicken gut. In this study, we transiently expressed the receptor binding domain of the Gp9 tailspike protein in Nicotiana benthamiana, and targeted it to the endoplasmic reticulum (ER) or to the chloroplast. Gp9 was also fused to either an elastin-like polypeptide (ELP) or hydrophobin I (HFBI) tag, which were previously described to improve accumulation levels of recombinant proteins. The highest levels of recombinant protein accumulation occurred when unfused Gp9 was targeted to the ER. Lower levels of chloroplast-targeted Gp9 were also detected. ELP-fused Gp9 was purified and demonstrated to bind to Salmonella enterica serovar Typhimurium in vitro. Upon oral administration of lyophilized leaves expressing Gp9-ELP to newly hatched chicks, we found that this tailspike protein has the potential to be used as a prophylactic to control Salmonella contamination in chickens. |
topic |
Chickens Salmonella plant biotechnology Nicotiana benthamiana Transient transformation bacteriophage tailspike protein |
url |
http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01221/full |
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