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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Main Authors: Sean Philip Miletic, David J Simpson, Christine M Szymanski, Michael K Deyholos, Rima eMenassa
Format: Article
Language:English
Published: Frontiers Media S.A. 2016-01-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01221/full
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spelling 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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