Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.

Plant genetic engineering, which has led to the production of plant-derived monoclonal antibodies (mAb(P)s), provides a safe and economically effective alternative to conventional antibody expression methods. In this study, the expression levels and biological properties of the anti-rabies virus mAb...

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Autores principales:	Jeong-Hwan Lee, Da-Young Park, Kyung-Jin Lee, Young-Kwan Kim, Yang-Kang So, Jae-Sung Ryu, Seung-Han Oh, Yeon-Soo Han, Kinarm Ko, Young-Kug Choo, Sung-Joo Park, Robert Brodzik, Kyoung-Ki Lee, Doo-Byoung Oh, Kyung-A Hwang, Hilary Koprowski, Yong Seong Lee, Kisung Ko
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/428e53c252f04074bd013423f1c0bc9e
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spelling	oai:doaj.org-article:428e53c252f04074bd013423f1c0bc9e2021-11-18T08:59:33ZIntracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.1932-620310.1371/journal.pone.0068772https://doaj.org/article/428e53c252f04074bd013423f1c0bc9e2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23967055/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Plant genetic engineering, which has led to the production of plant-derived monoclonal antibodies (mAb(P)s), provides a safe and economically effective alternative to conventional antibody expression methods. In this study, the expression levels and biological properties of the anti-rabies virus mAb(P) SO57 with or without an endoplasmic reticulum (ER)-retention peptide signal (Lys-Asp-Glu-Leu; KDEL) in transgenic tobacco plants (Nicotiana tabacum) were analyzed. The expression levels of mAb(P) SO57 with KDEL (mAb(P)K) were significantly higher than those of mAb(P) SO57 without KDEL (mAb(P)) regardless of the transcription level. The Fc domains of both purified mAb(P) and mAb(P)K and hybridoma-derived mAb (mAb(H)) had similar levels of binding activity to the FcγRI receptor (CD64). The mAb(P)K had glycan profiles of both oligomannose (OM) type (91.7%) and Golgi type (8.3%), whereas the mAb(P) had mainly Golgi type glycans (96.8%) similar to those seen with mAb(H). Confocal analysis showed that the mAb(P)K was co-localized to ER-tracker signal and cellular areas surrounding the nucleus indicating accumulation of the mAb(P) with KDEL in the ER. Both mAb(P) and mAb(P)K disappeared with similar trends to mAb(H) in BALB/c mice. In addition, mAb(P)K was as effective as mAb(H) at neutralizing the activity of the rabies virus CVS-11. These results suggest that the ER localization of the recombinant mAb(P) by KDEL reprograms OM glycosylation and enhances the production of the functional antivirus therapeutic antibody in the plant.Jeong-Hwan LeeDa-Young ParkKyung-Jin LeeYoung-Kwan KimYang-Kang SoJae-Sung RyuSeung-Han OhYeon-Soo HanKinarm KoYoung-Kug ChooSung-Joo ParkRobert BrodzikKyoung-Ki LeeDoo-Byoung OhKyung-A HwangHilary KoprowskiYong Seong LeeKisung KoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e68772 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jeong-Hwan Lee Da-Young Park Kyung-Jin Lee Young-Kwan Kim Yang-Kang So Jae-Sung Ryu Seung-Han Oh Yeon-Soo Han Kinarm Ko Young-Kug Choo Sung-Joo Park Robert Brodzik Kyoung-Ki Lee Doo-Byoung Oh Kyung-A Hwang Hilary Koprowski Yong Seong Lee Kisung Ko Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
description	Plant genetic engineering, which has led to the production of plant-derived monoclonal antibodies (mAb(P)s), provides a safe and economically effective alternative to conventional antibody expression methods. In this study, the expression levels and biological properties of the anti-rabies virus mAb(P) SO57 with or without an endoplasmic reticulum (ER)-retention peptide signal (Lys-Asp-Glu-Leu; KDEL) in transgenic tobacco plants (Nicotiana tabacum) were analyzed. The expression levels of mAb(P) SO57 with KDEL (mAb(P)K) were significantly higher than those of mAb(P) SO57 without KDEL (mAb(P)) regardless of the transcription level. The Fc domains of both purified mAb(P) and mAb(P)K and hybridoma-derived mAb (mAb(H)) had similar levels of binding activity to the FcγRI receptor (CD64). The mAb(P)K had glycan profiles of both oligomannose (OM) type (91.7%) and Golgi type (8.3%), whereas the mAb(P) had mainly Golgi type glycans (96.8%) similar to those seen with mAb(H). Confocal analysis showed that the mAb(P)K was co-localized to ER-tracker signal and cellular areas surrounding the nucleus indicating accumulation of the mAb(P) with KDEL in the ER. Both mAb(P) and mAb(P)K disappeared with similar trends to mAb(H) in BALB/c mice. In addition, mAb(P)K was as effective as mAb(H) at neutralizing the activity of the rabies virus CVS-11. These results suggest that the ER localization of the recombinant mAb(P) by KDEL reprograms OM glycosylation and enhances the production of the functional antivirus therapeutic antibody in the plant.
format	article
author	Jeong-Hwan Lee Da-Young Park Kyung-Jin Lee Young-Kwan Kim Yang-Kang So Jae-Sung Ryu Seung-Han Oh Yeon-Soo Han Kinarm Ko Young-Kug Choo Sung-Joo Park Robert Brodzik Kyoung-Ki Lee Doo-Byoung Oh Kyung-A Hwang Hilary Koprowski Yong Seong Lee Kisung Ko
author_facet	Jeong-Hwan Lee Da-Young Park Kyung-Jin Lee Young-Kwan Kim Yang-Kang So Jae-Sung Ryu Seung-Han Oh Yeon-Soo Han Kinarm Ko Young-Kug Choo Sung-Joo Park Robert Brodzik Kyoung-Ki Lee Doo-Byoung Oh Kyung-A Hwang Hilary Koprowski Yong Seong Lee Kisung Ko
author_sort	Jeong-Hwan Lee
title	Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
title_short	Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
title_full	Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
title_fullStr	Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
title_full_unstemmed	Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
title_sort	intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/428e53c252f04074bd013423f1c0bc9e
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Intracellular reprogramming of expression, glycosylation, and function of a plant-derived antiviral therapeutic monoclonal antibody.

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