The production of a genus-specific recombinant antibody (scFv) using a recombinant potyvirus protease

Research output: Contribution to journalArticleResearchpeer review

Authors

External Research Organisations

  • Technische Universität Braunschweig
View graph of relations

Details

Original languageEnglish
Pages (from-to)225-233
JournalJournal of Virological Methods
Volume106
Issue number2
Publication statusPublished - 2002

Abstract

A single chain variable fragment antibody (scFv; anti-NIa scFv102) was selected from a synthetic human antibody library by using a NIa protease of Plum pox virus (PPV) as an antigen, which was expressed in bacteria. The NIa protease forms the nuclear inclusion body A and acts as the major protease in the cleavage of the viral polyprotein into functional proteins. The NIa protein was detected with anti-NIa scFv102 after expression in Escherichia coli cells as well as from PPV-infected Nicotiana benthamiana plants. Furthermore, the scFv102 has the ability to identify not only PPV from infected plants but also can detect other infections with members of the potyviruses. Nineteen different potyviruses were recognized by the scFv102 in various infected plants tested through dot blot assays. Therefore, the antibody scFv102 has the potential of becoming a general tool to detect potyvirus infections in different plant species. ?? 2002 Published by Elsevier Science B.V.

Cite this

The production of a genus-specific recombinant antibody (scFv) using a recombinant potyvirus protease. / Reinard, Thomas; Maiß, Edgar; Hust, Michael.
In: Journal of Virological Methods, Vol. 106, No. 2, 2002, p. 225-233.

Research output: Contribution to journalArticleResearchpeer review

Download
@article{148dd513fc73413680e2571cdad2cdcb,
title = "The production of a genus-specific recombinant antibody (scFv) using a recombinant potyvirus protease",
abstract = "A single chain variable fragment antibody (scFv; anti-NIa scFv102) was selected from a synthetic human antibody library by using a NIa protease of Plum pox virus (PPV) as an antigen, which was expressed in bacteria. The NIa protease forms the nuclear inclusion body A and acts as the major protease in the cleavage of the viral polyprotein into functional proteins. The NIa protein was detected with anti-NIa scFv102 after expression in Escherichia coli cells as well as from PPV-infected Nicotiana benthamiana plants. Furthermore, the scFv102 has the ability to identify not only PPV from infected plants but also can detect other infections with members of the potyviruses. Nineteen different potyviruses were recognized by the scFv102 in various infected plants tested through dot blot assays. Therefore, the antibody scFv102 has the potential of becoming a general tool to detect potyvirus infections in different plant species. ?? 2002 Published by Elsevier Science B.V.",
author = "Thomas Reinard and Edgar Mai{\ss} and Michael Hust",
note = "Funding information: The generous gift of virus-infected plants from Dr. Vetten, BBA Braunschweig, Germany, is gratefully acknowledged. We thank Imdadul Hoque for helpful comments on the manuscript. This work is supported by the Ministry of Science and Culture (MWK) of the state Lower Saxony.",
year = "2002",
doi = "10.1016/S0166-0934(02)00166-0",
language = "English",
volume = "106",
pages = "225--233",
journal = "Journal of Virological Methods",
issn = "0166-0934",
publisher = "Elsevier",
number = "2",

}

Download

TY - JOUR

T1 - The production of a genus-specific recombinant antibody (scFv) using a recombinant potyvirus protease

AU - Reinard, Thomas

AU - Maiß, Edgar

AU - Hust, Michael

N1 - Funding information: The generous gift of virus-infected plants from Dr. Vetten, BBA Braunschweig, Germany, is gratefully acknowledged. We thank Imdadul Hoque for helpful comments on the manuscript. This work is supported by the Ministry of Science and Culture (MWK) of the state Lower Saxony.

PY - 2002

Y1 - 2002

N2 - A single chain variable fragment antibody (scFv; anti-NIa scFv102) was selected from a synthetic human antibody library by using a NIa protease of Plum pox virus (PPV) as an antigen, which was expressed in bacteria. The NIa protease forms the nuclear inclusion body A and acts as the major protease in the cleavage of the viral polyprotein into functional proteins. The NIa protein was detected with anti-NIa scFv102 after expression in Escherichia coli cells as well as from PPV-infected Nicotiana benthamiana plants. Furthermore, the scFv102 has the ability to identify not only PPV from infected plants but also can detect other infections with members of the potyviruses. Nineteen different potyviruses were recognized by the scFv102 in various infected plants tested through dot blot assays. Therefore, the antibody scFv102 has the potential of becoming a general tool to detect potyvirus infections in different plant species. ?? 2002 Published by Elsevier Science B.V.

AB - A single chain variable fragment antibody (scFv; anti-NIa scFv102) was selected from a synthetic human antibody library by using a NIa protease of Plum pox virus (PPV) as an antigen, which was expressed in bacteria. The NIa protease forms the nuclear inclusion body A and acts as the major protease in the cleavage of the viral polyprotein into functional proteins. The NIa protein was detected with anti-NIa scFv102 after expression in Escherichia coli cells as well as from PPV-infected Nicotiana benthamiana plants. Furthermore, the scFv102 has the ability to identify not only PPV from infected plants but also can detect other infections with members of the potyviruses. Nineteen different potyviruses were recognized by the scFv102 in various infected plants tested through dot blot assays. Therefore, the antibody scFv102 has the potential of becoming a general tool to detect potyvirus infections in different plant species. ?? 2002 Published by Elsevier Science B.V.

U2 - 10.1016/S0166-0934(02)00166-0

DO - 10.1016/S0166-0934(02)00166-0

M3 - Article

VL - 106

SP - 225

EP - 233

JO - Journal of Virological Methods

JF - Journal of Virological Methods

SN - 0166-0934

IS - 2

ER -

By the same author(s)