Biological activity and intracellular location of the Tat protein of equine infectious anemia virus

Rina Rosin-Arbesfeldb; Pnina Mashiah; Dieter Willbold; Paul Rosch; Steven R. Tronick; Abraham Yaniv; Arnona Gazit

doi:10.1016/0378-1119(94)90443-X

Biological activity and intracellular location of the Tat protein of equine infectious anemia virus

Rina Rosin-Arbesfeldb, Pnina Mashiah, Dieter Willbold, Paul Rosch, Steven R. Tronick, Abraham Yaniv, Arnona Gazit^*

^*Corresponding author for this work

Clinical Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

Abstract

The Tat protein of equine infectious anemia virus (EIAV) was synthesized in Escherichia coli using the inducible expression plasmid, pET16b, which contains a His.Tag leader, thus allowing for rapid and efficient enrichment of the histidine-tagged protein by metal affinity chromatography. Yields of up to 20 mg of Tat were obtained from 10¹¹ bacterial cells. The recombinant Tat protein was shown to potently trans-activate the EIAV long terminal repeat (LTR) following its introduction into canine cells by 'scrape loading'. The EIAV Tat protein was found to localize predominantly within the cytoplasm, in contrast to HIV-1 Tat. The availability of large amounts of purified functional EIAV Tat protein should greatly facilitate detailed structure-function analyses.

Original language	English
Pages (from-to)	307-311
Number of pages	5
Journal	Gene
Volume	150
Issue number	2
DOIs	https://doi.org/10.1016/0378-1119(94)90443-X
State	Published - 1994

Keywords

EIAV
His tag
Recombinant protein
frans-activation
lentiviruses
pET prokaryotic expression vector

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0378-1119(94)90443-X

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title = "Biological activity and intracellular location of the Tat protein of equine infectious anemia virus",

abstract = "The Tat protein of equine infectious anemia virus (EIAV) was synthesized in Escherichia coli using the inducible expression plasmid, pET16b, which contains a His.Tag leader, thus allowing for rapid and efficient enrichment of the histidine-tagged protein by metal affinity chromatography. Yields of up to 20 mg of Tat were obtained from 1011 bacterial cells. The recombinant Tat protein was shown to potently trans-activate the EIAV long terminal repeat (LTR) following its introduction into canine cells by 'scrape loading'. The EIAV Tat protein was found to localize predominantly within the cytoplasm, in contrast to HIV-1 Tat. The availability of large amounts of purified functional EIAV Tat protein should greatly facilitate detailed structure-function analyses.",

keywords = "EIAV, His tag, Recombinant protein, frans-activation, lentiviruses, pET prokaryotic expression vector",

author = "Rina Rosin-Arbesfeldb and Pnina Mashiah and Dieter Willbold and Paul Rosch and Tronick, {Steven R.} and Abraham Yaniv and Arnona Gazit",

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AU - Rosin-Arbesfeldb, Rina

AU - Mashiah, Pnina

AU - Willbold, Dieter

AU - Rosch, Paul

AU - Tronick, Steven R.

AU - Yaniv, Abraham

AU - Gazit, Arnona

PY - 1994

Y1 - 1994

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KW - Recombinant protein

KW - frans-activation

KW - lentiviruses

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Biological activity and intracellular location of the Tat protein of equine infectious anemia virus

Abstract

Keywords

UN SDGs

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