Cell receptor specific targeted toxins: Genetic construction and characterization of an interleukin 2 diphtheria toxin-related fusion protein

J. R. Murphy; D. P. Williams; P. Bacha; W. Bishai; C. Waters; T. B. Strom

doi:10.3109/10799898809049005

Cell receptor specific targeted toxins: Genetic construction and characterization of an interleukin 2 diphtheria toxin-related fusion protein

J. R. Murphy, D. P. Williams, P. Bacha, W. Bishai, C. Waters, T. B. Strom

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

5 Scopus citations

Abstract

We have genetically replaced the diphtheria toxin receptor binding domain with a DNA insert encoding the T-cell growth factor interleukin-2 (IL-2). The toxin-related IL-2 fusion gene encodes a 70,586 dalton protein, pro-IL-2-toxin. The mature form of IL-2-toxin is exported to the periplasmic space of recombinant Escherichia coli and has a molecular weight of 68,086. IL-2-toxin has been partially purified from periplasmic extracts of recombinant E. coli, and it is shown to contain immunologic determinants intrinsic to both its diphtheria toxin and IL-2 components. The chimeric toxin is targeted toward IL-2 receptor bearing T-cells in vitro.

Original language	English (US)
Pages (from-to)	467-480
Number of pages	14
Journal	Journal of Receptors and Signal Transduction
Volume	8
Issue number	1-4
DOIs	https://doi.org/10.3109/10799898809049005
State	Published - 1988
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.3109/10799898809049005

Cite this

@article{70ad968589804c94a345365c55d0710d,

title = "Cell receptor specific targeted toxins: Genetic construction and characterization of an interleukin 2 diphtheria toxin-related fusion protein",

abstract = "We have genetically replaced the diphtheria toxin receptor binding domain with a DNA insert encoding the T-cell growth factor interleukin-2 (IL-2). The toxin-related IL-2 fusion gene encodes a 70,586 dalton protein, pro-IL-2-toxin. The mature form of IL-2-toxin is exported to the periplasmic space of recombinant Escherichia coli and has a molecular weight of 68,086. IL-2-toxin has been partially purified from periplasmic extracts of recombinant E. coli, and it is shown to contain immunologic determinants intrinsic to both its diphtheria toxin and IL-2 components. The chimeric toxin is targeted toward IL-2 receptor bearing T-cells in vitro.",

author = "Murphy, {J. R.} and Williams, {D. P.} and P. Bacha and W. Bishai and C. Waters and Strom, {T. B.}",

note = "Funding Information: ACKNOWLEDGEMENTS This research was supparted in part by Public Health Service grants AI-21628 (JRM) and AI-22882 (TBS) from the National Institute of Allergy and Infectious Diseases, and grant CA-41746 (JRM) from the National Cancer Tnstitute. We thank Dr. Robert Schwartz, Tufts Medical School, Boston, MA, and Dr. John Williams, Harvard Medical School, Boston, MA, for providing eukaryotic cell lines. The authors wish to thank Dr. Frank Genbauffe for many helpful discussions.",

year = "1988",

doi = "10.3109/10799898809049005",

language = "English (US)",

volume = "8",

pages = "467--480",

journal = "Journal of Receptors and Signal Transduction",

issn = "1079-9893",

publisher = "Informa Healthcare",

number = "1-4",

}

TY - JOUR

T1 - Cell receptor specific targeted toxins

T2 - Genetic construction and characterization of an interleukin 2 diphtheria toxin-related fusion protein

AU - Murphy, J. R.

AU - Williams, D. P.

AU - Bacha, P.

AU - Bishai, W.

AU - Waters, C.

AU - Strom, T. B.

N1 - Funding Information: ACKNOWLEDGEMENTS This research was supparted in part by Public Health Service grants AI-21628 (JRM) and AI-22882 (TBS) from the National Institute of Allergy and Infectious Diseases, and grant CA-41746 (JRM) from the National Cancer Tnstitute. We thank Dr. Robert Schwartz, Tufts Medical School, Boston, MA, and Dr. John Williams, Harvard Medical School, Boston, MA, for providing eukaryotic cell lines. The authors wish to thank Dr. Frank Genbauffe for many helpful discussions.

PY - 1988

Y1 - 1988

N2 - We have genetically replaced the diphtheria toxin receptor binding domain with a DNA insert encoding the T-cell growth factor interleukin-2 (IL-2). The toxin-related IL-2 fusion gene encodes a 70,586 dalton protein, pro-IL-2-toxin. The mature form of IL-2-toxin is exported to the periplasmic space of recombinant Escherichia coli and has a molecular weight of 68,086. IL-2-toxin has been partially purified from periplasmic extracts of recombinant E. coli, and it is shown to contain immunologic determinants intrinsic to both its diphtheria toxin and IL-2 components. The chimeric toxin is targeted toward IL-2 receptor bearing T-cells in vitro.

AB - We have genetically replaced the diphtheria toxin receptor binding domain with a DNA insert encoding the T-cell growth factor interleukin-2 (IL-2). The toxin-related IL-2 fusion gene encodes a 70,586 dalton protein, pro-IL-2-toxin. The mature form of IL-2-toxin is exported to the periplasmic space of recombinant Escherichia coli and has a molecular weight of 68,086. IL-2-toxin has been partially purified from periplasmic extracts of recombinant E. coli, and it is shown to contain immunologic determinants intrinsic to both its diphtheria toxin and IL-2 components. The chimeric toxin is targeted toward IL-2 receptor bearing T-cells in vitro.

UR - http://www.scopus.com/inward/record.url?scp=0023924190&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023924190&partnerID=8YFLogxK

U2 - 10.3109/10799898809049005

DO - 10.3109/10799898809049005

M3 - Article

C2 - 3133472

AN - SCOPUS:0023924190

SN - 1079-9893

VL - 8

SP - 467

EP - 480

JO - Journal of Receptors and Signal Transduction

JF - Journal of Receptors and Signal Transduction

IS - 1-4

ER -

Cell receptor specific targeted toxins: Genetic construction and characterization of an interleukin 2 diphtheria toxin-related fusion protein

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this