Chimeric cytotoxin IL2-PE40 inhibits relapsing experimental allergic encephalomyelitis

John W. Rose; Haya Lorberboum-Galski; David Fitzgerald; Richard McCarron; Kenneth E. Hill; Jeannette J. Townsend; Ira Pastan

doi:10.1016/0165-5728(91)90190-I

Chimeric cytotoxin IL2-PE40 inhibits relapsing experimental allergic encephalomyelitis

John W. Rose^*
, Haya Lorberboum-Galski
, David Fitzgerald
, Richard McCarron
, Kenneth E. Hill
, Jeannette J. Townsend
, Ira Pastan

^*Corresponding author for this work

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

30 Scopus citations

Abstract

IL2-PE40 is a chimeric protein composed of human interleukin-2 (IL2) genetically fused to a modified form of Pseudomonas exotoxin lacking the cell recognition domain. IL2-PE40 is cytotoxic for IL2 receptor-bearing lymphocytes in culture and can inhibit activation of T cells in vivo. IL2-PE40 can significantly diminish antigen-stimulated proliferation of lymphocytes sensitized to myelin basic protein. Intraperitoneal administration of IL2-PE40 not only markedly inhibits the clinical manifestations of adoptively transferred relapsing experimental allergic encephalomyelitis but also dramatically reduces both inflammation and demyelination characteristic of the disease.

Original language	English
Pages (from-to)	209-217
Number of pages	9
Journal	Journal of Neuroimmunology
Volume	32
Issue number	3
DOIs	https://doi.org/10.1016/0165-5728(91)90190-I
State	Published - Jun 1991
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by VA Merit Review Funds and by Research Grant 1929-A-1 from the Multiple Sclerosis Society. We gratefully acknowledge the technical assistance of Craig Kamerath, Greg Gilson, Beckie McLain and Huschang Komeyli.

Funding Information:
Supported by VA Merit Review and Research Grant 1929-A-1 from the National Multiple Sclerosis Society, U.S.A.

Keywords

Chimeric cytotoxin
Experimental allergic encephalomyelitis
Interleukin-2
Pseudomonas exotoxin

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10.1016/0165-5728(91)90190-I

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title = "Chimeric cytotoxin IL2-PE40 inhibits relapsing experimental allergic encephalomyelitis",

abstract = "IL2-PE40 is a chimeric protein composed of human interleukin-2 (IL2) genetically fused to a modified form of Pseudomonas exotoxin lacking the cell recognition domain. IL2-PE40 is cytotoxic for IL2 receptor-bearing lymphocytes in culture and can inhibit activation of T cells in vivo. IL2-PE40 can significantly diminish antigen-stimulated proliferation of lymphocytes sensitized to myelin basic protein. Intraperitoneal administration of IL2-PE40 not only markedly inhibits the clinical manifestations of adoptively transferred relapsing experimental allergic encephalomyelitis but also dramatically reduces both inflammation and demyelination characteristic of the disease.",

keywords = "Chimeric cytotoxin, Experimental allergic encephalomyelitis, Interleukin-2, Pseudomonas exotoxin",

author = "Rose, \{John W.\} and Haya Lorberboum-Galski and David Fitzgerald and Richard McCarron and Hill, \{Kenneth E.\} and Townsend, \{Jeannette J.\} and Ira Pastan",

note = "Funding Information: This work was supported by VA Merit Review Funds and by Research Grant 1929-A-1 from the Multiple Sclerosis Society. We gratefully acknowledge the technical assistance of Craig Kamerath, Greg Gilson, Beckie McLain and Huschang Komeyli. Funding Information: Supported by VA Merit Review and Research Grant 1929-A-1 from the National Multiple Sclerosis Society, U.S.A.",

year = "1991",

month = jun,

doi = "10.1016/0165-5728(91)90190-I",

language = "אנגלית",

volume = "32",

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journal = "Journal of Neuroimmunology",

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T1 - Chimeric cytotoxin IL2-PE40 inhibits relapsing experimental allergic encephalomyelitis

AU - Rose, John W.

AU - Lorberboum-Galski, Haya

AU - Fitzgerald, David

AU - McCarron, Richard

AU - Hill, Kenneth E.

AU - Townsend, Jeannette J.

AU - Pastan, Ira

N1 - Funding Information: This work was supported by VA Merit Review Funds and by Research Grant 1929-A-1 from the Multiple Sclerosis Society. We gratefully acknowledge the technical assistance of Craig Kamerath, Greg Gilson, Beckie McLain and Huschang Komeyli. Funding Information: Supported by VA Merit Review and Research Grant 1929-A-1 from the National Multiple Sclerosis Society, U.S.A.

PY - 1991/6

Y1 - 1991/6

N2 - IL2-PE40 is a chimeric protein composed of human interleukin-2 (IL2) genetically fused to a modified form of Pseudomonas exotoxin lacking the cell recognition domain. IL2-PE40 is cytotoxic for IL2 receptor-bearing lymphocytes in culture and can inhibit activation of T cells in vivo. IL2-PE40 can significantly diminish antigen-stimulated proliferation of lymphocytes sensitized to myelin basic protein. Intraperitoneal administration of IL2-PE40 not only markedly inhibits the clinical manifestations of adoptively transferred relapsing experimental allergic encephalomyelitis but also dramatically reduces both inflammation and demyelination characteristic of the disease.

AB - IL2-PE40 is a chimeric protein composed of human interleukin-2 (IL2) genetically fused to a modified form of Pseudomonas exotoxin lacking the cell recognition domain. IL2-PE40 is cytotoxic for IL2 receptor-bearing lymphocytes in culture and can inhibit activation of T cells in vivo. IL2-PE40 can significantly diminish antigen-stimulated proliferation of lymphocytes sensitized to myelin basic protein. Intraperitoneal administration of IL2-PE40 not only markedly inhibits the clinical manifestations of adoptively transferred relapsing experimental allergic encephalomyelitis but also dramatically reduces both inflammation and demyelination characteristic of the disease.

KW - Chimeric cytotoxin

KW - Experimental allergic encephalomyelitis

KW - Interleukin-2

KW - Pseudomonas exotoxin

UR - https://www.scopus.com/pages/publications/0025797474

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AN - SCOPUS:0025797474

SN - 0165-5728

VL - 32

SP - 209

EP - 217

JO - Journal of Neuroimmunology

JF - Journal of Neuroimmunology

IS - 3

ER -

Chimeric cytotoxin IL2-PE40 inhibits relapsing experimental allergic encephalomyelitis

Abstract

Bibliographical note

Keywords

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