In vivo reconstitution of ricin-like activity from its A and B chain subunits

William Cushley, Michael J. Muirhead, Fred Silva, Joyce Greathouse, Thomas Tucker, Jonathan W. Uhr, Ellen S. Vitetta

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The capacity of highly purified preparations of ricin A and B chains to reconstitute ricin toxicity both in vitro and in vivo was studied. When the nontoxic A and B chain subunits were mixed and electrophoresed on sodium dodecyl sulphate-polyacrylamide gels (SDS-PAGE), reconstituted ricin was observed. The mixtures killed cells of the human Burkityt's lymphoma cell line Daudi in vitro and killed mice after i.v. injection. It was also shown that when mice were injected with one ricin subunit followed by administration of the complementary polypeptide up to 8 hr later, they died with lesions similar to those of ricin-induced death. This observation suggests that A and B chains recombine either in the serum or on the surface of cells. The rate of clearance of A and B chains from the blood of rats indicated that sufficient concentrations of either chain were present in the circulation 8 hr after injection to account for the observed toxicity. The above studies therefore suggest that the subunits of ricin have a very high affinity for each other and are capable of reconstituting biologically active ricin in vitro and in injected mice.

Original languageEnglish (US)
Pages (from-to)265-277
Number of pages13
JournalToxicon
Volume22
Issue number2
DOIs
StatePublished - 1984

Fingerprint

Ricin
Toxicity
Cells
Injections
Sodium Dodecyl Sulfate
Rats
Lymphoma
Blood
Cell Line
Peptides

ASJC Scopus subject areas

  • Toxicology

Cite this

Cushley, W., Muirhead, M. J., Silva, F., Greathouse, J., Tucker, T., Uhr, J. W., & Vitetta, E. S. (1984). In vivo reconstitution of ricin-like activity from its A and B chain subunits. Toxicon, 22(2), 265-277. https://doi.org/10.1016/0041-0101(84)90027-8

In vivo reconstitution of ricin-like activity from its A and B chain subunits. / Cushley, William; Muirhead, Michael J.; Silva, Fred; Greathouse, Joyce; Tucker, Thomas; Uhr, Jonathan W.; Vitetta, Ellen S.

In: Toxicon, Vol. 22, No. 2, 1984, p. 265-277.

Research output: Contribution to journalArticle

Cushley, W, Muirhead, MJ, Silva, F, Greathouse, J, Tucker, T, Uhr, JW & Vitetta, ES 1984, 'In vivo reconstitution of ricin-like activity from its A and B chain subunits', Toxicon, vol. 22, no. 2, pp. 265-277. https://doi.org/10.1016/0041-0101(84)90027-8
Cushley W, Muirhead MJ, Silva F, Greathouse J, Tucker T, Uhr JW et al. In vivo reconstitution of ricin-like activity from its A and B chain subunits. Toxicon. 1984;22(2):265-277. https://doi.org/10.1016/0041-0101(84)90027-8
Cushley, William ; Muirhead, Michael J. ; Silva, Fred ; Greathouse, Joyce ; Tucker, Thomas ; Uhr, Jonathan W. ; Vitetta, Ellen S. / In vivo reconstitution of ricin-like activity from its A and B chain subunits. In: Toxicon. 1984 ; Vol. 22, No. 2. pp. 265-277.
@article{fc9e1ee6d9854174a48b3753ccd1728d,
title = "In vivo reconstitution of ricin-like activity from its A and B chain subunits",
abstract = "The capacity of highly purified preparations of ricin A and B chains to reconstitute ricin toxicity both in vitro and in vivo was studied. When the nontoxic A and B chain subunits were mixed and electrophoresed on sodium dodecyl sulphate-polyacrylamide gels (SDS-PAGE), reconstituted ricin was observed. The mixtures killed cells of the human Burkityt's lymphoma cell line Daudi in vitro and killed mice after i.v. injection. It was also shown that when mice were injected with one ricin subunit followed by administration of the complementary polypeptide up to 8 hr later, they died with lesions similar to those of ricin-induced death. This observation suggests that A and B chains recombine either in the serum or on the surface of cells. The rate of clearance of A and B chains from the blood of rats indicated that sufficient concentrations of either chain were present in the circulation 8 hr after injection to account for the observed toxicity. The above studies therefore suggest that the subunits of ricin have a very high affinity for each other and are capable of reconstituting biologically active ricin in vitro and in injected mice.",
author = "William Cushley and Muirhead, {Michael J.} and Fred Silva and Joyce Greathouse and Thomas Tucker and Uhr, {Jonathan W.} and Vitetta, {Ellen S.}",
year = "1984",
doi = "10.1016/0041-0101(84)90027-8",
language = "English (US)",
volume = "22",
pages = "265--277",
journal = "Toxicon",
issn = "0041-0101",
publisher = "Elsevier Limited",
number = "2",

}

TY - JOUR

T1 - In vivo reconstitution of ricin-like activity from its A and B chain subunits

AU - Cushley, William

AU - Muirhead, Michael J.

AU - Silva, Fred

AU - Greathouse, Joyce

AU - Tucker, Thomas

AU - Uhr, Jonathan W.

AU - Vitetta, Ellen S.

PY - 1984

Y1 - 1984

N2 - The capacity of highly purified preparations of ricin A and B chains to reconstitute ricin toxicity both in vitro and in vivo was studied. When the nontoxic A and B chain subunits were mixed and electrophoresed on sodium dodecyl sulphate-polyacrylamide gels (SDS-PAGE), reconstituted ricin was observed. The mixtures killed cells of the human Burkityt's lymphoma cell line Daudi in vitro and killed mice after i.v. injection. It was also shown that when mice were injected with one ricin subunit followed by administration of the complementary polypeptide up to 8 hr later, they died with lesions similar to those of ricin-induced death. This observation suggests that A and B chains recombine either in the serum or on the surface of cells. The rate of clearance of A and B chains from the blood of rats indicated that sufficient concentrations of either chain were present in the circulation 8 hr after injection to account for the observed toxicity. The above studies therefore suggest that the subunits of ricin have a very high affinity for each other and are capable of reconstituting biologically active ricin in vitro and in injected mice.

AB - The capacity of highly purified preparations of ricin A and B chains to reconstitute ricin toxicity both in vitro and in vivo was studied. When the nontoxic A and B chain subunits were mixed and electrophoresed on sodium dodecyl sulphate-polyacrylamide gels (SDS-PAGE), reconstituted ricin was observed. The mixtures killed cells of the human Burkityt's lymphoma cell line Daudi in vitro and killed mice after i.v. injection. It was also shown that when mice were injected with one ricin subunit followed by administration of the complementary polypeptide up to 8 hr later, they died with lesions similar to those of ricin-induced death. This observation suggests that A and B chains recombine either in the serum or on the surface of cells. The rate of clearance of A and B chains from the blood of rats indicated that sufficient concentrations of either chain were present in the circulation 8 hr after injection to account for the observed toxicity. The above studies therefore suggest that the subunits of ricin have a very high affinity for each other and are capable of reconstituting biologically active ricin in vitro and in injected mice.

UR - http://www.scopus.com/inward/record.url?scp=0021364173&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021364173&partnerID=8YFLogxK

U2 - 10.1016/0041-0101(84)90027-8

DO - 10.1016/0041-0101(84)90027-8

M3 - Article

C2 - 6729842

AN - SCOPUS:0021364173

VL - 22

SP - 265

EP - 277

JO - Toxicon

JF - Toxicon

SN - 0041-0101

IS - 2

ER -