Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin

Joan E. Smallshaw; James A. Richardson; Seth Pincus; John Schindler; Ellen S. Vitetta

doi:10.1016/j.vaccine.2005.04.037

Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin

Joan E. Smallshaw, James A. Richardson, Seth Pincus, John Schindler, Ellen S. Vitetta

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

71 Scopus citations

Abstract

Ricin toxin is a plant-derived ribosome inactivating protein (RIP) of extraordinary toxicity. Vaccination using ricin toxoid or its A chain (RTA) is protective in animals but both vaccines have two potential toxicities, RIP and vascular leak syndrome (VLS). Previously we described three recombinant RTA constructs from which both toxicities were eliminated by site-specific mutations. One mutant, V76M/Y80A, RiVax, has now been further characterized for immunogenicity and toxicity in animals. We have found that RiVax is safe at doses of at least 8 mg in mice, 800-fold higher than the protective dose, and induces neutralizing antibodies in both mice and rabbits.

Original language	English (US)
Pages (from-to)	4775-4784
Number of pages	10
Journal	Vaccine
Volume	23
Issue number	39
DOIs	https://doi.org/10.1016/j.vaccine.2005.04.037
State	Published - Sep 15 2005

Keywords

Bioterrorism
RiVax
Ricin
Vaccine

ASJC Scopus subject areas

Molecular Medicine
Immunology and Microbiology(all)
veterinary(all)
Public Health, Environmental and Occupational Health
Infectious Diseases

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10.1016/j.vaccine.2005.04.037

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title = "Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin",

abstract = "Ricin toxin is a plant-derived ribosome inactivating protein (RIP) of extraordinary toxicity. Vaccination using ricin toxoid or its A chain (RTA) is protective in animals but both vaccines have two potential toxicities, RIP and vascular leak syndrome (VLS). Previously we described three recombinant RTA constructs from which both toxicities were eliminated by site-specific mutations. One mutant, V76M/Y80A, RiVax, has now been further characterized for immunogenicity and toxicity in animals. We have found that RiVax is safe at doses of at least 8 mg in mice, 800-fold higher than the protective dose, and induces neutralizing antibodies in both mice and rabbits.",

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T1 - Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin

AU - Smallshaw, Joan E.

AU - Richardson, James A.

AU - Pincus, Seth

AU - Schindler, John

AU - Vitetta, Ellen S.

PY - 2005/9/15

Y1 - 2005/9/15

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AB - Ricin toxin is a plant-derived ribosome inactivating protein (RIP) of extraordinary toxicity. Vaccination using ricin toxoid or its A chain (RTA) is protective in animals but both vaccines have two potential toxicities, RIP and vascular leak syndrome (VLS). Previously we described three recombinant RTA constructs from which both toxicities were eliminated by site-specific mutations. One mutant, V76M/Y80A, RiVax, has now been further characterized for immunogenicity and toxicity in animals. We have found that RiVax is safe at doses of at least 8 mg in mice, 800-fold higher than the protective dose, and induces neutralizing antibodies in both mice and rabbits.

KW - Bioterrorism

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KW - Ricin

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Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin

Abstract

Keywords

ASJC Scopus subject areas

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