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Process development and cGMP manufacturing of a recombinant ricin vaccine: an effective and stable recombinant ricin A-chain vaccine-RVEc™.
Meagher, Michael M; Seravalli, Javier G; Swanson, S Todd; Ladd, Roger G; Khasa, Yogender P; Inan, Mehmet; Harner, Jay C; Johnson, Scott K; Van Cott, Kevin; Lindsey, Changhong; Wannemacher, Robert; Smith, Leonard A.
Afiliación
  • Meagher MM; University of Nebraska-Lincoln Biological Process Development Facility, College of Engineering, University of Nebraska-Lincoln, Lincoln, NE 68588-0668, USA.
Biotechnol Prog ; 27(4): 1036-47, 2011 Jul.
Article en En | MEDLINE | ID: mdl-21630488
Ricin is a potent toxin and a potential bioterrorism weapon with no specific countermeasures or vaccines available. The holotoxin is composed of two polypeptide chains linked by a single disulfide bond: the A-chain (RTA), which is an N-glycosidase enzyme, and the B-chain (RTB), a lectin polypeptide that binds galactosyl moieties on the surface of the mammalian target cells. Previously (McHugh et al.), a recombinant truncated form of RTA (rRTA1-33/44-198 protein, herein denoted RVEa™) expressed in Escherichia coli using a codon-optimized gene was shown to be non-toxic, stable, and protective against a ricin challenge in mice. Here, we describe the process development and scale-up at the 12 L fermentation scale, and the current Good Manufacturing Practice (cGMP)-compliant production of RVEc™ at the 40 L scale. The average yield of the final purified bulk RVEc™ is approximately 16 g/kg of wet cell weight or 1.2 g/L of fermentation broth. The RVEc™ was >99% pure by three HPLC methods and SDS-PAGE. The intact mass and peptide mapping analysis of RVEc™ confirmed the identity of the product and is consistent with the absence of posttranslational modifications. Potency assays demonstrated that RVEc™ was immunoprotective against lethal ricin challenge and elicited neutralizing anti-ricin antibodies in 95-100% of the vaccinated mice.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ricina / Vacunas Sintéticas Límite: Animals Idioma: En Revista: Biotechnol Prog Asunto de la revista: BIOTECNOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ricina / Vacunas Sintéticas Límite: Animals Idioma: En Revista: Biotechnol Prog Asunto de la revista: BIOTECNOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos