Recombinant Protein Expression Unit (RPEU)

Kaslow, D C.

Abstract

This new initiative is to develop and support a recombinant protein expression unit, RPEU, designed to identify suitable expression systems to produce milligram to gram amounts of adequately folded and post- translationally modified proteins for early stages of vaccine development and for structural studies. The RPEU will consist of 1) a molecular biology group for designing and engineering recombinant DNA for transfection into bacteria, yeast and baculovirus; 2) a production group which will analyze protein production and optimize fermentation conditions from the resultant recombinant bacteria, yeast and baculovirus-infected insect cells; 3) a protein purification and analysis group that will work on post-production process development and will do the preliminary analysis of the resultant recombinant protein for structural and immunological integrity; and 4) a collaborative group that will include LPD and extramural investigators whose major goal will be studying the functional/immunological and structural characteristics of the recombinant malaria parasite proteins produced.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Allergy and Infectious Diseases (NIAID)
• Type: Intramural Research (Z01)
• Project #: 1Z01AI000727-01
• Application #: 5200611
• Support Year: 1
• Fiscal Year: 1995

Institution

• Name: National Institute of Allergy and Infectious Diseases
• Country: United States

Publications

Collins, William E; Barnwell, John W; Sullivan, Joann S et al. (2006) Assessment of transmission-blocking activity of candidate Pvs25 vaccine using gametocytes from chimpanzees. Am J Trop Med Hyg 74:215-21

Tsai, Chiawei W; Duggan, Peter F; Shimp Jr, Richard L et al. (2006) Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris. J Biotechnol 121:458-70

Makobongo, Morris O; Keegan, Brian; Long, Carole A et al. (2006) Immunization of Aotus monkeys with recombinant cysteine-rich interdomain region 1 alpha protects against severe disease during Plasmodium falciparum reinfection. J Infect Dis 193:731-40

Wille-Reece, Ulrike; Flynn, Barbara J; Lore, Karin et al. (2006) Toll-like receptor agonists influence the magnitude and quality of memory T cell responses after prime-boost immunization in nonhuman primates. J Exp Med 203:1249-58

Giersing, Birgitte K; Dubovsky, Filip; Saul, Allan et al. (2006) Potency assay design for adjuvanted recombinant proteins as malaria vaccines. Vaccine 24:4264-70

Trinh, Loc; Phue, Je-Nie; Jaluria, Pratik et al. (2006) Screen-less expanded bed column: new approach for the recovery and purification of a malaria transmission blocking vaccine candidate from Pichia pastoris. Biotechnol Lett 28:951-8

Saxena, Ajay K; Singh, Kavita; Su, Hua-Poo et al. (2006) The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms. Nat Struct Mol Biol 13:90-1

Mullen, Gregory E D; Giersing, Birgitte K; Ajose-Popoola, Olubunmi et al. (2006) Enhancement of functional antibody responses to AMA1-C1/Alhydrogel, a Plasmodium falciparum malaria vaccine, with CpG oligodeoxynucleotide. Vaccine 24:2497-505

Woehlbier, Ute; Epp, Christian; Kauth, Christian W et al. (2006) Analysis of antibodies directed against merozoite surface protein 1 of the human malaria parasite Plasmodium falciparum. Infect Immun 74:1313-22

Shimp Jr, Richard L; Martin, Laura B; Zhang, Yanling et al. (2006) Production and characterization of clinical grade Escherichia coli derived Plasmodium falciparum 42 kDa merozoite surface protein 1 (MSP1(42)) in the absence of an affinity tag. Protein Expr Purif 50:58-67