Merozoite surface protein-1 of Plasmodium yoelii fused via an oligosaccharide moiety of cholera toxin B subunit glycoprotein expressed in yeast induced protective immunity against lethal malaria infection in mice

Highlights ► Yeast Pichia pastoris produced cholera toxin B subunit (CTB) as a glycoprotein. ► Oligosaccharide (OS) extends from the lateral circumference of the CTB pentamer ring. ► The OS chain was exploited as an anchoring scaffold for a malaria antigen (MSP1). ► MSP1 fused via the OS chain induc...

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Veröffentlicht in:	Vaccine 2012-01, Vol.30 (5), p.948-958
Hauptverfasser:	Miyata, Takeshi, Harakuni, Tetsuya, Taira, Toki, Matsuzaki, Goro, Arakawa, Takeshi
Format:	Artikel
Sprache:	eng
Schlagworte:	Administration, Intranasal Allergy and Immunology Animals antigens binding capacity cholera toxin Cholera Toxin - genetics Cholera Toxin - immunology CTB Delivery system Disease Models, Animal edema Female gangliosides glycoproteins Glycoproteins - genetics Glycoproteins - immunology glycosylation immunity immunization Injections, Subcutaneous Malaria Malaria - immunology Malaria - prevention & control Malaria Vaccines - administration & dosage Malaria Vaccines - genetics Malaria Vaccines - immunology Merozoite Surface Protein 1 - genetics Merozoite Surface Protein 1 - immunology merozoites Mice Mice, Inbred BALB C Mice, Inbred C57BL oligosaccharides parasites Pichia - genetics Pichia - metabolism Pichia pastoris Plasmodium yoelii Plasmodium yoelii - genetics Plasmodium yoelii - immunology protein bodies Subunit vaccine Survival Analysis vaccines Vaccines, Conjugate - administration & dosage Vaccines, Conjugate - genetics Vaccines, Conjugate - immunology Vaccines, Synthetic - administration & dosage Vaccines, Synthetic - genetics Vaccines, Synthetic - immunology yeasts
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Beschreibung
Zusammenfassung:	Highlights ► Yeast Pichia pastoris produced cholera toxin B subunit (CTB) as a glycoprotein. ► Oligosaccharide (OS) extends from the lateral circumference of the CTB pentamer ring. ► The OS chain was exploited as an anchoring scaffold for a malaria antigen (MSP1). ► MSP1 fused via the OS chain induced increased protection against malaria infection. ► Increased protection was due to higher Ag loading capacity of the CTB glycoprotein.
ISSN:	0264-410X 1873-2518
DOI:	10.1016/j.vaccine.2011.11.059