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
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container_end_page 958
container_issue 5
container_start_page 948
container_title Vaccine
container_volume 30
creator Miyata, Takeshi
Harakuni, Tetsuya
Taira, Toki
Matsuzaki, Goro
Arakawa, Takeshi
description 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.
doi_str_mv 10.1016/j.vaccine.2011.11.059
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control</topic><topic>Malaria Vaccines - administration &amp; dosage</topic><topic>Malaria Vaccines - genetics</topic><topic>Malaria Vaccines - immunology</topic><topic>Merozoite Surface Protein 1 - genetics</topic><topic>Merozoite Surface Protein 1 - immunology</topic><topic>merozoites</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Inbred C57BL</topic><topic>oligosaccharides</topic><topic>parasites</topic><topic>Pichia - genetics</topic><topic>Pichia - metabolism</topic><topic>Pichia pastoris</topic><topic>Plasmodium yoelii</topic><topic>Plasmodium yoelii - genetics</topic><topic>Plasmodium yoelii - immunology</topic><topic>protein bodies</topic><topic>Subunit vaccine</topic><topic>Survival Analysis</topic><topic>vaccines</topic><topic>Vaccines, Conjugate - administration &amp; dosage</topic><topic>Vaccines, Conjugate - genetics</topic><topic>Vaccines, Conjugate - immunology</topic><topic>Vaccines, Synthetic - administration &amp; dosage</topic><topic>Vaccines, Synthetic - genetics</topic><topic>Vaccines, Synthetic - immunology</topic><topic>yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyata, Takeshi</creatorcontrib><creatorcontrib>Harakuni, Tetsuya</creatorcontrib><creatorcontrib>Taira, Toki</creatorcontrib><creatorcontrib>Matsuzaki, Goro</creatorcontrib><creatorcontrib>Arakawa, Takeshi</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyata, Takeshi</au><au>Harakuni, Tetsuya</au><au>Taira, Toki</au><au>Matsuzaki, Goro</au><au>Arakawa, Takeshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Vaccine</jtitle><addtitle>Vaccine</addtitle><date>2012-01-20</date><risdate>2012</risdate><volume>30</volume><issue>5</issue><spage>948</spage><epage>958</epage><pages>948-958</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><abstract>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.</abstract><cop>Netherlands</cop><pub>Elsevier Ltd</pub><pmid>22119928</pmid><doi>10.1016/j.vaccine.2011.11.059</doi><tpages>11</tpages></addata></record>
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source MEDLINE; ScienceDirect Journals (5 years ago - present); ProQuest Central UK/Ireland
subjects 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
title 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
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