Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2011-9-22
pubmed:abstractText
The creation of subunit vaccines to prevent malaria infection has been hampered by the intrinsically weak immunogenicity of the recombinant antigens. We have developed a novel strategy to increase immune responses by creating genetic fusion proteins to target specific antigen-presenting cells (APCs). The fusion complex was composed of three physically linked molecular entities: (i) a vaccine antigen, (ii) a multimeric ?-helical coiled-coil core, and (iii) an APC-targeting ligand linked to the core via a flexible linker. The vaccine efficacy of the tricomponent complex was evaluated using an ookinete surface protein of Plasmodium vivax, Pvs25, and merozoite surface protein-1 of Plasmodium yoelii. Immunization of mice with the tricomponent complex induced a robust antibody response and conferred substantial levels of P. vivax transmission blockade as evaluated by a membrane feed assay, as well as protection from lethal P. yoelii infection. The observed effect was strongly dependent on the presence of all three components physically integrated as a fusion complex. This system, designated the tricomponent immunopotentiating system (TIPS), onto which any recombinant protein antigens or nonproteinaceous substances could be loaded, may be a promising strategy for devising subunit vaccines or adjuvants against various infectious diseases, including malaria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Malaria Vaccines, http://linkedlifedata.com/resource/pubmed/chemical/Merozoite Surface Protein 1, http://linkedlifedata.com/resource/pubmed/chemical/Pvs25 protein, P vivax, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Subunit, http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Synthetic, http://linkedlifedata.com/resource/pubmed/chemical/cartilage matrix protein
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1098-5522
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4260-75
pubmed:meshHeading
pubmed-meshheading:21807905-Amino Acid Sequence, pubmed-meshheading:21807905-Animals, pubmed-meshheading:21807905-Antigen-Presenting Cells, pubmed-meshheading:21807905-Antigens, Protozoan, pubmed-meshheading:21807905-Antigens, Surface, pubmed-meshheading:21807905-B-Lymphocytes, pubmed-meshheading:21807905-Base Sequence, pubmed-meshheading:21807905-Drug Design, pubmed-meshheading:21807905-Extracellular Matrix Proteins, pubmed-meshheading:21807905-Female, pubmed-meshheading:21807905-Glycoproteins, pubmed-meshheading:21807905-Ligands, pubmed-meshheading:21807905-Lymphocyte Activation, pubmed-meshheading:21807905-Malaria, pubmed-meshheading:21807905-Malaria, Vivax, pubmed-meshheading:21807905-Malaria Vaccines, pubmed-meshheading:21807905-Merozoite Surface Protein 1, pubmed-meshheading:21807905-Mice, pubmed-meshheading:21807905-Mice, Inbred BALB C, pubmed-meshheading:21807905-Mice, Inbred C57BL, pubmed-meshheading:21807905-Molecular Sequence Data, pubmed-meshheading:21807905-Plasmodium vivax, pubmed-meshheading:21807905-Plasmodium yoelii, pubmed-meshheading:21807905-Recombinant Fusion Proteins, pubmed-meshheading:21807905-Vaccines, Subunit, pubmed-meshheading:21807905-Vaccines, Synthetic
pubmed:year
2011
pubmed:articleTitle
Tricomponent immunopotentiating system as a novel molecular design strategy for malaria vaccine development.
pubmed:affiliation
Molecular Microbiology Group, Tropical Biosphere Research Center, COMB, University of the Ryukyus, Okinawa Japan. tarakawa@comb.u-ryukyu.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't