{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Faber BW"],"funding":["Medical Research Council"],"pagination":["5947-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2168333"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["75(12)"],"pubmed_abstract":["We show that the smallest module of Plasmodium falciparum AMA1 (PfAMA1) that can be expressed in the yeast Pichia pastoris while retaining the capacity to induce high levels of parasite-inhibitory antibodies comprises domains I and II. Based on this, two fusion proteins, differing in the order of the modules, were developed. Each comprised one module of PfAMA1 (FVO strain, amino acids [aa] 97 to 442) (module A) and one module of PfMSP1(19) (Wellcome strain, aa 1526 to 1621) (module Mm) in which a cystine had been removed to improve immune responses. Both fusion proteins retained the antigenicity of each component and yielded over 30 mg/liter purified protein under fed-batch fermentation. Rabbits immunized with purified fusion proteins MmA and AMm had up to eightfold-higher immune responses"],"journal":["Infection and immunity"],"pubmed_title":["Malaria vaccine-related benefits of a single protein comprising Plasmodium falciparum apical membrane antigen 1 domains I and II fused to a modified form of the 19-kilodalton C-terminal fragment of merozoite surface protein 1."],"pmcid":["PMC2168333"],"funding_grant_id":["MC_U117532067"],"pubmed_authors":["Kocken CH","Morgan WD","Remarque EJ","Faber BW","Thomas AW","Holder AA"],"additional_accession":[]},"is_claimable":false,"name":"Malaria vaccine-related benefits of a single protein comprising Plasmodium falciparum apical membrane antigen 1 domains I and II fused to a modified form of the 19-kilodalton C-terminal fragment of merozoite surface protein 1.","description":"We show that the smallest module of Plasmodium falciparum AMA1 (PfAMA1) that can be expressed in the yeast Pichia pastoris while retaining the capacity to induce high levels of parasite-inhibitory antibodies comprises domains I and II. Based on this, two fusion proteins, differing in the order of the modules, were developed. Each comprised one module of PfAMA1 (FVO strain, amino acids [aa] 97 to 442) (module A) and one module of PfMSP1(19) (Wellcome strain, aa 1526 to 1621) (module Mm) in which a cystine had been removed to improve immune responses. Both fusion proteins retained the antigenicity of each component and yielded over 30 mg/liter purified protein under fed-batch fermentation. Rabbits immunized with purified fusion proteins MmA and AMm had up to eightfold-higher immune responses","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Dec","modification":"2025-04-21T15:28:11.267Z","creation":"2019-03-27T02:22:20Z"},"accession":"S-EPMC2168333","cross_references":{"pubmed":["17938224"],"doi":["10.1128/IAI.01804-06","10.1128/iai.01804-06"]}}