<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Faber BW</submitter><funding>Medical Research Council</funding><pagination>5947-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2168333</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>75(12)</volume><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</pubmed_abstract><journal>Infection and immunity</journal><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.</pubmed_title><pmcid>PMC2168333</pmcid><funding_grant_id>MC_U117532067</funding_grant_id><pubmed_authors>Kocken CH</pubmed_authors><pubmed_authors>Morgan WD</pubmed_authors><pubmed_authors>Remarque EJ</pubmed_authors><pubmed_authors>Faber BW</pubmed_authors><pubmed_authors>Thomas AW</pubmed_authors><pubmed_authors>Holder AA</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007 Dec</publication><modification>2025-04-21T15:28:11.267Z</modification><creation>2019-03-27T02:22:20Z</creation></dates><accession>S-EPMC2168333</accession><cross_references><pubmed>17938224</pubmed><doi>10.1128/IAI.01804-06</doi><doi>10.1128/iai.01804-06</doi></cross_references></HashMap>