Tetrahymena thermophila granule lattice protein 3 improves solubility of sexual stage malaria antigens expressed in Escherichia coli

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dc.authoridAKKALE, CENGIZ/0000-0002-9537-7104
dc.contributor.authorAkkale, Cengiz
dc.contributor.authorCassidy-Hanley, Donna Marie
dc.contributor.authorClark, Theodore G.
dc.date.accessioned2025-01-06T17:43:32Z
dc.date.available2025-01-06T17:43:32Z
dc.date.issued2022
dc.description.abstractThe requirement for low cost manufacturing makes bacterial cells a logical platform for the production of recombinant subunit vaccines for malaria. However, protein solubility has been a major stumbling block with prokaryotic expression systems. Notable examples include the transmission blocking vaccine candidates, Pfs25 and Pfs48/45, which are almost entirely insoluble when expressed as recombinant proteins in Escherichia coli. Various solubility tags have been used with limited success in improving solubility, although recent studies with granule lattice protein 1 (Grl1p) from the ciliated protozoan, Tetrahymena thermophila, have shown promise. Here, we examine a related solubility tag, granule lattice protein 3 (Grl3p) from T. thermophila, and compare it to both Grl1p and the well-studied maltose binding protein (MBP) used to improve the solubility of multiple protein targets. We find that Grl3p performs comparably to Grl1p when linked to Pfs25 but significantly improves solubility when paired with Pfs48/45.
dc.identifier.doi10.1016/j.pep.2022.106060
dc.identifier.issn1046-5928
dc.identifier.issn1096-0279
dc.identifier.pmid35134517
dc.identifier.scopus2-s2.0-85124487252
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1016/j.pep.2022.106060
dc.identifier.urihttps://hdl.handle.net/20.500.14669/2698
dc.identifier.volume194
dc.identifier.wosWOS:000776069300005
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherAcademic Press Inc Elsevier Science
dc.relation.ispartofProtein Expression and Purification
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_20241211
dc.subjectMalaria
dc.subjectVaccine
dc.subjectTransmission blocking
dc.subjectTetrahymena thermophila
dc.subjectGranule lattice protein
dc.titleTetrahymena thermophila granule lattice protein 3 improves solubility of sexual stage malaria antigens expressed in Escherichia coli
dc.typeArticle

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