Tetrahymena thermophila Granule Lattice Protein 3 Improves Solubility of Sexual Stage Malaria Antigens Expressed in Escherichia coli
| Autor: | Theodore G. Clark, Donna Cassidy-Hanley, Cengiz Akkale |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Plasmodium falciparum
Protozoan Proteins Antibodies Protozoan Antigens Protozoan medicine.disease_cause Article Tetrahymena thermophila law.invention Maltose-binding protein Antigen law Malaria Vaccines Lattice protein Escherichia coli medicine Humans Solubility Escherichia coli Infections biology Chemistry Granule (cell biology) Tetrahymena biology.organism_classification Malaria Biochemistry biology.protein Recombinant DNA Biotechnology |
| Zdroj: | Protein Expr Purif |
| DOI: | 10.1101/2021.06.29.450425 |
| Popis: | The 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. |
| Databáze: | OpenAIRE |
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