Tetrahymena thermophila granule lattice protein 3 improves solubility of sexual stage malaria antigens expressed in Escherichia coli.
Tetrahymena thermophila granule lattice protein 3 improves solubility of sexual stage malaria antigens expressed in Escherichia coli.
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DOI:
10.1016/j.pep.2022.106060
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发表时间:
2022-06
影响因子:
1.6
通讯作者:
Clark, Theodore G.
中科院分区:
文献类型:
--
作者:
Akkale, Cengiz;Cassidy-Hanley, Donna Marie;Clark, Theodore G.
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.
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影响因子:
3.7
作者:
Chowdhury DR;Angov E;Kariuki T;Kumar N
通讯作者:
Kumar N
DOI:
10.1084/jem.174.5.1203
发表时间:
1991-11-01
期刊:
The Journal of experimental medicine
影响因子:
--
作者:
Barr PJ;Green KM;Gibson HL;Bathurst IC;Quakyi IA;Kaslow DC
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Kaslow DC
影响因子:
3.3
作者:
Cowan, AT;Bowman, GR;Turkewitz, AP
通讯作者:
Turkewitz, AP
影响因子:
8.8
作者:
Angrisano F;Sala KA;Da DF;Liu Y;Pei J;Grishin NV;Snell WJ;Blagborough AM
通讯作者:
Blagborough AM
DOI:
10.1073/pnas.96.24.13703
发表时间:
1999-11-23
影响因子:
11.1
作者:
Bessette, PH;Åslund, F;Georgiou, G
通讯作者:
Georgiou, G