Amino Terminal Fusion of Heterologous Proteins to CotC Increases Display Efficiencies in the Bacillus Subtilis Spore System
Author(s) -
Rachele Isticato,
Donatella Scotto Di Mase,
Emilia M. F. Mauriello,
Maurilio De Felice,
Ezio Ricca
Publication year - 2007
Publication title -
biotechniques
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.617
H-Index - 131
eISSN - 1940-9818
pISSN - 0736-6205
DOI - 10.2144/000112329
Subject(s) - bacillus subtilis , heterologous , spore , bacillales , biology , bacillaceae , amino acid , microbiology and biotechnology , biochemistry , fusion protein , chemistry , bacteria , recombinant dna , genetics , gene
Show Me the Protein The key to phage or bacteria protein display technologies is the ability to display as much protein as possible on the cell surface. Recently, several groups have utilized Bacillus subtilis spores for the purpose of displaying heterologous proteins. Isticato et al. demonstrate that the current Bacillus spore display method can be improved up to 5-fold with a simple modification. Fusion of a heterologous protein to a coat protein, CotC, directs the heterologous protein to the surface of the Bacillus spore for display. The authors found that fusion of the heterologous protein to the amino terminus of the CotC protein results in a dramatic increase in the amount of heterologous protein displayed on the spore surface. They validated this work by examining CotC fusions to both green fluorescent protein and the C fragment of the tetanus toxin and found that, in both cases, fusion to the amino terminus of CotC increases display efficiencies when directly compared to fusions to the carboxyl te...
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