期刊
PLANT BIOTECHNOLOGY JOURNAL
卷 15, 期 9, 页码 1130-1140出版社
WILEY
DOI: 10.1111/pbi.12703
关键词
antimicrobials; Chlamydomonas reinhardtii; chloroplast; Pal; Cpl-1; endolysin
资金
- UK's Biotechnology and Biological Sciences Research Council [BB/F016948/1, BB/I007660/1]
- UCL
- Supreme Biotechnologies Ltd.
- Biotechnology and Biological Sciences Research Council [BB/L002957/1, BB/I007660/1, 1352461] Funding Source: researchfish
- BBSRC [BB/L002957/1, BB/I007660/1] Funding Source: UKRI
There is a pressing need to develop novel antibacterial agents given the widespread antibiotic resistance among pathogenic bacteria and the low specificity of the drugs available. Endolysins are antibacterial proteins that are produced by bacteriophage-infected cells to digest the bacterial cell wall for phage progeny release at the end of the lytic cycle. These highly efficient enzymes show a considerable degree of specificity for the target bacterium of the phage. Furthermore, the emergence of resistance against endolysins appears to be rare as the enzymes have evolved to target molecules in the cell wall that are essential for bacterial viability. Taken together, these factors make recombinant endolysins promising novel antibacterial agents. The chloroplast of the green unicellular alga Chlamydomonas reinhardtii represents an attractive platform for production of therapeutic proteins in general, not least due to the availability of established techniques for foreign gene expression, a lack of endotoxins or potentially infectious agents in the algal host, and low cost of cultivation. The chloroplast is particularly well suited to the production of endolysins as it mimics the native bacterial expression environment of these proteins while being devoid of their cell wall target. In this study, the endolysins Cpl-1 and Pal, specific to the major human pathogen Streptococcus pneumoniae, were produced in the C. reinhardtii chloroplast. The antibacterial activity of cell lysates and the isolated endolysins was demonstrated against different serotypes of S. pneumoniae, including clinical isolates and total recombinant protein yield was quantified at similar to 1.3 mg/g algal dry weight.
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