Publication: Display of organophosphorus hydrolase on the cyanobacterial cell surface using synechococcus outer membrane protein a as an anchoring motif
Issued Date
2011-08-01
Resource Type
ISSN
15590291
02732289
02732289
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2-s2.0-79960091044
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Mahidol University
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SCOPUS
Bibliographic Citation
Applied Biochemistry and Biotechnology. Vol.164, No.7 (2011), 1048-1057
Suggested Citation
Wipa Chungjatupornchai, Attapon Kamlangdee, Sirirat Fa-Aroonsawat Display of organophosphorus hydrolase on the cyanobacterial cell surface using synechococcus outer membrane protein a as an anchoring motif. Applied Biochemistry and Biotechnology. Vol.164, No.7 (2011), 1048-1057. doi:10.1007/s12010-011-9193-3 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/11495
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Title
Display of organophosphorus hydrolase on the cyanobacterial cell surface using synechococcus outer membrane protein a as an anchoring motif
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Abstract
The display of proteins to cyanobacterial cell surface is made complex by combination of Gram-positive and Gram-negative features of cyanobacterial cell wall. Here, we showed that Synechococcus outer membrane protein A (SomA) can be used as an anchoring motif for the display of organophosphorus hydrolase (OPH) on cyanobacterial cell surface. The OPH, capable of degrading a wide range of organophosphate pesticides, was fused in frame to the carboxyl-terminus of different cell-surface exposed loops of SomA. Proteinase K accessibility assay and immunostaining visualized under confocal laser scanning microscopy demonstrated that a minor fraction of OPH with 12 histidines fused in frame with the third cell-surface exposed loop of SomA (SomAL3-OPH12H) was displayed onto the outermost cell surface with a substantial fraction buried in the cell wall, whereas OPH fused in frame with the fifth cell-surface exposed loop of SomA (SomAL5-OPH) was successfully translocated across the membrane and completely displayed onto the outermost surface of Synechococcus. The successful display of the functional heterologous protein on cell surface provides a useful model for variety of applications in cyanobacteria including screening of polypeptide libraries and whole-cell biocatalysts by immobilizing enzymes. © 2011 Springer Science+Business Media, LLC.