Premium
Bacterial surface display of an anti‐pollutant antibody fragment
Author(s) -
Dhillon J. K.,
Drew P. D.,
Porter A. J. R.
Publication year - 1999
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1365-2672.1999.00552.x
Subject(s) - atrazine , bioremediation , escherichia coli , antibody , pollutant , chemistry , lysis , alkaline phosphatase , conjugate , bacteria , peptidoglycan , microbiology and biotechnology , biochemistry , biology , cell wall , environmental chemistry , enzyme , pesticide , ecology , immunology , mathematical analysis , genetics , mathematics , organic chemistry , gene
A peptidoglycan‐associated lipoprotein (PAL) fused to an antibody fragment (scFv) specific to the herbicide and environmental pollutant atrazine, has been successfully targeted to the cell surface of Escherichia coli. Anti‐atrazine binding could be observed via an atrazine‐alkaline phosphatase conjugate. Cells containing the PAL fusion grew with little cellular toxicity when compared with the control. In contrast, expression of anti‐atrazine antibody fragments alone caused the cells to lyse after 4 h. The surface display of anti‐pollutant antibodies may have a future role in the bioremediation of contaminated water or the development of pollutant‐specific, whole‐cell biosensors.