Abstract
Viable Escherichia coli populations are chromatographically retained on a matrix containing immobilized starch. This retention is dependent upon the LamB protein (the λ receptor) in the outer membrane and can be reversed by maltodextrin ligands of the receptor. Mutants altered in LamB structure or regulation can be isolated from a wild-type population on the basis of differences in Chromatographic retention of mutant cells. In particular, a new class of phage λ-sensitive lamB missense mutant with altered affinities for starch/maltodextrins could be isolated in this way. These results suggest that affinity chromatography of cells offers a function-directed genetic selection for changes in surface receptor structure or expression.
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