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Selection for a periplasmic factor improving phage display and functional periplasmic expression.

Abstract：

:The efficiency of both phage display in Escherichia coli and periplasmic expression of recombinant proteins may be limited by the same periplasmic folding steps. To search for E. coli factors that improve the efficiency of both procedures, a library of E. coli proteins was coexpressed in a phagemid vector that contained a poorly folding single-chain Fv antibody (scFv) fragment fused to g3p. We enriched, by panning for antigen binding, those phagemids in which the amount of displayed scFv is highest. We thus identified the periplasmic protein Skp/OmpH/HlpA as improving phage display of a wide range of scFv fragments. This occurs as a result of an increase in the amount of hybrid protein displayed on the phage. Coexpression of skp also increases the functional yield of scFv fragments when expressed by secretion to the periplasm.

journal_name

Nat Biotechnol

journal_title

Nature biotechnology

authors

Bothmann H,Plückthun A

doi

10.1038/nbt0498-376

subject

Has Abstract

pub_date

1998-04-01 00:00:00

pages

376-80

issue

4

eissn

1087-0156

issn

1546-1696

journal_volume

16

pub_type

杂志文章

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