Reliable titration of filamentous bacteriophages independent of pIII fusion moiety and genome size by using trypsin to restore wild-type pIII phenotype.

Abstract:

:Phage display holds a key position in the use of combinatorial library approaches for the purpose of protein engineering and discovery. However, modifying the pIII protein of the phage can severely and negatively influence the infectiousness of the phage particle. This concern is particularly relevant when large pIII fusions in combination with multivalent display systems are in use. We here describe the use of trypsin to restore wild-type pIII phenotype as a small modification to the standard titration protocol. The results show that the trypsin treatment has a very large but heterogeneous effect on the phage infection efficiency, depending on the pIII fusion domain and the valence of display.

journal_name

Biotechniques

journal_title

BioTechniques

authors

Løset GÅ,Kristinsson SG,Sandlie I

doi

10.2144/000112724

subject

Has Abstract

pub_date

2008-04-01 00:00:00

pages

551-2, 554

issue

4

eissn

0736-6205

issn

1940-9818

pii

000112724

journal_volume

44

pub_type

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