Phage display of a double-headed proteinase inhibitor: Analysis of the binding domains of potato proteinase inhibitor II View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-06

AUTHORS

Maarten A. Jongsma, Petra L. Bakker, Willem J. Stiekema, Dirk Bosch

ABSTRACT

Potato proteinase inhibitor II (PI2) is a serine proteinase inhibitor composed of two domains that are thought to bind independently to proteinases. To determine the activities of each domain separately, various inactive and active domain combinations were constructed by substituting amino acid residues in the active domains by alanines. These derivatives were expressed as soluble protein inEscherichia coli and exposed on M13 phage as fusions to gene 3 in a phagemid system for monovalent phage display. Inactivation of both active domains by Ala residues reduced binding of phage to trypsin and chymotrypsin by 95%. Ten times more phage were bound to proteinases by domain II compared to domain I, while a point mutation (Leu5 → Arg) altered the binding specificity of domain I of PI2 phage from chymotrypsin to trypsin. The mutants were used to show that functional PI2 phage mixed with nonfunctional PI2 phage could be enriched 323 000-fold after three rounds of panning. Thus, these results open up the possibility to use phage display for the selection of engineered PI2 derivatives with improved binding characteristics towards digestive proteinases of plants pests. More... »

PAGES

181-191

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01249702

DOI

http://dx.doi.org/10.1007/bf01249702

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047931526


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