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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

Engineering sortase A by screening a second-generation library using phage display.

Lena Schmohl¹, Jan Bierlmeier¹, Fabian Gerth²

¹Interfaculty Institute of Biochemistry, University of Tübingen, Hoppe-Seyler-Str. 4, D-72076, Tübingen, Germany.

Journal of Peptide Science : an Official Publication of the European Peptide Society

|February 11, 2017

Summary

This summary is machine-generated.

Researchers engineered sortase enzymes for protein modification. New sortase mutants recognize different protein sequences, expanding the versatility of sortase-mediated ligation for biotechnological applications.

Keywords:

directed evolution phage display protein engineering sortase A sortase-mediated ligation

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Last Updated: Mar 7, 2026

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

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Published on: October 15, 2016

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Published on: January 17, 2015

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

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Published on: August 8, 2016

Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Sortase-mediated ligation is a key chemo-enzymatic technique for site-specific protein modification.
Existing sortase methods rely on the canonical LPxTG recognition motif.

Purpose of the Study:

To develop a new library of sortase mutants for directed evolution.
To engineer sortase enzymes with altered substrate selectivity.

Main Methods:

Established a second-generation sortase mutant library.
Utilized phage display screening to identify functional mutants.

Main Results:

Identified sortase mutants capable of ligating proteins with APxTG or FPxTG recognition sequences.
Demonstrated successful engineering of sortase substrate selectivity.

Conclusions:

The second-generation sortase library enables enhanced sortase engineering.
These advancements increase the versatility of sortase-mediated ligation techniques.