The Bacillus Licheniformis BlaP Beta-lactamase As a Model Protein Scaffold to Study the Insertion of Protein Fragments

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2007 Sep 26

PMID 17893363

Citations 14

Authors

Marylene Vandevenne

Patrice Filee

Natacha Scarafone

Benoit Cloes

Gilles Gaspard

Nursel Yilmaz

Mireille Dumoulin

Jean-Marie Francois

Jean-Marie Frere

Moreno Galleni

Affiliations

Soon will be listed here.

Abstract

Using genetic engineering technologies, the chitin-binding domain (ChBD) of the human macrophage chitotriosidase has been inserted into the host protein BlaP, a class A beta-lactamase produced by Bacillus licheniformis. The product of this construction behaved as a soluble chimeric protein that conserves both the capacity to bind chitin and to hydrolyze beta-lactam moiety. Here we describe the biochemical and biophysical properties of this protein (BlaPChBD). This work contributes to a better understanding of the reciprocal structural and functional effects of the insertion on the host protein scaffold and the heterologous structured protein fragments. The use of BlaP as a protein carrier represents an efficient approach to the functional study of heterologous protein fragments.

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