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Protein Science (2007), 16:2260-2271. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments

Marylène Vandevenne1, Patrice Filee1, Natacha Scarafone2, Benoît Cloes1, Gilles Gaspard1, Nursel Yilmaz1, Mireille Dumoulin2, Jean-Marie François1, Jean-Marie Frère2, and Moreno Galleni1

1 Macromolécules Biologiques, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège, Belgium
2 Laboratoire d'Enzymologie, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège, Belgium

(RECEIVED April 2, 2007; FINAL REVISION July 13, 2007; ACCEPTED July 15, 2007)

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.

Keywords: beta-Lactamase; domain insertion; protein engineering; hybrid protein; chitin-binding domain; protein stability


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