Site-specific tetrameric streptavidin-protein conjugation using sortase A.

Abstract:

:Streptavidin is tetrameric protein which has tight and specific biotin binding affinity, and streptavidin modification of proteins or small molecules is widely used for biotechnology tool. Here, we demonstrate site-specific streptavidin-protein conjugation using enzymes. We focused on sortase A, a transpeptidase from Staphylococcus aureus. A streptavidin-tagged LPETG motif (Stav-LPETG) was expressed in Escherichia coli. We achieved soluble streptavidin expression in E. coli without refolding using a cold shock expression system. Then we successfully conjugated Stav-LPETG with pentaglycine-appended green fluorescence protein (Gly5-GFP) or triglycine-appended glucose oxidase (Gly3-GOD) using sortase A. SDS-PAGE analysis showed site-specific tetrameric streptavidin-protein conjugation with the tagged proteins. In addition, the functions of a Stav-GOD conjugate, i.e., biotin-binding and glucose oxidase activity, were significantly higher compared to those of streptavidin-GOD conjugates prepared by chemical modification.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Matsumoto T,Sawamoto S,Sakamoto T,Tanaka T,Fukuda H,Kondo A

doi

10.1016/j.jbiotec.2011.01.008

subject

Has Abstract

pub_date

2011-03-10 00:00:00

pages

37-42

issue

1-2

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(11)00052-6

journal_volume

152

pub_type

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