| Modulation of infectivity in phage display as a tool to determine the substrate specificity of proteases. | |
| | |
MedLine Citation:
|
PMID: 16642518 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Proteases play an important role in human and animal diseases. Rapid determination of substrate specificity is possible through the use of substrate phage display; however, current methods possess several drawbacks. They require phage-immobilization and cannot be used for infectivity-destroying or affinity tag-destroying proteases; this can make entire libraries useless. To overcome these limitations, here we introduce infectivity-modulated phage display (IMOP). IMOP uses a protease-resistant and infectivity-reducing tag fused to substrate-displaying polyvalent phages, and the specific cleavage of the substrate increases the infectivity of the phages by releasing the infectivity-reducing tag. The resulting phages were first tested with the infectivity-destroying detergent protease subtilisin; this resulted in a highly specific substrate at a 200-fold enrichment. In a second example, the protease ompT was used and led to an enrichment of the known double-arginine motif. The IMOP system thus substantially improves and simplifies previous systems. |
| | |
Authors:
|
Javier F Chaparro-Riggers; Roland Breves; Karl-Heinz Maurer; Uwe Bornscheuer |
Related Documents
:
|
8994788 - Antimicrobial resistance in organisms causing diarrheal disease. 146868 - Comparison of therapeutic efficacy of doxycycline, chlortetracycline and lincomycin-spe... 21718568 - Chlamydia (uncomplicated, genital). 15917288 - Emergence of enterobacteriaceae producing extended-spectrum beta-lactamases (esbls) in ... 8135318 - Nosocomial blood-borne infection secondary to intravascular devices. 1210528 - The location of taenia pisiformis, taenia ovis and taenia hydatigena in the gut of the ... |
Publication Detail:
|
Type: Journal Article |
Journal Detail:
|
Title: Chembiochem : a European journal of chemical biology Volume: 7 ISSN: 1439-4227 ISO Abbreviation: Chembiochem Publication Date: 2006 Jun |
Date Detail:
|
Created Date: 2006-05-31 Completed Date: 2006-11-08 Revised Date: 2012-07-11 |
Medline Journal Info:
|
Nlm Unique ID: 100937360 Medline TA: Chembiochem Country: Germany |
Other Details:
|
Languages: eng Pagination: 965-70 Citation Subset: IM |
Affiliation:
|
Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, Soldmannstrasse 16, 17487 Greifswald, Germany. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Peptide Hydrolases
/
chemistry* Peptide Library* Serine Endopeptidases / chemistry, metabolism Substrate Specificity Subtilisin / chemistry, metabolism |
| Chemical | |
Reg. No./Substance:
|
0/Peptide Library; EC 3.4.-/Peptide Hydrolases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.62/Subtilisin; EC 3.4.23.49/omptin outer membrane protease |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Shape control of semiconductor and metal oxide nanocrystals through nonhydrolytic colloidal routes.
Next Document: Heteropolynuclear palladium complexes with pyrazolate and its 3-tert-butyl derivatives: the effect o...