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Open AccessArticle

The Auxiliary Role of the Amidase Domain in Cell Wall Binding and Exolytic Activity of Staphylococcal Phage Endolysins

by Bokyung Son 1,2,†, Minsuk Kong 1,2,†,‡ and Sangryeol Ryu 1,2,*
1
Laboratory of Molecular Food Microbiology, Department of Food and Animal Biotechnology, Seoul National University, Seoul 08826, Korea
2
Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 08826, Korea
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Current address: Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Viruses 2018, 10(6), 284; https://doi.org/10.3390/v10060284
Received: 25 April 2018 / Revised: 17 May 2018 / Accepted: 24 May 2018 / Published: 25 May 2018
(This article belongs to the Special Issue Phage Lytic Enzymes and Their Applications)
In response to increasing concern over antibiotic-resistant Staphylococcus aureus, the development of novel antimicrobials has been called for, with bacteriophage endolysins having received considerable attention as alternatives to antibiotics. Most staphylococcal phage endolysins have a modular structure consisting of an N-terminal cysteine, histidine-dependent amidohydrolases/peptidase domain (CHAP), a central amidase domain, and a C-terminal cell wall binding domain (CBD). Despite extensive studies using truncated staphylococcal endolysins, the precise function of the amidase domain has not been determined. Here, a functional analysis of each domain of two S. aureus phage endolysins (LysSA12 and LysSA97) revealed that the CHAP domain conferred the main catalytic activity, while the central amidase domain showed no enzymatic activity in degrading the intact S. aureus cell wall. However, the amidase-lacking endolysins had reduced hydrolytic activity compared to the full-length endolysins. Comparison of the binding affinities of fusion proteins consisting of the green fluorescent protein (GFP) with CBD and GFP with the amidase domain and CBD revealed that the major function of the amidase domain was to enhance the binding affinity of CBD, resulting in higher lytic activity of endolysin. These results suggest an auxiliary binding role of the amidase domain of staphylococcal endolysins, which can be useful information for designing effective antimicrobial and diagnostic agents against S. aureus. View Full-Text
Keywords: Staphylococcus aureus; endolysin; amidase domain; cell wall binding Staphylococcus aureus; endolysin; amidase domain; cell wall binding
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Son, B.; Kong, M.; Ryu, S. The Auxiliary Role of the Amidase Domain in Cell Wall Binding and Exolytic Activity of Staphylococcal Phage Endolysins. Viruses 2018, 10, 284.

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