Abstract
Endolysin from Staphylococcus aureus phage SA97 (LysSA97) was cloned and investigated. LysSA97 specifically lyse the staphylococcal strains and effectively disrupted staphylococcal biofilms. Bioinformatic analysis of LysSA97 revealed a novel putative cell wall binding domain (CBD) as well as two enzymatically active domains (EADs) containing cysteine, histidine-dependent amidohydrolases/peptidases (CHAP, PF05257) and N-acetylmuramoyl-L-alanine amidase (Amidase-3, PF01520) domains. Comparison of 98 endolysin genes of S. aureus phages deposited in GenBank showed that they can be classified into six groups based on their domain composition. Interestingly, approximately 80.61 % of the staphylococcal endolysins have a src-homology 3 (SH3, PF08460) domain as CBD, but the remaining 19.39 %, including LysSA97, has a putative C-terminal CBD with no homology to the known CBD. The fusion protein containing green fluorescent protein and the putative CBD of LysSA97 showed a specific binding spectrum against staphylococcal cells comparable to SH3 domain (PF08460), suggesting that the C-terminal domain of LysSA97 is a novel CBD of staphylococcal endolysins.
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Acknowledgments
We thank Dr. Bok Luel Lee at Pusan National University for sharing S. aureus strains (Newman and RN4220 wild-type strains). This work was supported by Agriculture, Food and Rural Affairs Research Center Support Program, Ministry of Agriculture, Food and Rural Affairs, and the National Research Foundation of Korea (NRF) grant funded by the MSIP (NRF-2014R1A2A1A10051563), Republic of Korea.
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Chang, Y., Ryu, S. Characterization of a novel cell wall binding domain-containing Staphylococcus aureus endolysin LysSA97. Appl Microbiol Biotechnol 101, 147–158 (2017). https://doi.org/10.1007/s00253-016-7747-6
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DOI: https://doi.org/10.1007/s00253-016-7747-6