Effect of Domain Manipulation in the Staphylococcal Phage Endolysin, Endo88, on Lytic Efficiency and Host Range
Author:
Funder
Kementerian Pendidikan Malaysia
Universiti Putra Malaysia
Publisher
Springer Science and Business Media LLC
Link
https://link.springer.com/content/pdf/10.1007/s12033-024-01216-4.pdf
Reference27 articles.
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2. Becker, S. C., Dong, S., Baker, J. R., Foster-Frey, J., Pritchard, D. G., & Donovan, D. M. (2009). LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells. FEMS Microbiology Letters, 294(1), 52–60. https://doi.org/10.1111/j.1574-6968.2009.01541.x
3. Becker, S. C., Foster-Frey, J., Stodola, A. J., Anacker, D., & Donovan, D. M. (2009). Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. Gene, 443(1–2), 32–41. https://doi.org/10.1016/j.gene.2009.04.023
4. Becker, S. C., Swift, S., Korobova, O., Schischkova, N., Kopylov, P., Donovan, D. M., & Abaev, I. (2015). Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain. FEMS Microbiology Letters, 362(1), 1–8. https://doi.org/10.1093/femsle/fnu019
5. Benešík, M., Nováček, J., Janda, L., Dopitová, R., Pernisová, M., Melková, K., Tišáková, L., Doškař, J., Žídek, L., Hejátko, J., & Pantůček, R. (2018). Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity. Virus Genes, 54(1), 130–139. https://doi.org/10.1007/s11262-017-1507-2
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