Lytic enzymes of staphylococcal phages: Correlation between secondary structure and stability

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• 作者：L. Y. Filatova ; D. M. Donovan ; J. A. Foster-Frey…
• 关键词：Staphylococcus aureus ; phage lysins ; secondary structure ; stability
• 刊名：Moscow University Chemistry Bulletin
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：71
• 期：1
• 页码：7-11
• 全文大小：431 KB
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  9.Filatova, L.Y., Donovan, D.M., Foster-Frey, J., Pugachev, V.G., Dmitrieva, N.F., Chubar, T.A., Klyachko, N.L., and Kabanov, A.V., Enzyme Microb. Technol., 2015, vols. 73–74, p. 51.CrossRef
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• 作者单位：L. Y. Filatova (1)
  D. M. Donovan (2)
  J. A. Foster-Frey (2)
  V. G. Pugachev (3)
  E. V. Kudryashova (1)
  N. L. Klyachko (1)
  
  1. Moscow State University, Moscow, 119991, Russia
  2. Animal and Natural Resources Institute, Agricultural Research Center, Beltsville, MD, 20705, USA
  3. Vector State Research Center of Virology and Biotechnology, Novosibirsk, Russia
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Chemistry
  Russian Library of Science
  
• 出版者：Allerton Press, Inc. distributed exclusively by Springer Science+Business Media LLC
• ISSN：1935-0260

文摘

Lytic enzymes of bacteriophages K, phi11, and phi80α can lyse (destroy) cells of antibiotic-resistant strains of Staphylococcus aureus, which makes these enzymes promising antimicrobial agents. The stability of recombinant lysins of phages K, phi11, and phi80α was investigated under the conditions of storage and functioning, and the correlation between the stability and the secondary structure of the enzymes was found. It has been shown that the lower the content of disordered structures in the enzyme molecules, the greater the stability (half-inactivation time) of the lysins. At the storage temperature, the beta-structural lysin of phage phi11 shows the highest stability, while the phage K lysin with an alpha-helical structure and the phi80α lysin with a disordered secondary structure are less stable.