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Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells

Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class na...

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Autores principales: Sykilinda, Nina N., Nikolaeva, Alena Y., Shneider, Mikhail M., Mishkin, Dmitry V., Patutin, Artem A., Popov, Vladimir O., Boyko, Konstantin M., Klyachko, Natalia L., Miroshnikov, Konstantin A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6024848/
https://www.ncbi.nlm.nih.gov/pubmed/29882827
http://dx.doi.org/10.3390/v10060309
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author Sykilinda, Nina N.
Nikolaeva, Alena Y.
Shneider, Mikhail M.
Mishkin, Dmitry V.
Patutin, Artem A.
Popov, Vladimir O.
Boyko, Konstantin M.
Klyachko, Natalia L.
Miroshnikov, Konstantin A.
author_facet Sykilinda, Nina N.
Nikolaeva, Alena Y.
Shneider, Mikhail M.
Mishkin, Dmitry V.
Patutin, Artem A.
Popov, Vladimir O.
Boyko, Konstantin M.
Klyachko, Natalia L.
Miroshnikov, Konstantin A.
author_sort Sykilinda, Nina N.
collection PubMed
description Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of Acinetobacter baumannii AB 5075 genome. Recombinant protein expressed in E. coli exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1.5–2 log colony forming units (CFU)/mL. However the protein becomes rapidly inactivated and enables the bacteria to restore the population. AcLys structure determined by X-ray crystallography reveals a predominantly α—helical fold similar to bacteriophage P22 lysozyme. The С-terminal part of AcLys polypeptide chains forms an α—helix enriched by Lys and Arg residues exposed outside of the protein globule. Presumably this type of structure of the C-terminal α—helix has evolved evolutionally enabling the endolysin to pass the inner membrane during the host lysis or, potentially, to penetrate the outer membrane of the Gram-negative bacteria.
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spelling pubmed-60248482018-07-16 Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells Sykilinda, Nina N. Nikolaeva, Alena Y. Shneider, Mikhail M. Mishkin, Dmitry V. Patutin, Artem A. Popov, Vladimir O. Boyko, Konstantin M. Klyachko, Natalia L. Miroshnikov, Konstantin A. Viruses Article Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of Acinetobacter baumannii AB 5075 genome. Recombinant protein expressed in E. coli exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1.5–2 log colony forming units (CFU)/mL. However the protein becomes rapidly inactivated and enables the bacteria to restore the population. AcLys structure determined by X-ray crystallography reveals a predominantly α—helical fold similar to bacteriophage P22 lysozyme. The С-terminal part of AcLys polypeptide chains forms an α—helix enriched by Lys and Arg residues exposed outside of the protein globule. Presumably this type of structure of the C-terminal α—helix has evolved evolutionally enabling the endolysin to pass the inner membrane during the host lysis or, potentially, to penetrate the outer membrane of the Gram-negative bacteria. MDPI 2018-06-06 /pmc/articles/PMC6024848/ /pubmed/29882827 http://dx.doi.org/10.3390/v10060309 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sykilinda, Nina N.
Nikolaeva, Alena Y.
Shneider, Mikhail M.
Mishkin, Dmitry V.
Patutin, Artem A.
Popov, Vladimir O.
Boyko, Konstantin M.
Klyachko, Natalia L.
Miroshnikov, Konstantin A.
Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title_full Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title_fullStr Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title_full_unstemmed Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title_short Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal α-Helix with the Proposed Role in Activity against Live Bacterial Cells
title_sort structure of an acinetobacter broad-range prophage endolysin reveals a c-terminal α-helix with the proposed role in activity against live bacterial cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6024848/
https://www.ncbi.nlm.nih.gov/pubmed/29882827
http://dx.doi.org/10.3390/v10060309
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