Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins
ABSTRACT In this study, we present the discovery and characterization of a highly thermostable endolysin from bacteriophage Ph2119 infecting Thermus strain MAT2119 isolated from geothermal areas in Iceland. Nucleotide sequence analysis of the 16S rRNA gene affiliated the strain with the species Ther...
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American Society for Microbiology
2014
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Online Access: | http://dx.doi.org/10.1128/aem.03074-13 https://journals.asm.org/doi/pdf/10.1128/AEM.03074-13 |
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crasmicro:10.1128/aem.03074-13 2024-10-13T14:08:30+00:00 Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins Plotka, Magdalena Kaczorowska, Anna-Karina Stefanska, Aleksandra Morzywolek, Agnieszka Fridjonsson, Olafur H. Dunin-Horkawicz, Stanislaw Kozlowski, Lukasz Hreggvidsson, Gudmundur O. Kristjansson, Jakob K. Dabrowski, Slawomir Bujnicki, Janusz M. Kaczorowski, Tadeusz 2014 http://dx.doi.org/10.1128/aem.03074-13 https://journals.asm.org/doi/pdf/10.1128/AEM.03074-13 en eng American Society for Microbiology https://journals.asm.org/non-commercial-tdm-license Applied and Environmental Microbiology volume 80, issue 3, page 886-895 ISSN 0099-2240 1098-5336 journal-article 2014 crasmicro https://doi.org/10.1128/aem.03074-13 2024-09-23T04:07:27Z ABSTRACT In this study, we present the discovery and characterization of a highly thermostable endolysin from bacteriophage Ph2119 infecting Thermus strain MAT2119 isolated from geothermal areas in Iceland. Nucleotide sequence analysis of the 16S rRNA gene affiliated the strain with the species Thermus scotoductus . Bioinformatics analysis has allowed identification in the genome of phage 2119 of an open reading frame (468 bp in length) coding for a 155-amino-acid basic protein with an M r of 17,555. Ph2119 endolysin does not resemble any known thermophilic phage lytic enzymes. Instead, it has conserved amino acid residues (His 30 , Tyr 58 , His 132 , and Cys 140 ) that form a Zn 2+ binding site characteristic of T3 and T7 lysozymes, as well as eukaryotic peptidoglycan recognition proteins, which directly bind to, but also may destroy, bacterial peptidoglycan. The purified enzyme shows high lytic activity toward thermophiles, i.e., T. scotoductus (100%), Thermus thermophilus (100%), and Thermus flavus (99%), and also, to a lesser extent, toward mesophilic Gram-negative bacteria, i.e., Escherichia coli (34%), Serratia marcescens (28%), Pseudomonas fluorescens (13%), and Salmonella enterica serovar Panama (10%). The enzyme has shown no activity against a number of Gram-positive bacteria analyzed, with the exception of Deinococcus radiodurans (25%) and Bacillus cereus (15%). Ph2119 endolysin was found to be highly thermostable: it retains approximately 87% of its lytic activity after 6 h of incubation at 95°C. The optimum temperature range for the enzyme activity is 50°C to 78°C. The enzyme exhibits lytic activity in the pH range of 6 to 10 (maximum at pH 7.5 to 8.0) and is also active in the presence of up to 500 mM NaCl. Article in Journal/Newspaper Iceland ASM Journals (American Society for Microbiology) Applied and Environmental Microbiology 80 3 886 895 |
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ASM Journals (American Society for Microbiology) |
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English |
description |
ABSTRACT In this study, we present the discovery and characterization of a highly thermostable endolysin from bacteriophage Ph2119 infecting Thermus strain MAT2119 isolated from geothermal areas in Iceland. Nucleotide sequence analysis of the 16S rRNA gene affiliated the strain with the species Thermus scotoductus . Bioinformatics analysis has allowed identification in the genome of phage 2119 of an open reading frame (468 bp in length) coding for a 155-amino-acid basic protein with an M r of 17,555. Ph2119 endolysin does not resemble any known thermophilic phage lytic enzymes. Instead, it has conserved amino acid residues (His 30 , Tyr 58 , His 132 , and Cys 140 ) that form a Zn 2+ binding site characteristic of T3 and T7 lysozymes, as well as eukaryotic peptidoglycan recognition proteins, which directly bind to, but also may destroy, bacterial peptidoglycan. The purified enzyme shows high lytic activity toward thermophiles, i.e., T. scotoductus (100%), Thermus thermophilus (100%), and Thermus flavus (99%), and also, to a lesser extent, toward mesophilic Gram-negative bacteria, i.e., Escherichia coli (34%), Serratia marcescens (28%), Pseudomonas fluorescens (13%), and Salmonella enterica serovar Panama (10%). The enzyme has shown no activity against a number of Gram-positive bacteria analyzed, with the exception of Deinococcus radiodurans (25%) and Bacillus cereus (15%). Ph2119 endolysin was found to be highly thermostable: it retains approximately 87% of its lytic activity after 6 h of incubation at 95°C. The optimum temperature range for the enzyme activity is 50°C to 78°C. The enzyme exhibits lytic activity in the pH range of 6 to 10 (maximum at pH 7.5 to 8.0) and is also active in the presence of up to 500 mM NaCl. |
format |
Article in Journal/Newspaper |
author |
Plotka, Magdalena Kaczorowska, Anna-Karina Stefanska, Aleksandra Morzywolek, Agnieszka Fridjonsson, Olafur H. Dunin-Horkawicz, Stanislaw Kozlowski, Lukasz Hreggvidsson, Gudmundur O. Kristjansson, Jakob K. Dabrowski, Slawomir Bujnicki, Janusz M. Kaczorowski, Tadeusz |
spellingShingle |
Plotka, Magdalena Kaczorowska, Anna-Karina Stefanska, Aleksandra Morzywolek, Agnieszka Fridjonsson, Olafur H. Dunin-Horkawicz, Stanislaw Kozlowski, Lukasz Hreggvidsson, Gudmundur O. Kristjansson, Jakob K. Dabrowski, Slawomir Bujnicki, Janusz M. Kaczorowski, Tadeusz Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
author_facet |
Plotka, Magdalena Kaczorowska, Anna-Karina Stefanska, Aleksandra Morzywolek, Agnieszka Fridjonsson, Olafur H. Dunin-Horkawicz, Stanislaw Kozlowski, Lukasz Hreggvidsson, Gudmundur O. Kristjansson, Jakob K. Dabrowski, Slawomir Bujnicki, Janusz M. Kaczorowski, Tadeusz |
author_sort |
Plotka, Magdalena |
title |
Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
title_short |
Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
title_full |
Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
title_fullStr |
Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
title_full_unstemmed |
Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins |
title_sort |
novel highly thermostable endolysin from thermus scotoductus mat2119 bacteriophage ph2119 with amino acid sequence similarity to eukaryotic peptidoglycan recognition proteins |
publisher |
American Society for Microbiology |
publishDate |
2014 |
url |
http://dx.doi.org/10.1128/aem.03074-13 https://journals.asm.org/doi/pdf/10.1128/AEM.03074-13 |
genre |
Iceland |
genre_facet |
Iceland |
op_source |
Applied and Environmental Microbiology volume 80, issue 3, page 886-895 ISSN 0099-2240 1098-5336 |
op_rights |
https://journals.asm.org/non-commercial-tdm-license |
op_doi |
https://doi.org/10.1128/aem.03074-13 |
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Applied and Environmental Microbiology |
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80 |
container_issue |
3 |
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886 |
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895 |
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1812815183212445696 |