Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions
In this study, several different depolymerases encoded in the prophage regions of <i>Acinetobacter baumannii</i> genomes have been bioinformatically predicted and recombinantly produced. The identified depolymerases possessed multi-domain structures and were identical or closely homologo...
| Main Authors: | , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-04-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/23/9/4971 |
| _version_ | 1797504493370212352 |
|---|---|
| author | Alena Y. Drobiazko Anastasia A. Kasimova Peter V. Evseev Mikhail M. Shneider Evgeniy I. Klimuk Alexander S. Shashkov Andrei S. Dmitrenok Alexander O. Chizhov Pavel V. Slukin Yuriy P. Skryabin Nikolay V. Volozhantsev Konstantin A. Miroshnikov Yuriy A. Knirel Anastasia V. Popova |
| author_facet | Alena Y. Drobiazko Anastasia A. Kasimova Peter V. Evseev Mikhail M. Shneider Evgeniy I. Klimuk Alexander S. Shashkov Andrei S. Dmitrenok Alexander O. Chizhov Pavel V. Slukin Yuriy P. Skryabin Nikolay V. Volozhantsev Konstantin A. Miroshnikov Yuriy A. Knirel Anastasia V. Popova |
| author_sort | Alena Y. Drobiazko |
| collection | DOAJ |
| description | In this study, several different depolymerases encoded in the prophage regions of <i>Acinetobacter baumannii</i> genomes have been bioinformatically predicted and recombinantly produced. The identified depolymerases possessed multi-domain structures and were identical or closely homologous to various proteins encoded in other <i>A. baumannii</i> genomes. This means that prophage-derived depolymerases are widespread, and different bacterial genomes can be the source of proteins with polysaccharide-degrading activities. For two depolymerases, the specificity to capsular polysaccharides (CPSs) of <i>A. baumannii</i> belonging to K1 and K92 capsular types (K types) was determined. The data obtained showed that the prophage-derived depolymerases were glycosidases that cleaved the <i>A. baumannii</i> CPSs by the hydrolytic mechanism to yield monomers and oligomers of the K units. The recombinant proteins with established enzymatic activity significantly reduced the mortality of <i>Galleria mellonella</i> larvae infected with <i>A. baumannii</i> of K1 and K92 capsular types. Therefore, these enzymes can be considered as suitable candidates for the development of new antibacterials against corresponding <i>A. baumannii</i> K types. |
| first_indexed | 2024-03-10T04:05:22Z |
| format | Article |
| id | doaj.art-661b0b27a3884f518e63568fd3e2fd07 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T04:05:22Z |
| publishDate | 2022-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-661b0b27a3884f518e63568fd3e2fd072023-11-23T08:24:59ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-04-01239497110.3390/ijms23094971Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage RegionsAlena Y. Drobiazko0Anastasia A. Kasimova1Peter V. Evseev2Mikhail M. Shneider3Evgeniy I. Klimuk4Alexander S. Shashkov5Andrei S. Dmitrenok6Alexander O. Chizhov7Pavel V. Slukin8Yuriy P. Skryabin9Nikolay V. Volozhantsev10Konstantin A. Miroshnikov11Yuriy A. Knirel12Anastasia V. Popova13Moscow Institute of Physics and Technology (National Research University), 141700 Dolgoprudny, RussiaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaInstitute of Molecular Genetics of National Research Centre «Kurchatov Institute», 123182 Moscow, RussiaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, RussiaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, RussiaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, RussiaState Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, RussiaState Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, RussiaState Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, RussiaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, RussiaState Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, RussiaIn this study, several different depolymerases encoded in the prophage regions of <i>Acinetobacter baumannii</i> genomes have been bioinformatically predicted and recombinantly produced. The identified depolymerases possessed multi-domain structures and were identical or closely homologous to various proteins encoded in other <i>A. baumannii</i> genomes. This means that prophage-derived depolymerases are widespread, and different bacterial genomes can be the source of proteins with polysaccharide-degrading activities. For two depolymerases, the specificity to capsular polysaccharides (CPSs) of <i>A. baumannii</i> belonging to K1 and K92 capsular types (K types) was determined. The data obtained showed that the prophage-derived depolymerases were glycosidases that cleaved the <i>A. baumannii</i> CPSs by the hydrolytic mechanism to yield monomers and oligomers of the K units. The recombinant proteins with established enzymatic activity significantly reduced the mortality of <i>Galleria mellonella</i> larvae infected with <i>A. baumannii</i> of K1 and K92 capsular types. Therefore, these enzymes can be considered as suitable candidates for the development of new antibacterials against corresponding <i>A. baumannii</i> K types.https://www.mdpi.com/1422-0067/23/9/4971<i>Acinetobacter baumannii</i>prophagesphage receptor-binding proteinsstructural depolymeraseglycosidasecapsular polysaccharide |
| spellingShingle | Alena Y. Drobiazko Anastasia A. Kasimova Peter V. Evseev Mikhail M. Shneider Evgeniy I. Klimuk Alexander S. Shashkov Andrei S. Dmitrenok Alexander O. Chizhov Pavel V. Slukin Yuriy P. Skryabin Nikolay V. Volozhantsev Konstantin A. Miroshnikov Yuriy A. Knirel Anastasia V. Popova Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions International Journal of Molecular Sciences <i>Acinetobacter baumannii</i> prophages phage receptor-binding proteins structural depolymerase glycosidase capsular polysaccharide |
| title | Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions |
| title_full | Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions |
| title_fullStr | Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions |
| title_full_unstemmed | Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions |
| title_short | Capsule-Targeting Depolymerases Derived from <i>Acinetobacter baumannii</i> Prophage Regions |
| title_sort | capsule targeting depolymerases derived from i acinetobacter baumannii i prophage regions |
| topic | <i>Acinetobacter baumannii</i> prophages phage receptor-binding proteins structural depolymerase glycosidase capsular polysaccharide |
| url | https://www.mdpi.com/1422-0067/23/9/4971 |
| work_keys_str_mv | AT alenaydrobiazko capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT anastasiaakasimova capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT petervevseev capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT mikhailmshneider capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT evgeniyiklimuk capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT alexandersshashkov capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT andreisdmitrenok capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT alexanderochizhov capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT pavelvslukin capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT yuriypskryabin capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT nikolayvvolozhantsev capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT konstantinamiroshnikov capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT yuriyaknirel capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions AT anastasiavpopova capsuletargetingdepolymerasesderivedfromiacinetobacterbaumanniiiprophageregions |