Identification of a phage-derived depolymerase specific for KL64 capsule of Klebsiella pneumoniae and its anti-biofilm effect
The increasing prevalence of Carbapenem-resistant Klebsiella pneumoniae (CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type K. pneumoniae was isolated and ch...
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| Published in: | Virus genes Vol. 57; no. 5; pp. 434 - 442 |
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| Main Authors: | , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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01.10.2021
Springer Nature B.V |
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| ISSN: | 0920-8569, 1572-994X, 1572-994X |
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| Abstract | The increasing prevalence of Carbapenem-resistant
Klebsiella pneumoniae
(CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type
K. pneumoniae
was isolated and characterized. Whole genome analysis and electron microscopy analysis showed that phage P510 belonged to genus
Przondovirus
, family
Autographiviridae
, the order
Caudovirales
. The tail fiber protein of the phage was predicted to encode capsule depolymerase. Further analysis demonstrated that recombinant depolymerase P510dep had polysaccharide-degrading activity against KL64-types capsule of
K. pneumoniae
, and its lysis spectrum matched to host range of phage P510. We also demonstrated that the recombinant depolymerase was able to significantly inhibit biofilm formation. The discovery of the phage-derived depolymerase lays the foundation for controlling the spread of CRKPs. |
|---|---|
| AbstractList | The increasing prevalence of Carbapenem-resistant
Klebsiella pneumoniae
(CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type
K. pneumoniae
was isolated and characterized. Whole genome analysis and electron microscopy analysis showed that phage P510 belonged to genus
Przondovirus
, family
Autographiviridae
, the order
Caudovirales
. The tail fiber protein of the phage was predicted to encode capsule depolymerase. Further analysis demonstrated that recombinant depolymerase P510dep had polysaccharide-degrading activity against KL64-types capsule of
K. pneumoniae
, and its lysis spectrum matched to host range of phage P510. We also demonstrated that the recombinant depolymerase was able to significantly inhibit biofilm formation. The discovery of the phage-derived depolymerase lays the foundation for controlling the spread of CRKPs. The increasing prevalence of Carbapenem-resistant Klebsiella pneumoniae (CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type K. pneumoniae was isolated and characterized. Whole genome analysis and electron microscopy analysis showed that phage P510 belonged to genus Przondovirus, family Autographiviridae, the order Caudovirales. The tail fiber protein of the phage was predicted to encode capsule depolymerase. Further analysis demonstrated that recombinant depolymerase P510dep had polysaccharide-degrading activity against KL64-types capsule of K. pneumoniae, and its lysis spectrum matched to host range of phage P510. We also demonstrated that the recombinant depolymerase was able to significantly inhibit biofilm formation. The discovery of the phage-derived depolymerase lays the foundation for controlling the spread of CRKPs. The increasing prevalence of Carbapenem-resistant Klebsiella pneumoniae (CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type K. pneumoniae was isolated and characterized. Whole genome analysis and electron microscopy analysis showed that phage P510 belonged to genus Przondovirus, family Autographiviridae, the order Caudovirales. The tail fiber protein of the phage was predicted to encode capsule depolymerase. Further analysis demonstrated that recombinant depolymerase P510dep had polysaccharide-degrading activity against KL64-types capsule of K. pneumoniae, and its lysis spectrum matched to host range of phage P510. We also demonstrated that the recombinant depolymerase was able to significantly inhibit biofilm formation. The discovery of the phage-derived depolymerase lays the foundation for controlling the spread of CRKPs.The increasing prevalence of Carbapenem-resistant Klebsiella pneumoniae (CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained increasing attention for controling CRKP infections. In this study, a lytic phage P510 infecting KL64 type K. pneumoniae was isolated and characterized. Whole genome analysis and electron microscopy analysis showed that phage P510 belonged to genus Przondovirus, family Autographiviridae, the order Caudovirales. The tail fiber protein of the phage was predicted to encode capsule depolymerase. Further analysis demonstrated that recombinant depolymerase P510dep had polysaccharide-degrading activity against KL64-types capsule of K. pneumoniae, and its lysis spectrum matched to host range of phage P510. We also demonstrated that the recombinant depolymerase was able to significantly inhibit biofilm formation. The discovery of the phage-derived depolymerase lays the foundation for controlling the spread of CRKPs. |
| Author | Li, Pei Li, Min Chen, Liang Du, Hong Zhang, Wei Xiao, Yuyi Chen, Long Guo, Genglin |
| Author_xml | – sequence: 1 givenname: Min surname: Li fullname: Li, Min organization: College of Veterinary Medicine, Nanjing Agricultural University, Key Lab of Animal Bacteriology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University – sequence: 2 givenname: Pei surname: Li fullname: Li, Pei organization: College of Veterinary Medicine, Nanjing Agricultural University, Key Lab of Animal Bacteriology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University – sequence: 3 givenname: Long surname: Chen fullname: Chen, Long organization: Department of Clinical Laboratory, Zhangjiagang Hospital Affiliated To Soochow University – sequence: 4 givenname: Genglin surname: Guo fullname: Guo, Genglin organization: College of Veterinary Medicine, Nanjing Agricultural University, Key Lab of Animal Bacteriology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University – sequence: 5 givenname: Yuyi surname: Xiao fullname: Xiao, Yuyi organization: College of Veterinary Medicine, Nanjing Agricultural University, Key Lab of Animal Bacteriology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University – sequence: 6 givenname: Liang surname: Chen fullname: Chen, Liang organization: Center for Discovery and Innovation, Hackensack-Meridian Health, Hackensack Meridian School of Medicine at Seton Hall University – sequence: 7 givenname: Hong surname: Du fullname: Du, Hong organization: Department of Clinical Laboratory, The Second Affiliated Hospital of Soochow University – sequence: 8 givenname: Wei orcidid: 0000-0002-3575-6225 surname: Zhang fullname: Zhang, Wei email: vszw@njau.edu.cn organization: College of Veterinary Medicine, Nanjing Agricultural University, Key Lab of Animal Bacteriology, Ministry of Agriculture, MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University |
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| ContentType | Journal Article |
| Copyright | The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021 The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021. 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature. |
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| Keywords | Bacteriophages Biofilm Carbapenem-resistant Depolymerase Capsular type |
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| Snippet | The increasing prevalence of Carbapenem-resistant
Klebsiella pneumoniae
(CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained... The increasing prevalence of Carbapenem-resistant Klebsiella pneumoniae (CRKP) poses a serious threat to global health. Phages and phage-derived enzymes gained... |
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| StartPage | 434 |
| SubjectTerms | Antibiotics Autographiviridae bacteriophages biofilm Biofilms Biomedical and Life Sciences Biomedicine Electron microscopy Genomes Host range Klebsiella pneumoniae Lysis Medical Microbiology Original Paper Phages Plant Sciences Polysaccharides Public health sequence analysis tail Tail fiber protein Virology |
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| Title | Identification of a phage-derived depolymerase specific for KL64 capsule of Klebsiella pneumoniae and its anti-biofilm effect |
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| Volume | 57 |
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