Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study
ABSTRACTResistance to β-lactams is one of the most serious problems associated with Gram-negative infections. β-Lactamases are able to hydrolyze β-lactams such as cephalosporins and/or carbapenems. Evolutionary origin of metallo-β-lactamases (MBLs), conferring critical antibiotic resistance threats,...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2019-01-01
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| Series: | Emerging Microbes and Infections |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/22221751.2019.1692638 |
| _version_ | 1797385787507998720 |
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| author | Jung Hun Lee Masayuki Takahashi Jeong Ho Jeon Lin-Woo Kang Mineaki Seki Kwang Seung Park Myoung-Ki Hong Yoon Sik Park Tae Yeong Kim Asad Mustafa Karim Jung-Hyun Lee Masayuki Nashimoto Sang Hee Lee |
| author_facet | Jung Hun Lee Masayuki Takahashi Jeong Ho Jeon Lin-Woo Kang Mineaki Seki Kwang Seung Park Myoung-Ki Hong Yoon Sik Park Tae Yeong Kim Asad Mustafa Karim Jung-Hyun Lee Masayuki Nashimoto Sang Hee Lee |
| author_sort | Jung Hun Lee |
| collection | DOAJ |
| description | ABSTRACTResistance to β-lactams is one of the most serious problems associated with Gram-negative infections. β-Lactamases are able to hydrolyze β-lactams such as cephalosporins and/or carbapenems. Evolutionary origin of metallo-β-lactamases (MBLs), conferring critical antibiotic resistance threats, remains unknown. We discovered PNGM-1, the novel subclass B3 MBL, in deep-sea sediments that predate the antibiotic era. Here, our phylogenetic analysis suggests that PNGM-1 yields insights into the evolutionary origin of subclass B3 MBLs. We reveal the structural similarities between tRNase Zs and PNGM-1, and demonstrate that PNGM-1 has both MBL and tRNase Z activities, suggesting that PNGM-1 is thought to have evolved from a tRNase Z. We also show kinetic and structural comparisons between PNGM-1 and other proteins including subclass B3 MBLs and tRNase Zs. These comparisons revealed that the B3 MBL activity of PNGM-1 is a promiscuous activity and subclass B3 MBLs are thought to have evolved through PNGM-1 activity. |
| first_indexed | 2024-03-08T21:59:18Z |
| format | Article |
| id | doaj.art-b66c33fe431a4d90b977a4e418c63d60 |
| institution | Directory Open Access Journal |
| issn | 2222-1751 |
| language | English |
| last_indexed | 2024-03-08T21:59:18Z |
| publishDate | 2019-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Emerging Microbes and Infections |
| spelling | doaj.art-b66c33fe431a4d90b977a4e418c63d602023-12-19T16:09:57ZengTaylor & Francis GroupEmerging Microbes and Infections2222-17512019-01-01811688170010.1080/22221751.2019.1692638Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary studyJung Hun Lee0Masayuki Takahashi1Jeong Ho Jeon2Lin-Woo Kang3Mineaki Seki4Kwang Seung Park5Myoung-Ki Hong6Yoon Sik Park7Tae Yeong Kim8Asad Mustafa Karim9Jung-Hyun Lee10Masayuki Nashimoto11Sang Hee Lee12National Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaResearch Institute for Healthy Living, Niigata University of Pharmacy and Applied Life Sciences, Niigata, JapanNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaDepartment of Biological Sciences, Konkuk University, Seoul, Republic of KoreaResearch Institute for Healthy Living, Niigata University of Pharmacy and Applied Life Sciences, Niigata, JapanNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaDepartment of Biological Sciences, Konkuk University, Seoul, Republic of KoreaDepartment of Biological Sciences, Konkuk University, Seoul, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaMarine Biotechnology Research Center, Korea Institute of Ocean Science & Technology, Busan, Republic of KoreaResearch Institute for Healthy Living, Niigata University of Pharmacy and Applied Life Sciences, Niigata, JapanNational Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, Yongin, Republic of KoreaABSTRACTResistance to β-lactams is one of the most serious problems associated with Gram-negative infections. β-Lactamases are able to hydrolyze β-lactams such as cephalosporins and/or carbapenems. Evolutionary origin of metallo-β-lactamases (MBLs), conferring critical antibiotic resistance threats, remains unknown. We discovered PNGM-1, the novel subclass B3 MBL, in deep-sea sediments that predate the antibiotic era. Here, our phylogenetic analysis suggests that PNGM-1 yields insights into the evolutionary origin of subclass B3 MBLs. We reveal the structural similarities between tRNase Zs and PNGM-1, and demonstrate that PNGM-1 has both MBL and tRNase Z activities, suggesting that PNGM-1 is thought to have evolved from a tRNase Z. We also show kinetic and structural comparisons between PNGM-1 and other proteins including subclass B3 MBLs and tRNase Zs. These comparisons revealed that the B3 MBL activity of PNGM-1 is a promiscuous activity and subclass B3 MBLs are thought to have evolved through PNGM-1 activity.https://www.tandfonline.com/doi/10.1080/22221751.2019.1692638Antimicrobial resistancesubclass B3 metallo-β-lactamasetRNase Zdual activitystructure and evolutionary origin |
| spellingShingle | Jung Hun Lee Masayuki Takahashi Jeong Ho Jeon Lin-Woo Kang Mineaki Seki Kwang Seung Park Myoung-Ki Hong Yoon Sik Park Tae Yeong Kim Asad Mustafa Karim Jung-Hyun Lee Masayuki Nashimoto Sang Hee Lee Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study Emerging Microbes and Infections Antimicrobial resistance subclass B3 metallo-β-lactamase tRNase Z dual activity structure and evolutionary origin |
| title | Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study |
| title_full | Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study |
| title_fullStr | Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study |
| title_full_unstemmed | Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study |
| title_short | Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-β-lactamases: a molecular and evolutionary study |
| title_sort | dual activity of pngm 1 pinpoints the evolutionary origin of subclass b3 metallo β lactamases a molecular and evolutionary study |
| topic | Antimicrobial resistance subclass B3 metallo-β-lactamase tRNase Z dual activity structure and evolutionary origin |
| url | https://www.tandfonline.com/doi/10.1080/22221751.2019.1692638 |
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