A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile
Antibiotics of the β-lactam class inhibit bacterial cell wall synthesis by targeting penicillin-binding proteins (PBPs). Here, Sacco et al. study the four PBPs present in the pathogen C. difficile, revealing unique structural features and shedding light on the mechanisms underlying β-lactam resistan...
| Main Authors: | , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-32086-6 |
| _version_ | 1828430316797165568 |
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| author | Michael D. Sacco Shaohui Wang Swamy R. Adapa Xiujun Zhang Eric M. Lewandowski Maura V. Gongora Dimitra Keramisanou Zachary D. Atlas Julia A. Townsend Jean R. Gatdula Ryan T. Morgan Lauren R. Hammond Michael T. Marty Jun Wang Prahathees J. Eswara Ioannis Gelis Rays H. Y. Jiang Xingmin Sun Yu Chen |
| author_facet | Michael D. Sacco Shaohui Wang Swamy R. Adapa Xiujun Zhang Eric M. Lewandowski Maura V. Gongora Dimitra Keramisanou Zachary D. Atlas Julia A. Townsend Jean R. Gatdula Ryan T. Morgan Lauren R. Hammond Michael T. Marty Jun Wang Prahathees J. Eswara Ioannis Gelis Rays H. Y. Jiang Xingmin Sun Yu Chen |
| author_sort | Michael D. Sacco |
| collection | DOAJ |
| description | Antibiotics of the β-lactam class inhibit bacterial cell wall synthesis by targeting penicillin-binding proteins (PBPs). Here, Sacco et al. study the four PBPs present in the pathogen C. difficile, revealing unique structural features and shedding light on the mechanisms underlying β-lactam resistance in this organism. |
| first_indexed | 2024-12-10T17:47:01Z |
| format | Article |
| id | doaj.art-ab479e50342c4a208865cf0e9e27f5cd |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-10T17:47:01Z |
| publishDate | 2022-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-ab479e50342c4a208865cf0e9e27f5cd2022-12-22T01:39:13ZengNature PortfolioNature Communications2041-17232022-07-0113111310.1038/s41467-022-32086-6A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficileMichael D. Sacco0Shaohui Wang1Swamy R. Adapa2Xiujun Zhang3Eric M. Lewandowski4Maura V. Gongora5Dimitra Keramisanou6Zachary D. Atlas7Julia A. Townsend8Jean R. Gatdula9Ryan T. Morgan10Lauren R. Hammond11Michael T. Marty12Jun Wang13Prahathees J. Eswara14Ioannis Gelis15Rays H. Y. Jiang16Xingmin Sun17Yu Chen18Department of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Global and Planetary Health, USF Genomics Program, Global Health and Infectious Disease Center, College of Public Health, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Chemistry, University of South FloridaSchool of Geosciences, University of South FloridaDepartment of Chemistry and Biochemistry, The University of ArizonaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Cell Biology, Microbiology, and Molecular Biology, University of South FloridaDepartment of Chemistry and Biochemistry, The University of ArizonaDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, the State University of New JerseyDepartment of Cell Biology, Microbiology, and Molecular Biology, University of South FloridaDepartment of Chemistry, University of South FloridaDepartment of Global and Planetary Health, USF Genomics Program, Global Health and Infectious Disease Center, College of Public Health, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaDepartment of Molecular Medicine, Morsani College of Medicine, University of South FloridaAntibiotics of the β-lactam class inhibit bacterial cell wall synthesis by targeting penicillin-binding proteins (PBPs). Here, Sacco et al. study the four PBPs present in the pathogen C. difficile, revealing unique structural features and shedding light on the mechanisms underlying β-lactam resistance in this organism.https://doi.org/10.1038/s41467-022-32086-6 |
| spellingShingle | Michael D. Sacco Shaohui Wang Swamy R. Adapa Xiujun Zhang Eric M. Lewandowski Maura V. Gongora Dimitra Keramisanou Zachary D. Atlas Julia A. Townsend Jean R. Gatdula Ryan T. Morgan Lauren R. Hammond Michael T. Marty Jun Wang Prahathees J. Eswara Ioannis Gelis Rays H. Y. Jiang Xingmin Sun Yu Chen A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile Nature Communications |
| title | A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile |
| title_full | A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile |
| title_fullStr | A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile |
| title_full_unstemmed | A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile |
| title_short | A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile |
| title_sort | unique class of zn2 binding serine based pbps underlies cephalosporin resistance and sporogenesis in clostridioides difficile |
| url | https://doi.org/10.1038/s41467-022-32086-6 |
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