Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses
- Autores
- Alsenani, Tahani A.; Rodríguez, María Margarita; Ghiglione, Barbara; Taracila, Magdalena A.; Mojica, Maria F.; Rojas, Laura J.; Hujer, Andrea M.; Gutkind, Gabriel Osvaldo; Bethel, Christopher R.; Rather, Philip N.; Introvigne, Maria Luisa; Prati, Fabio; Caselli, Emilia; Power, Pablo; van den Akker, Focco; Bonomo, Robert A.
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Design of novel β-lactamase inhibitors (BLIs) is one of the currently accepted strategies to combat the threat of cephalosporin and carbapenem resistance in Gram-negative bacteria. Boronic acid transition state inhibitors (BATSIs) are competitive, reversible BLIs that offer promise as novel therapeutic agents. In this study, the activities of two α-amido-β-triazolylethaneboronic acid transition state inhibitors (S02030 and MB_076) targeting representative KPC (KPC-2) and CTX-M (CTX-M-96, a CTX-M-15-type extended-spectrum β-lactamase [ESBL]) β-lactamases were evaluated. The 50% inhibitory concentrations (IC50s) for both inhibitors were measured in the nanomolar range (2 to 135 nM). For S02030, the k2/K for CTX-M-96 (24,000 M21 s21) was twice the reported value for KPC-2 (12,000 M21 s21); for MB_076, the k2/K values ranged from 1,200 M21 s21 (KPC-2) to 3,900 M21 s21 (CTX-M-96). Crystal structures of KPC-2 with MB_076 (1.38-Å resolution) and S02030 and the in silico models of CTX-M-96 with these two BATSIs show that interaction in the CTX-M-96–S02030 and CTX-M-96–MB_076 complexes were overall equivalent to that observed for the crystallographic structure of KPC-2–S02030 and KPC-2–MB_076. The tetrahedral interaction surrounding the boron atom from S02030 and MB_076 creates a favorable hydrogen bonding network with S70, S130, N132, N170, and S237. However, the changes from W105 in KPC-2 to Y105 in CTX-M-96 and the missing residue R220 in CTX-M-96 alter the arrangement of the inhibitors in the active site of CTX-M-96, partially explaining the difference in kinetic parameters. The novel BATSI scaffolds studied here advance our understanding of structure-activity relationships (SARs) and illustrate the importance of new approaches to β-lactamase inhibitor design.
Fil: Alsenani, Tahani A.. Case Western Reserve University School of Medicine; Estados Unidos
Fil: Rodríguez, María Margarita. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
Fil: Ghiglione, Barbara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina
Fil: Taracila, Magdalena A.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos
Fil: Mojica, Maria F.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos
Fil: Rojas, Laura J.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos. Case Western Reserve University School of Medicine; Estados Unidos
Fil: Hujer, Andrea M.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos
Fil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina
Fil: Bethel, Christopher R.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos
Fil: Rather, Philip N.. University of Emory; Estados Unidos. Atlanta VA Medical Center; Estados Unidos
Fil: Introvigne, Maria Luisa. Università di Modena e Reggio Emilia; Italia
Fil: Prati, Fabio. Università di Modena e Reggio Emilia; Italia
Fil: Caselli, Emilia. Università di Modena e Reggio Emilia; Italia
Fil: Power, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina
Fil: van den Akker, Focco. Case Western Reserve University School of Medicine; Estados Unidos
Fil: Bonomo, Robert A.. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos - Materia
-
BORONATE
CARBAPENEMASE
CTX-M
CTX-M-96
ESBL
KPC
KPC-2
MB_076
S02030
Β-LACTAMASES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/225318
Ver los metadatos del registro completo
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Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural AnalysesAlsenani, Tahani A.Rodríguez, María MargaritaGhiglione, BarbaraTaracila, Magdalena A.Mojica, Maria F.Rojas, Laura J.Hujer, Andrea M.Gutkind, Gabriel OsvaldoBethel, Christopher R.Rather, Philip N.Introvigne, Maria LuisaPrati, FabioCaselli, EmiliaPower, Pablovan den Akker, FoccoBonomo, Robert A.BORONATECARBAPENEMASECTX-MCTX-M-96ESBLKPCKPC-2MB_076S02030Β-LACTAMASEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Design of novel β-lactamase inhibitors (BLIs) is one of the currently accepted strategies to combat the threat of cephalosporin and carbapenem resistance in Gram-negative bacteria. Boronic acid transition state inhibitors (BATSIs) are competitive, reversible BLIs that offer promise as novel therapeutic agents. In this study, the activities of two α-amido-β-triazolylethaneboronic acid transition state inhibitors (S02030 and MB_076) targeting representative KPC (KPC-2) and CTX-M (CTX-M-96, a CTX-M-15-type extended-spectrum β-lactamase [ESBL]) β-lactamases were evaluated. The 50% inhibitory concentrations (IC50s) for both inhibitors were measured in the nanomolar range (2 to 135 nM). For S02030, the k2/K for CTX-M-96 (24,000 M21 s21) was twice the reported value for KPC-2 (12,000 M21 s21); for MB_076, the k2/K values ranged from 1,200 M21 s21 (KPC-2) to 3,900 M21 s21 (CTX-M-96). Crystal structures of KPC-2 with MB_076 (1.38-Å resolution) and S02030 and the in silico models of CTX-M-96 with these two BATSIs show that interaction in the CTX-M-96–S02030 and CTX-M-96–MB_076 complexes were overall equivalent to that observed for the crystallographic structure of KPC-2–S02030 and KPC-2–MB_076. The tetrahedral interaction surrounding the boron atom from S02030 and MB_076 creates a favorable hydrogen bonding network with S70, S130, N132, N170, and S237. However, the changes from W105 in KPC-2 to Y105 in CTX-M-96 and the missing residue R220 in CTX-M-96 alter the arrangement of the inhibitors in the active site of CTX-M-96, partially explaining the difference in kinetic parameters. The novel BATSI scaffolds studied here advance our understanding of structure-activity relationships (SARs) and illustrate the importance of new approaches to β-lactamase inhibitor design.Fil: Alsenani, Tahani A.. Case Western Reserve University School of Medicine; Estados UnidosFil: Rodríguez, María Margarita. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; ArgentinaFil: Ghiglione, Barbara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; ArgentinaFil: Taracila, Magdalena A.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados UnidosFil: Mojica, Maria F.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados UnidosFil: Rojas, Laura J.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos. Case Western Reserve University School of Medicine; Estados UnidosFil: Hujer, Andrea M.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados UnidosFil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; ArgentinaFil: Bethel, Christopher R.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados UnidosFil: Rather, Philip N.. University of Emory; Estados Unidos. Atlanta VA Medical Center; Estados UnidosFil: Introvigne, Maria Luisa. Università di Modena e Reggio Emilia; ItaliaFil: Prati, Fabio. Università di Modena e Reggio Emilia; ItaliaFil: Caselli, Emilia. Università di Modena e Reggio Emilia; ItaliaFil: Power, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; ArgentinaFil: van den Akker, Focco. Case Western Reserve University School of Medicine; Estados UnidosFil: Bonomo, Robert A.. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados UnidosAmerican Society for Microbiology2023-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/225318Alsenani, Tahani A.; Rodríguez, María Margarita; Ghiglione, Barbara; Taracila, Magdalena A.; Mojica, Maria F.; et al.; Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 67; 1; 1-2023; 1-100066-4804CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.asm.org/doi/10.1128/aac.00930-22info:eu-repo/semantics/altIdentifier/doi/10.1128/aac.00930-22info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:30Zoai:ri.conicet.gov.ar:11336/225318instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:45:31.091CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| title |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| spellingShingle |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses Alsenani, Tahani A. BORONATE CARBAPENEMASE CTX-M CTX-M-96 ESBL KPC KPC-2 MB_076 S02030 Β-LACTAMASES |
| title_short |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| title_full |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| title_fullStr |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| title_full_unstemmed |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| title_sort |
Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses |
| dc.creator.none.fl_str_mv |
Alsenani, Tahani A. Rodríguez, María Margarita Ghiglione, Barbara Taracila, Magdalena A. Mojica, Maria F. Rojas, Laura J. Hujer, Andrea M. Gutkind, Gabriel Osvaldo Bethel, Christopher R. Rather, Philip N. Introvigne, Maria Luisa Prati, Fabio Caselli, Emilia Power, Pablo van den Akker, Focco Bonomo, Robert A. |
| author |
Alsenani, Tahani A. |
| author_facet |
Alsenani, Tahani A. Rodríguez, María Margarita Ghiglione, Barbara Taracila, Magdalena A. Mojica, Maria F. Rojas, Laura J. Hujer, Andrea M. Gutkind, Gabriel Osvaldo Bethel, Christopher R. Rather, Philip N. Introvigne, Maria Luisa Prati, Fabio Caselli, Emilia Power, Pablo van den Akker, Focco Bonomo, Robert A. |
| author_role |
author |
| author2 |
Rodríguez, María Margarita Ghiglione, Barbara Taracila, Magdalena A. Mojica, Maria F. Rojas, Laura J. Hujer, Andrea M. Gutkind, Gabriel Osvaldo Bethel, Christopher R. Rather, Philip N. Introvigne, Maria Luisa Prati, Fabio Caselli, Emilia Power, Pablo van den Akker, Focco Bonomo, Robert A. |
| author2_role |
author author author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
BORONATE CARBAPENEMASE CTX-M CTX-M-96 ESBL KPC KPC-2 MB_076 S02030 Β-LACTAMASES |
| topic |
BORONATE CARBAPENEMASE CTX-M CTX-M-96 ESBL KPC KPC-2 MB_076 S02030 Β-LACTAMASES |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Design of novel β-lactamase inhibitors (BLIs) is one of the currently accepted strategies to combat the threat of cephalosporin and carbapenem resistance in Gram-negative bacteria. Boronic acid transition state inhibitors (BATSIs) are competitive, reversible BLIs that offer promise as novel therapeutic agents. In this study, the activities of two α-amido-β-triazolylethaneboronic acid transition state inhibitors (S02030 and MB_076) targeting representative KPC (KPC-2) and CTX-M (CTX-M-96, a CTX-M-15-type extended-spectrum β-lactamase [ESBL]) β-lactamases were evaluated. The 50% inhibitory concentrations (IC50s) for both inhibitors were measured in the nanomolar range (2 to 135 nM). For S02030, the k2/K for CTX-M-96 (24,000 M21 s21) was twice the reported value for KPC-2 (12,000 M21 s21); for MB_076, the k2/K values ranged from 1,200 M21 s21 (KPC-2) to 3,900 M21 s21 (CTX-M-96). Crystal structures of KPC-2 with MB_076 (1.38-Å resolution) and S02030 and the in silico models of CTX-M-96 with these two BATSIs show that interaction in the CTX-M-96–S02030 and CTX-M-96–MB_076 complexes were overall equivalent to that observed for the crystallographic structure of KPC-2–S02030 and KPC-2–MB_076. The tetrahedral interaction surrounding the boron atom from S02030 and MB_076 creates a favorable hydrogen bonding network with S70, S130, N132, N170, and S237. However, the changes from W105 in KPC-2 to Y105 in CTX-M-96 and the missing residue R220 in CTX-M-96 alter the arrangement of the inhibitors in the active site of CTX-M-96, partially explaining the difference in kinetic parameters. The novel BATSI scaffolds studied here advance our understanding of structure-activity relationships (SARs) and illustrate the importance of new approaches to β-lactamase inhibitor design. Fil: Alsenani, Tahani A.. Case Western Reserve University School of Medicine; Estados Unidos Fil: Rodríguez, María Margarita. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina Fil: Ghiglione, Barbara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina Fil: Taracila, Magdalena A.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos Fil: Mojica, Maria F.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos Fil: Rojas, Laura J.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos. Case Western Reserve University School of Medicine; Estados Unidos Fil: Hujer, Andrea M.. Case Western Reserve University School of Medicine; Estados Unidos. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos Fil: Gutkind, Gabriel Osvaldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina Fil: Bethel, Christopher R.. Louis Stokes Cleveland Department of Veterans Affairs Medical Center; Estados Unidos Fil: Rather, Philip N.. University of Emory; Estados Unidos. Atlanta VA Medical Center; Estados Unidos Fil: Introvigne, Maria Luisa. Università di Modena e Reggio Emilia; Italia Fil: Prati, Fabio. Università di Modena e Reggio Emilia; Italia Fil: Caselli, Emilia. Università di Modena e Reggio Emilia; Italia Fil: Power, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Investigaciones en Bacteriología y Virología Molecular; Argentina Fil: van den Akker, Focco. Case Western Reserve University School of Medicine; Estados Unidos Fil: Bonomo, Robert A.. Case Western Reserve University School of Medicine; Estados Unidos. Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology; Estados Unidos |
| description |
Design of novel β-lactamase inhibitors (BLIs) is one of the currently accepted strategies to combat the threat of cephalosporin and carbapenem resistance in Gram-negative bacteria. Boronic acid transition state inhibitors (BATSIs) are competitive, reversible BLIs that offer promise as novel therapeutic agents. In this study, the activities of two α-amido-β-triazolylethaneboronic acid transition state inhibitors (S02030 and MB_076) targeting representative KPC (KPC-2) and CTX-M (CTX-M-96, a CTX-M-15-type extended-spectrum β-lactamase [ESBL]) β-lactamases were evaluated. The 50% inhibitory concentrations (IC50s) for both inhibitors were measured in the nanomolar range (2 to 135 nM). For S02030, the k2/K for CTX-M-96 (24,000 M21 s21) was twice the reported value for KPC-2 (12,000 M21 s21); for MB_076, the k2/K values ranged from 1,200 M21 s21 (KPC-2) to 3,900 M21 s21 (CTX-M-96). Crystal structures of KPC-2 with MB_076 (1.38-Å resolution) and S02030 and the in silico models of CTX-M-96 with these two BATSIs show that interaction in the CTX-M-96–S02030 and CTX-M-96–MB_076 complexes were overall equivalent to that observed for the crystallographic structure of KPC-2–S02030 and KPC-2–MB_076. The tetrahedral interaction surrounding the boron atom from S02030 and MB_076 creates a favorable hydrogen bonding network with S70, S130, N132, N170, and S237. However, the changes from W105 in KPC-2 to Y105 in CTX-M-96 and the missing residue R220 in CTX-M-96 alter the arrangement of the inhibitors in the active site of CTX-M-96, partially explaining the difference in kinetic parameters. The novel BATSI scaffolds studied here advance our understanding of structure-activity relationships (SARs) and illustrate the importance of new approaches to β-lactamase inhibitor design. |
| publishDate |
2023 |
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2023-01 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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http://hdl.handle.net/11336/225318 Alsenani, Tahani A.; Rodríguez, María Margarita; Ghiglione, Barbara; Taracila, Magdalena A.; Mojica, Maria F.; et al.; Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 67; 1; 1-2023; 1-10 0066-4804 CONICET Digital CONICET |
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http://hdl.handle.net/11336/225318 |
| identifier_str_mv |
Alsenani, Tahani A.; Rodríguez, María Margarita; Ghiglione, Barbara; Taracila, Magdalena A.; Mojica, Maria F.; et al.; Boronic Acid Transition State Inhibitors as Potent Inactivators of KPC and CTX-M β-Lactamases: Biochemical and Structural Analyses; American Society for Microbiology; Antimicrobial Agents and Chemotherapy; 67; 1; 1-2023; 1-10 0066-4804 CONICET Digital CONICET |
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eng |
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American Society for Microbiology |
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American Society for Microbiology |
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