Protein determinants of dissemination and host specificity of metallo-β-lactamases

Código QR

Protein determinants of dissemination and host specificity of metallo-β-lactamases

Metallo-β-lactamases (MBLs) confer resistance to carbapenem antibiotics. Here, López et al. show that the host range of MBLs depends on the efficiency of MBL signal peptide processing and secretion into outer membrane vesicles, which affects bacterial fitness.

Guardado en:

Detalles Bibliográficos
Autores principales:	Carolina López, Juan A. Ayala, Robert A. Bonomo, Lisandro J. González, Alejandro J. Vila
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/934c5d6a060f488fa03d11300b789a9c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

Ejemplares similares

Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.
por: Lisandro J González, et al.
Publicado: (2014)

On the Offensive: the Role of Outer Membrane Vesicles in the Successful Dissemination of New Delhi Metallo-β-lactamase (NDM-1)
por: Melina M. B. Martínez, et al.
Publicado: (2021)

A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
por: María-Natalia Lisa, et al.
Publicado: (2017)

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
por: Jürgen Brem, et al.
Publicado: (2016)

Human metallo-β-lactamase enzymes degrade penicillin
por: Seydina M. Diene, et al.
Publicado: (2019)

Tigecycline activity against metallo-β-lactamase-producing bacteria
por: Simit Kumar, et al.
Publicado: (2013)

A metallo-β-lactamase enzyme for internal detoxification of the antibiotic thienamycin
por: Seydina M. Diene, et al.
Publicado: (2021)

Plasmid analysis of NDM metallo-β-lactamase-producing Enterobacterales isolated in Vietnam.
por: Aki Hirabayashi, et al.
Publicado: (2021)

Bismuth antimicrobial drugs serve as broad-spectrum metallo-β-lactamase inhibitors
por: Runming Wang, et al.
Publicado: (2018)

ENTEROBACTERIACAE, PRODUCING ESBLS AND METALLO-β-LACTAMASE NDM-1, ISOLATED IN HOSPITALS OF BALTIC REGION COUNTRIES
por: S. A. Egorova, et al.
Publicado: (2014)

A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family
por: Pablo Perez-Garcia, et al.
Publicado: (2021)

Sulfamoyl Heteroarylcarboxylic Acids as Promising Metallo-β-Lactamase Inhibitors for Controlling Bacterial Carbapenem Resistance
por: Jun-ichi Wachino, et al.
Publicado: (2020)

Inhibitor discovery of full-length New Delhi metallo-β-lactamase-1 (NDM-1).
por: Bingzheng Shen, et al.
Publicado: (2013)

Identification of New Delhi metallo-β-lactamase 1 in Acinetobacter lwoffii of food animal origin.
por: Yang Wang, et al.
Publicado: (2012)

Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli
por: Ying Zhu, et al.
Publicado: (2021)

Structure of apo- and monometalated forms of NDM-1--a highly potent carbapenem-hydrolyzing metallo-β-lactamase.
por: Youngchang Kim, et al.
Publicado: (2011)

The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase
por: Bo Ma, et al.
Publicado: (2019)

Corrigendum: Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli
por: Ying Zhu, et al.
Publicado: (2021)

Functional Metagenomics Reveals a New Catalytic Domain, the Metallo-β-Lactamase Superfamily Domain, Associated with Phytase Activity
por: Genis Andrés Castillo Villamizar, et al.
Publicado: (2019)

Discovery of potential inhibitors against New Delhi metallo-β-lactamase-1 from natural compounds: in silico-based methods
por: Azhar Salari-jazi, et al.
Publicado: (2021)

A protein of the metallo-hydrolase/oxidoreductase superfamily with both beta-lactamase and ribonuclease activity is linked with translation in giant viruses
por: Philippe Colson, et al.
Publicado: (2020)

New Delhi metallo-β-lactamase-1 among Escherichia coli strains isolated from leukemia patients in Iran: two case reports
por: Mahdane Roshani, et al.
Publicado: (2021)

Increasing New Delhi metallo-β-lactamase-positive Escherichia coli among carbapenem non-susceptible Enterobacteriaceae in Taiwan during 2016 to 2018
por: Yu-Shan Huang, et al.
Publicado: (2021)

Structural analysis of the boronic acid β-lactamase inhibitor vaborbactam binding to Pseudomonas aeruginosa penicillin-binding protein 3.
por: Vijay Kumar, et al.
Publicado: (2021)

Potential inhibitors designed against NDM-1 type metallo-β-lactamases: an attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteria
por: Asad U. Khan, et al.
Publicado: (2017)

Emergence of New Delhi Metallo-β-Lactamase (NDM-5) in <italic toggle="yes">Klebsiella quasipneumoniae</italic> from Neonates in a Nigerian Hospital
por: Lauren M. Brinkac, et al.
Publicado: (2019)

Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity
por: Tushar Modi, et al.
Publicado: (2021)

IMP-68, a Novel IMP-Type Metallo-β-Lactamase in Imipenem-Susceptible <named-content content-type="genus-species">Klebsiella pneumoniae</named-content>
por: Hiroaki Kubota, et al.
Publicado: (2019)

Probing the effect of the non-active-site mutation Y229W in New Delhi metallo-β-lactamase-1 by site-directed mutagenesis, kinetic studies, and molecular dynamics simulations.
por: Jiao Chen, et al.
Publicado: (2013)

Population Structure, Molecular Epidemiology, and β-Lactamase Diversity among <named-content content-type="genus-species">Stenotrophomonas maltophilia</named-content> Isolates in the United States
por: Maria F. Mojica, et al.
Publicado: (2019)

Emergence and Spread of Carbapenem-Resistant and Aminoglycoside-Panresistant <italic toggle="yes">Enterobacter cloacae</italic> Complex Isolates Coproducing NDM-Type Metallo-β-Lactamase and 16S rRNA Methylase in Myanmar
por: Satoshi Oshiro, et al.
Publicado: (2020)

Variations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificity.
por: Deeptak Verma, et al.
Publicado: (2013)

Spherical trihedral metallo-borospherenes
por: Teng-Teng Chen, et al.
Publicado: (2020)

Emergence and Global Dissemination of Host-Specific <italic toggle="yes">Streptococcus agalactiae</italic> Clones
por: Uffe B. Skov Sørensen, et al.
Publicado: (2010)

High Rates of Aminoglycoside Methyltransferases Associated with Metallo-Beta-Lactamases in Multidrug-Resistant and Extensively Drug-Resistant Pseudomonas aeruginosa Clinical Isolates from a Tertiary Care Hospital in Egypt
por: El-Far A, et al.
Publicado: (2021)

Quantitative Insights Into β-Lactamase Inhibitor’s Contribution in the Treatment of Carbapenemase-Producing Organisms With β-Lactams
por: Yanfang Feng, et al.
Publicado: (2021)

Collateral sensitivity constrains resistance evolution of the CTX-M-15 β-lactamase
por: Carola E. H. Rosenkilde, et al.
Publicado: (2019)

Development of a generic β-lactamase screening system for improved signal peptides for periplasmic targeting of recombinant proteins in Escherichia coli
por: Tania Selas Castiñeiras, et al.
Publicado: (2018)

Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
por: Akihiro Nakamura, et al.
Publicado: (2019)

Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin.
por: Ejaz Ahmad, et al.
Publicado: (2012)