Antimicrobial-resistant pathogens are an ongoing threat tohuman and animal health. According to the World Health Organization (WHO),colistin is considered the last resort antibiotic against human infections dueto multidrug-resistant Gram-negative organisms—including Acinetobacterbaumanni, a priority-1 pathogen. Despite colistin being considered a last resortantibiotic, transferable bacterial resistance to this drug has been reported inhumans and animals. This makes addressing colistin resistance a critical priorityin public health efforts. The large PetN transferase membrane protein PmrC isresponsible for colistin resistance due to its catalysed modification of lipid A ofthe external membrane. Despite its importance, this potential drug target wasnever characterised at a molecular level (PDF) Structure-based targeting of the lipid A-modifying enzyme PmrC to contrast colistin resistance in Acinetobacter baumannii. Available from: https://www.researchgate.net/publication/386878267_Structure-based_targeting_of_the_lipid_A-modifying_enzyme_PmrC_to_contrast_colistin_resistance_in_Acinetobacter_baumannii#fullTextFileContent [accessed Dec 19 2024].

Structure-based targeting of the lipid A-modifying enzyme PmrC to contrast colistin resistance in Acinetobacter baumannii

Maria Romano
Primo
Writing – Review & Editing
;
Alessia Ruggiero
Methodology
;
Valeria Napolitano
Methodology
;
Ida Autiero
Software
;
Flavia Squeglia
Penultimo
Writing – Original Draft Preparation
;
Rita Berisio
Ultimo
Writing – Original Draft Preparation
2024

Abstract

Antimicrobial-resistant pathogens are an ongoing threat tohuman and animal health. According to the World Health Organization (WHO),colistin is considered the last resort antibiotic against human infections dueto multidrug-resistant Gram-negative organisms—including Acinetobacterbaumanni, a priority-1 pathogen. Despite colistin being considered a last resortantibiotic, transferable bacterial resistance to this drug has been reported inhumans and animals. This makes addressing colistin resistance a critical priorityin public health efforts. The large PetN transferase membrane protein PmrC isresponsible for colistin resistance due to its catalysed modification of lipid A ofthe external membrane. Despite its importance, this potential drug target wasnever characterised at a molecular level (PDF) Structure-based targeting of the lipid A-modifying enzyme PmrC to contrast colistin resistance in Acinetobacter baumannii. Available from: https://www.researchgate.net/publication/386878267_Structure-based_targeting_of_the_lipid_A-modifying_enzyme_PmrC_to_contrast_colistin_resistance_in_Acinetobacter_baumannii#fullTextFileContent [accessed Dec 19 2024].
2024
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli
protein structure
colistin resistance
virtual screening
pEtN transferase
cell wall
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Descrizione: Antimicrobial-resistant pathogens are an ongoing threat to human and animal health. According to the World Health Organization (WHO), colistin is considered the last resort antibiotic against human infections due to multidrug-resistant Gram-negative organisms-including Acinetobacter baumanni, a priority-1 pathogen. Despite colistin being considered a last resort antibiotic, transferable bacterial resistance to this drug has been reported in humans and animals. This makes addressing colistin resistance a critical priority in public health efforts. The large PetN transferase membrane protein PmrC is responsible for colistin resistance due to its catalysed modification of lipid A of the external membrane. Despite its importance, this potential drug target was never characterised at a molecular level.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/520439
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