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Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
N-acetylglucosamine deacetylase
Overview
Resistance to mucosal lysozyme compensates for the fitness deficit of peptidoglycan modifications by Streptococcus pneumoniae.
The study identifies pgdA and adr as genes involved in peptidoglycan modifications that confer resistance to human lysozyme in Streptococcus pneumoniae.
Helicobacter pylori peptidoglycan modifications confer lysozyme resistance and contribute to survival in the host.
The study identifies PgdA and PatA as peptidoglycan modification enzymes in Helicobacter pylori that confer lysozyme resistance. Both genes contribute synergistically to protect the bacterium from lysozyme-mediated killing, particularly in the presence of lactoferrin.
Listeria monocytogenes Is Resistant to Lysozyme through the Regulation, Not the Acquisition, of Cell Wall-Modifying Enzymes.
The study identifies pgdA, pbpX, degU, and rli31 as key players in Listeria monocytogenes resistance to lysozyme, highlighting the importance of gene regulation rather than the acquisition of new enzymes.
Lysozyme Resistance in Clostridioides difficile Is Dependent on Two Peptidoglycan Deacetylases.
The study identifies two peptidoglycan deacetylases, PgdA and PdaV, as essential for lysozyme resistance in Clostridioides difficile. Both genes contribute to peptidoglycan deacetylation, which is crucial for resisting lysozyme-mediated cell lysis.
Peptidoglycan analysis reveals that synergistic deacetylase activity in vegetative Clostridium difficile impacts the host response.
The study identifies PgdA and PdaV as the primary N-deacetylases in C. difficile responsible for peptidoglycan N-deacetylation and lysozyme resistance. PgdB shows limited involvement in N-deacetylation and lysozyme resistance.
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