CSIR–CCMB Scientists find ‘proofreading' enzyme in bacteria
The study reveals that during cell wall construction, bacteria can mistakenly add amino acids like L-serine or glycine instead of L-alanine, weakening the wall and increasing vulnerability to antibiotics. The bacterial cell wall, made of a polymer called peptidoglycan, is essential for survival and is a common target of antibiotics.
The team identified an enzyme, Peptidoglycan Editing Factor (PgeF), that acts as a molecular editor by detecting and removing these misincorporated amino acids. 'Using advanced genetics and high-resolution mass spectrometry, we showed that PgeF ensures cell wall strength by maintaining its correct composition,' said Dr Shambhavi Garde, the study's first author.
Significantly, the team also found a human homologue of this enzyme, known as LACC1, which is linked to several autoinflammatory disorders, conditions in which the immune system becomes overactive. Though LACC1's exact function remains unclear, this research suggests a possible role in how the body responds to bacterial infections.
'This discovery not only opens new avenues for targeting bacterial vulnerabilities but also hints at shared mechanisms between microbial and human biology,' said Dr Manjula. 'Fundamental studies like this can drive novel strategies for both antimicrobial therapies and immune regulation.'
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