Latest news with #PgeF
New Indian Express
6 days ago
- Health
- New Indian Express
CSIR–CCMB Scientists find ‘proofreading' enzyme in bacteria
HYDERABAD: A team of scientists at the CSIR–Centre for Cellular and Molecular Biology (CCMB), Hyderabad, led by Dr Manjula Reddy, has discovered a novel proofreading mechanism in bacteria that could pave the way for new antibiotics and deepen understanding of human immune disorders. The findings were published in the journal Proceedings of the National Academy of Sciences (PNAS). 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.'
The Hindu
6 days ago
- Health
- The Hindu
Bacterial cell walls could hold clues to better human health, say CCMB scientists
Bacteria are enclosed by protective cell walls, made from a unique substance called peptidoglycan. This material is absent in other life forms, including humans, which is why many antibiotics target it. A team of scientists led by Manjula Reddy at CSIR-Centre for Cellular and Molecular Biology (CCMB), Hyderabad, has found that bacteria sometimes make mistakes while building this wall. Instead of using the correct amino acid L-alanine, they occasionally use a structurally similar one called glycine. This weakens the wall and makes bacteria more vulnerable to antibiotics. These findings have been published in the PNAS journal. Also Read | CCMB team uses E. coli to study bacterial cell wall development The bacterial cell wall is made of sugars and short chains of amino acids. Dr. Reddy's team discovered that bacteria have a special enzyme called PgeF (Peptidoglycan Editing Factor) to maintain the composition of the cell using a combination of genetics and high-resolution mass-spectrometry, according to the study's first author, Shambhavi Garde. Interestingly, a similar enzyme exists in humans. Called LACC1, it has been linked to several autoinflammatory diseases — conditions where the immune system is hyperactived, said Though LACC1's role isn't fully understood, this study suggests it might be involved in how the body responds to bacterial infections. 'By studying such vulnerabilities in cell wall synthesis, new ways of blocking bacterial growth can be designed,' the scientists said in a press release.
Time of India
6 days ago
- Health
- Time of India
Scientists identify correction mechanism in bacteria that helps maintain protective wall
Hyderabad: Scientists at the CSIR-Centre for Cellular and Molecular Biology (CCMB) in Hyderabad identified a crucial correction mechanism in bacteria that helps maintain the strength of their protective outer wall. The study, led by Dr Manjula Reddy and published in the journal Proceedings of the National Academy of Sciences (PNAS), provides new insight into how bacteria survive and how they might be better targeted by antibiotics. This could hold clues to better human health. Bacteria have a tough outer wall made of a substance called peptidoglycan, which is essential for their protection and survival. This material is not found in humans, making it an ideal target for many antibiotics. The research team found that while building this wall, bacteria can sometimes make mistakes by using the wrong amino acids, the building blocks of proteins, which weakens the wall and leaves the bacteria more vulnerable. To prevent this, bacteria use a special enzyme called PgeF (Peptidoglycan Editing Factor) that spots and removes the incorrect amino acids. "Using genetics and high-resolution mass spectrometry, we showed that PgeF works like a quality control tool to ensure the wall is built properly," said Dr Shambhavi Garde. by Taboola by Taboola Sponsored Links Sponsored Links Promoted Links Promoted Links You May Like Indonesia: New Container Houses (Prices May Surprise You) Container House | Search ads Search Now Undo You Can Also Check: Hyderabad AQI | Weather in Hyderabad | Bank Holidays in Hyderabad | Public Holidays in Hyderabad The study also found that a similar enzyme exists in humans, called LACC1. Problems in this human enzyme are linked to autoinflammatory disorders — conditions where the body's immune system goes into overdrive. This raises the possibility that understanding how LACC1 works could help develop treatments for these diseases and improve how our immune system responds to bacterial infections. Reddy noted that this discovery opens up new directions in both antibiotic development and research into immune-related conditions.
