Scientists discover how potent bacterial toxin kills MRSA bacteria

New research from the University of 葫芦影业 has revealed the mechanism an enzyme uses to target and kill MRSA bacteria.

lysostaphin

Scientists from the University of 葫芦影业 have discovered how a potent bacterial toxin is able to target and kill MRSA, paving the way for potential new treatments for superbugs.

New research, led by Dr St茅phane Mesnage from the University of 葫芦影业, has explained how lysostaphin specifically recognises MRSA cell walls and quickly causes the breakdown of this pathogen.

The lysostaphin is able to increase the number of its molecules bound to the surface of the MRSA cell and this allows the enzyme to 鈥榳alk鈥 along the cell walls and cause rapid breakdown.

Lysostaphin is an enzyme that has been shown to eradicate Staphylococcal infections, such as MRSA, alone or in combination with antibiotics. Although it was discovered over 50 years ago, not much has been known about how it kills these infections.

The scientists hope to use their findings to develop new treatments for MRSA and other antibiotic resistant superbugs which target the infection in a similar way.

MRSA is a bacterial superbug that is resistant to several antibiotics and frequently spreads in hospitals where people are more susceptible to infection.

Dr St茅phane Mesnage, Senior Lecturer in Molecular Biology and Biotechnology, said: 鈥淟ysostaphin is arguably the most studied enzyme after lysozyme, so we are delighted that our research is able to explain the mechanism underpinning its potent antibacterial activity.

鈥淥ur study explains how this enzyme is able to target and digest the MRSA bacteria and why it is so potent. Hospital-acquired infections caused by bacteria resistant to last resort antibiotics are on the rise, but our work could lead to the development of new treatments for these superbugs that use the same targeting mechanism.鈥

The paper 鈥楾wo-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b鈥, is published today (Monday 4 November) in Nature Chemical Biology.

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