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Discoveries about bacterial cell walls could lead to new antibiotics.
Oh Scheme of amino acid exchange reactions catalyzed by LD3,3-TPases with non-canonical (NCDAA, e.g., D-Met) and fluorescent (FDAA, e.g., HADA) D-amino acids. . B of phase contrast (PC) and fluorescence microscopy G. Oxidants Wild type, Δldtgo Mutant and ldtgo::ycbBE.C Allelic exchange cells labeled with HADA. Credit: Nature Communications (2024). DOI: 10.1038/s41467-024-45620-5

Researchers at Umeå University in Sweden, led by Professor Felipe Kava, have identified a new family of enzymes that create a unique type of cross-linking between the building blocks of bacterial cell walls. This discovery may help develop new antibiotics against infectious diseases.

Bacterial cell walls form a lattice-like structure, which protects the cells from bursting under high internal pressure and protects against external threats. The cell wall consists of sugar and are interconnected by various types of cross-links. These cross-links play an important role in providing strength and stability to the cell wall, while enabling bacteria to adapt to diverse environments and stresses.

In a ___ the study Recently published Nature Communicationsresearchers at Umeå University and international institutions have unveiled a new family of enzymes responsible for creating a unique cross-link between L-alanine and meso-diaminopimelic acid.

These amino acids are essential components of the peptide chains that make up the cell wall of many bacterial species. This enzyme, called LD1,3-transpeptidase, has been identified in various groups of alpha- and beta-proteobacteria, including opportunistic pathogens such as Burkholderia and Achromobacter.

The researchers used Gluconobacter oxydans, a A novel LD1,3-transpeptidase enzyme is employed to identify and elucidate its three-dimensional structure in vinegar production. They have shown that this enzyme has unique properties that distinguish it from other known enzymes involved in cell wall cross-linking. These specific properties enable the enzyme to utilize different substrates and carry out diverse reactions, which are important for maintaining the integrity of the cell wall.

Notably, their results show that cells lacking these cross-links show increased sensitivity to β-lactam antibiotics, making LD1,3-transpeptidases potential targets for promising therapeutic interventions. appear as promising targets, particularly those intended to enhance antibiotic effectiveness.

The study’s principal investigator is Felipe Cava, professor of infection biology at Amio University and director of the Amio Hypoxic Research Facility. With extensive expertise in bacterial cell wall research and its implications in bacterial survival Professor Kawa has led research in this field for a significant period.

“Bacteria Standing as one of the most remarkable structures, much remains to be revealed about its diversity and dynamics. Through the identification and characterization of the novel In families such as LD1,3-transpeptidase, we not only expand our understanding of bacterial biology but also discover new targets for developing antibiotics to combat them. “says Felipe Cava.

More information:
Akbar Espilat et al., A Distinct Family of L-D-Transpeptidases Catalyzes L-Ala-mDAP Crosslinks in Alpha- and Beta-Proteobacteria. Nature Communications (2024). DOI: 10.1038/s41467-024-45620-5

Provided by
Umeå University


Reference: Discovery of New Bacterial Cell Wall Enzymes May Lead to Novel Antibiotics (2024, Feb 19) https://phys.org/news/2024-02-discovery-enzymes-bacterial-cell 19 Feb 2024 Obtained from -walls. html

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