Researchers have uncovered a broad mechanism in bacteria that boosts their ability to defend against environmental dangers. This finding, which could be significant for the development of new treatment methods, illustrates how a particular type of cross-linking in the bacteria’s peptidoglycan cell wall works to inhibit certain enzymes that degrade the cell wall, thereby offering protection to the bacteria.
Researchers from Umeå University in Sweden and Cornell University in the USA have uncovered a common mechanism in bacteria that enhances their defense against environmental hazards. This important discovery could be crucial for developing future treatments, as it demonstrates how a specific crosslinking method in the peptidoglycan cell wall blocks the action of certain enzymes that break down the cell wall, thus protecting the bacteria.
Bacteria are safeguarded by their peptidoglycan cell wall, which allows them to endure both the internal pressure and external threats like attacks from other bacteria and viruses. For growth and strength, bacteria require a balance of enzymes that both construct and deconstruct the cell wall. Lytic transglycolases are a key type of enzyme responsible for breaking down the peptidoglycan chains. Until now, the regulatory factors influencing their activity have not been well understood.
This research, led by Felipe Cava’s team at Umeå University alongside collaborators at Cornell University in New York, shows that a specific kind of cross-linking in the cell wall known as LD-crosslinking can inhibit the function of lytic transglycolases.
The implications of this finding are significant. For instance, some bacteria exploit these enzymes to release cell wall fragments that can influence the host’s immune response. Additionally, specific bacteria and viruses utilize these enzymes to eradicate other bacterial cells. By regulating these enzymes’ activities, bacteria can potentially shield themselves from immune responses and attacks from competing microorganisms.
“This discovery addresses a critical gap in understanding the role of LD-crosslinking in maintaining cell wall integrity,” says Felipe Cava, a professor at Umeå University. “We have demonstrated that bacteria can enhance their protection against environmental challenges, including phage attacks, through a single structural modification in their cell wall.”
This discovery sheds new light on the maintenance of bacterial cell walls and opens up potential new pathways for the development of innovative antibacterial treatments.
“Targeting LD-crosslinking may allow for the creation of new therapies that weaken the bacteria’s defenses, increasing their susceptibility to antibiotics and immune reactions,” explains Laura Alvarez, a researcher in the Department of Molecular Biology at Umeå University and the study’s first author.
This study, published in the journal Nature Communications, received funding from the Swedish Research Council, the Knut and Alice Wallenberg Foundation, and the Kempe Foundations.
