Attacking pneumonia at the molecular level!

Atomic details of a molecular crowbar that breaks Klebsiella Pneumoniae polysaccaride shielding, have been obtained from XRD2 structural data. It represents a potential new tool to fight this tough nosocomial pathogen!

(Ref: Squeglia F. et al, Structure, 28(6),613–624.e4 (2020))

Klebsiella Pneumoniae (KP) is the bacterium responsible for the most common human nosocomial infections (i.e. pneumonia, respiratory tract-urinary system infections, and septicemia). To treat K. pneumoniae infections, different antimicrobials have been widely used, leading to evolution of antibiotic resistant bacterial strains.
Virulence in KP is mediated by several factors, such as its external polysaccharide capsule (CPS). CPS protects bacteria from unfavourable environmental conditions and enables the adherence to host tissues; poorly capsulated KP strains are indeed more efficiently phagocytized by immune defenses. This capsule and other bacterial surface polysaccharides act also as a physical barrier that limits bacteriophage (viral) infection. That's why some bacterial viruses (phages) have special tools to degrade capsules (i.e. proteins with depolymerization activity).
These highly specific phage-borne enzymes can be effective in treating and preventing bacterial infections, demolishing bacterial biofilms. XRD2 structural data provide atomic details on this novel potential anti-pneumonia swiss-knife.

Retrieve Article
Structural and Functional Studies of a Klebsiella Phage Capsule Depolymerase Tailspike: Mechanistic Insights into Capsular Degradation,
Flavia Squeglia, Barbara Maciejewska, Agnieszka Łątka, Yves Briers, Zuzanna Drulis-Kawa and Rita Berisio
Structure 2020 28(6),613–624.e4, doi: 10.1016/j.str.2020.04.015, PDB: 6TKU
Last Updated on Sunday, 07 June 2020 10:17