The challenging treatment of infections caused by multi-antibiotic-resistant bacteria is an increasingly pressing health concern. Phage therapy is a promising alternative to conventional antibiotics. Phages are naturally occurring viruses that specifically target and lyse bacteria.
We used cryo-electron microscopy to gain insights into the process of phage LUZ19 infection of a clinically relevant P. aeruginosa strain. The phage LUZ19 virion consists of a 43,5 kbp dsDNA genome packaged into a 640 Å wide icosahedral capsid. The capsid is composed of major capsid protein, head cement protein, and flexible head decoration proteins. The internal core, portal, and tail occupy one of the capsid vertices and serve for genome delivery into the bacterial cell. A dodecameric portal complex mediates the symmetry mismatch between the five-fold symmetric capsid vertex and the four-fold symmetric core complex. The tail has 280 Å in length and is differentiated into a dodecameric adaptor and a hexameric tail nozzle. It is further decorated by six flexible tail fibers. [ZC1] The whole tail has a channel passing through it that is employed to transfer the genome from the head. The tail fibers consist of a proximal arm, elbow, and distal arm facing the capsid. The research on the phage LUZ19 structure broadens our understanding of phage infection, to fight P. aeruginosa infections.
The research of the phage LUZ19 structure broadens our understanding of phage infection, to fight Pseudomonas aeruginosa infections.
Cryo-electron Microscopy and Tomography core facility (CEMCOF) of CEITEC Masaryk University is gratefully acknowledged for the obtaining of the scientific data presented on this poster.