Publications by authors named "Annabel Itterbeek"
Article Synopsis
- Type IV pili (T4P) are structures on the surface of gram-negative bacteria that enable various functions such as attaching to surfaces, forming biofilms, and moving around.
- * A protein called PlzR was found to inhibit the assembly of T4P in Pseudomonas aeruginosa, affecting how the bacteria can be infected by certain bacteriophages.
- * PlzR binds to a T4P chaperone called PilZ, disrupting the proper assembly of T4P by influencing an ATPase named PilB, and its expression is regulated by levels of cyclic di-GMP.
Mycophage endolysins are highly diverse and modular enzymes composed of domains involved in peptidoglycan binding and degradation. Mostly, they are characterized by a three-module design: an N-terminal peptidase domain, a central catalytic domain and a C-terminal peptidoglycan binding domain. Previously, the affinity of cell wall binding domains (CBDs) to the mycobacterial peptidoglycan layer was shown for some of these endolysins.
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