Interference with AI-2-mediated bacterial cell-cell communication.
Xavier, K. B. & Bassler, B. L. Interference with AI-2-mediated bacterial cell-cell communication.
ZipA is a membrane anchored protein in Escherichia coli that interacts with FtsZ, a homolog of eukaryotic tubulins, forming a septal ring structure that mediates bacterial cell division.
Cumulatively, this study uncovered novel new layers of transcriptional regulation mediating the bacterial cell cycle.
It is well known that bacterial lectins mediate cell-cell recognition and play key roles in infection by promoting bacterial adherence to the host cells [ 36].
These include adhesins and membrane proteins that mediate bacterial attachment, colonization, and invasion of host cells.
The Listeria monocytogenes surface protein InlB mediates bacterial invasion into host cells by activating the human receptor tyrosine kinase Met.
The adherence of Actinomyces naeslundii to human buccal mucosa is mediated by specific interactions between the bacterial cell surface fimbriae and complementary beta-linked galactoside receptors on the epithelial cell surface.
Cho, H, Wivagg, CN, Kapoor, M, Barry, Z, Rohs, PD, Suh, H, Marto, JA, Garner, EC, and Bernhardt, TG. (2016) Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously.
Pili and fimbriae on the bacterial cell are virulence factors that mediate adhesion of pathogenic bacteria to host cell receptors [1].
The C-terminal domain also mediates autoproteolytic cleavage, which releases the passenger from the bacterial cell.
