Related Experiment Video
Updated: Oct 18, 2026

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
Published on: September 19, 2013
Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L.
1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0314, USA.
Abstract:
The L. monocytogenes protein lnlB activates phosphoinositide 3-kinase and induces phagocytosis in several mammalian cell types. The 1.86 A resolution X-ray crystal structure of the leucine-rich repeat domain of lnlB that is both necessary and sufficient to induce phagocytosis is presented here. The structure supports a crucial role for calcium in host cell invasion by L. monocytogenes and supplies a rationale for its function. Calciums are bound to the protein in an unusually exposed manner that suggests that the metals may act as a bridge between lnlB and mammalian cell surface receptors. The structure also identifies surfaces on the curved and elongated molecule that may constitute additional interaction sites in forming a bacterial-mammalian signaling complex.
Related Concept Videos
Colonisation of Pathogens
Receptor-mediated Endocytosis
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-mediated Endocytosis
Viral Replication: Lysogenic Cycle
Intracellular Movement of Viruses and Bacteria
Adherens Junctions
Adherens Junctions are Dynamic
The endothelial cells...

