Atomic Force Microscopy Demonstrates that Candida glabrata Uses Three Epa Proteins To Mediate Adhesion to Abiotic Surfaces.

The fungal pathogen can cause both mucosal and disseminated infections. Cell adhesion, a key step in colonization and infection, depends in primarily on the Epa family of cell adhesion proteins. While Epa proteins have been documented to mediate specific adhesion to host glycans, some of them also promote nonspecific adhesion to abiotic surfaces, though this is incompletely understood.

Binding of Protein A to von Willebrand Factor Is Regulated by Mechanical Force.

Binding of to the large plasma glycoprotein von Willebrand factor (vWF) is controlled by hydrodynamic flow conditions. Currently, we know little about the molecular details of this shear-stress-dependent interaction. Using single-molecule atomic force microscopy, we demonstrate that vWF binds to the surface protein A (SpA) via a previously undescribed force-sensitive mechanism.

Mechanical Forces Guiding Staphylococcus aureus Cellular Invasion.

Staphylococcus aureus can invade various types of mammalian cells, thereby enabling it to evade host immune defenses and antibiotics. The current model for cellular invasion involves the interaction between the bacterial cell surface located fibronectin (Fn)-binding proteins (FnBPA and FnBPB) and the α5β1 integrin in the host cell membrane. While it is believed that the extracellular matrix protein Fn serves as a bridging molecule between FnBPs and integrins, the fundamental forces involved are not known.

Single-Cell and Single-Molecule Analysis Unravels the Multifunctionality of the Staphylococcus aureus Collagen-Binding Protein Cna.

The collagen-binding protein Cna is a prototype cell surface protein from Staphylococcus aureus which fulfils important physiological functions during pathogenesis. While it is established that Cna binds to collagen (Cn) via the high-affinity collagen hug mechanism, whether this protein is engaged in other ligand-binding mechanisms is poorly understood. Here, we use atomic force microscopy to demonstrate that Cna mediates attachment to two structurally and functionally different host proteins, i.

Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier.

Existence of a selective nucleocytoplasmic permeability barrier is attributed to Phenylalanine-Glycine rich proteins (FG-nups) within the central channel of the nuclear pore complex (NPC). Limited understanding of the FG-nup structural arrangement hinders development of strategies directed at disrupting the NPC permeability barrier. In this report we explore an alternative approach to enhancing the NPC permeability for exogenous macromolecules.