Endosomes supporting fusion mediated by vesicular stomatitis virus glycoprotein have distinctive motion and acidification.

Most enveloped viruses infect cells by binding receptors at the cell surface and undergo trafficking through the endocytic pathway to a compartment with the requisite conditions to trigger fusion with a host endosomal membrane. Broad categories of compartments in the endocytic pathway include early and late endosomes, which can be further categorized into subpopulations with differing rates of maturation and motility characteristics. Endocytic compartments have varying protein and lipid components, luminal ionic conditions and pH that provide uniquely hospitable environments for specific viruses to fuse.

Genome-Wide Exome Analysis of -Disparate Mouse Strains that Differ in Host Resistance to Murine Cytomegalovirus Infection.

Host resistance to murine cytomegalovirus (MCMV) varies in different strains of laboratory mice due to differences in expression of determinants that control and clear viral infection. The major histocompatibility complex class I D molecule is one such determinant that controls MCMV through the action of natural killer (NK) cells. However, the extent of NK cell-mediated D-dependent resistance to infection varies in different mouse strains.

Modulating Vascular Hemodynamics With an Alpha Globin Mimetic Peptide (HbαX).

The ability of hemoglobin to scavenge the potent vasodilator nitric oxide (NO) in the blood has been well established as a mechanism of vascular tone homeostasis. In endothelial cells, the alpha chain of hemoglobin (hereafter, alpha globin) and endothelial NO synthase form a macromolecular complex, providing a sink for NO directly adjacent to the production source. We have developed an alpha globin mimetic peptide (named HbαX) that displaces endogenous alpha globin and increases bioavailable NO for vasodilation.