Rat CD111/Nectin-1/PVRL1 (His Tag) recombinant protein

Rat CD111/Nectin-1/PVRL1 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1 is a cell adhesion molecule belonging to the immunoglobulin superfamily that can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). CD111/Nectin-1/PVRL1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were tested for the ability to bind soluble forms of viral gD and to be infected by HSV and PRV, before and after calcium depletion. It has been revealed that binding of HSV and PRV gD was localized to adherens junctions in cells maintained in normal medium but was distributed, along with nectin-1, over the entire cell surface after calcium depletion. Both the binding of gD and the fraction of cells that could be infected by HSV-1 and PRV were enhanced by calcium depletion. Taken together, CD111/Nectin-1/PVRL1 confined to adherens junctions in epithelial cells is not very accessible to virus, whereas dissociation of cell junctions releases nectin-1 to serve more efficiently as an entry recptor.

OFC7; HIGR; MGC16207; AW549174; NECTIN-1; PRR; ED4; AI835281; HVEC; MGC142031; SK-12; PVRR; PVRR1; PRR1; HV1S; CD111; CLPED1; PVRL1

Human Cells

A DNA sequence encoding the rat PVRL1 (XP_236210.3) (Met1-Ala354) was expressed, fused with a polyhistidine tag at the C-terminus.

Rat

The recombinant rat PVRL1 comprises 335 amino acids and predicts a molecular mass of 37.6 kDa. The apparent molecular mass of the recombinant protein is approximately 55-60 kDa in SDS-PAGE under reducing conditions due to glycosylation.

> 97 % as determined by SDS-PAGE