Disulfide bond structure of glycoprotein D of herpes simplex virus types 1 and 2

Disulfide bond structure determination and biochemical analysis of glycoprotein C from herpes simplex virus.

A biochemical analysis of glycoprotein C (gC of herpes simplex virus was undertaken to further characterize the structure of the glycoprotein and to determine its disulfide bond arrangement. We used three recombinant forms of gC, gC1(457t), gC1(delta33-123t), and gC2(426t), each truncated prior to the transmembrane region. The proteins were expressed and secreted by using a baculovirus expressi...

Immunogenicity and Efficacy of Baculovirus Derived Glycoprotein D of Herpes Simplex Virus Type-I in Mice

Prevalence of Herpes Simplex Virus type-1, 2 and Varicella Zoster Virus (VZV) in Eye Infection

Abstract Background and Aims: Herpes simplex virus (HSV) is a common cause of corneal disease and is the leading infectious cause of corneal blindness among developed nations. This study is aimed to provide an estimation of the incidence of Herpes Simplex Virustype-1, 2(HSV1, 2) and Varicella Zoster Virus (VZV) in tears and swab from eye infection by polymerase chain reaction (PCR) in eye ...

Crystal structure of glycoprotein B from herpes simplex virus 1.

Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extend...

Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1

Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells. Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells. We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution. The structure reveals that the nectin-1 bi...