HSV-2 gD

Herpes Simplex Virus-2 gD Recombinant
Cat. No.
BT18724
Source
Synonyms
Appearance
Sterile Filtered clear solution.
Purity
HSV-2 gD protein is >95% pure as determined by 10% PAGE (coomassie staining).
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

The E.Coli derived 39.7 kDa recombinant protein contains the HSV-2 gD immunodominant regions 266-394 amino acids, fused with 26 kDa GST-tag.

Product Specs

Introduction
Herpes simplex virus (HSV) entry into host cells is mediated by interactions between viral glycoproteins and cell surface receptors. The virus particle's envelope, upon binding to specific cell surface receptors, fuses with the cell membrane. This fusion creates a pore, allowing the virus to enter the host cell. HSV entry follows a sequential process akin to other viruses. Initially, complementary receptors on the virus and cell surface facilitate membrane proximity. Subsequently, the membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore forms, enabling the release of viral envelope contents into the host cell.
Description
This recombinant protein, derived from E. coli, has a molecular weight of 39.7 kDa and comprises the immunodominant regions (amino acids 266-394) of HSV-2 gD, fused with a 26 kDa GST-tag.
Purity
Analysis by 10% SDS-PAGE and Coomassie staining indicates that the purity of HSV-2 gD protein is greater than 95%.
Physical Appearance
The product is a sterile-filtered, clear solution.
Formulation
The protein is supplied in a buffer consisting of 25mM Tris (pH 7.2), 1mM EDTA, and 50% glycerol.
Stability
For optimal storage, HSV-2 gD protein should be kept at -18°C or lower. While it remains stable at 4°C for up to one week, repeated freeze-thaw cycles should be avoided.
Purification Method
HSV-2 gD protein was purified by proprietary chromatographic technique.
Specificity
Immunoreactive with sera of HSV-infected individuals.

Product Science Overview

Introduction

Herpes Simplex Virus-2 (HSV-2) is a significant pathogen responsible for genital herpes, a common sexually transmitted infection. The virus has a complex structure, with several glycoproteins on its surface that play crucial roles in its ability to infect host cells and evade the immune system. One of these glycoproteins, glycoprotein D (gD), has been a focal point in the development of vaccines and therapeutic interventions.

Glycoprotein D (gD) and Its Role

Glycoprotein D (gD) is essential for HSV-2’s entry into host cells. It interacts with specific receptors on the surface of host cells, facilitating the fusion of the viral envelope with the host cell membrane. This interaction is critical for the virus’s ability to infect and spread from cell to cell .

Development of gD Recombinant Vaccines

The technology to produce recombinant gD-2 emerged in the early 1980s. Since then, the formulation of gD-2 subunit vaccines has undergone continuous testing and refinement . These vaccines aim to elicit an immune response specifically targeting gD, thereby preventing the virus from entering host cells and establishing infection.

Efficacy and Challenges

Despite the promising potential of gD-2 subunit vaccines, they have faced challenges in providing complete protection against HSV-2. Studies have shown that while these vaccines can elicit an immune response, they may not be sufficient to prevent infection entirely . This has led researchers to explore alternative strategies, such as live-attenuated vaccines and vaccines targeting multiple viral antigens .

Recent Advances

Recent research has focused on understanding the broader immune response to HSV-2 and identifying additional viral proteins that could serve as vaccine targets. For instance, live-attenuated HSV-2 vaccines have been shown to elicit a more comprehensive immune response, including antibodies against multiple viral proteins . This increased breadth of antibody-generating proteins may contribute to superior protection against genital herpes compared to gD subunit vaccines .

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