Synonym |
HSV-1 gB (497-507) |
Species |
Virus |
Protein Accession |
NA |
Purity |
> 95% by SDS-PAGE |
Endotoxin Level |
< 1.0 EU per µg of the protein |
Biological Activity |
NA |
Expression System |
E.coli |
Fusion Tag |
His-tag |
Predicted Molecular Mass |
NA |
Formulation |
Lyophilized from a 0.2 µm filtered PBS solution |
Reconstitution |
Reconstitute in PBS to a concentration of 0.1-1.0 mg/ml |
Storage & Stability |
Store lyophilized protein at -20°C. Reconstituted protein should be stored at 4°C and is stable
for at least 6 months. |
FAQ
What is HSV-1 Glycoprotein (gB) (497-507) and what is its significance in research?
HSV-1
Glycoprotein (gB) (497-507) refers to a specific peptide sequence within the glycoprotein B of Herpes
Simplex Virus type 1 (HSV-1). Glycoprotein B is a critical component of the viral envelope and plays a
pivotal role in the virus's ability to infect host cells. It is involved in the fusion of the viral
envelope with the host cell membrane, facilitating viral entry into the cell. The sequence 497-507
represents a particular segment of the glycoprotein that has garnered interest for its potential roles
in immune recognition and vaccine development. Researchers have focused on this specific fragment
because it contains epitopes that might be targeted by neutralizing antibodies, which can block the
infection process. Understanding how the immune system recognizes and responds to this segment can
provide insights into designing vaccines and therapeutics that elicit strong protective immunity.
Furthermore, because HSV-1 is a prevalent infection affecting a significant portion of the global
population, research into this glycoprotein has implications for public health, contributing to the
development of strategies to combat not just primary infections but also the recurrent episodes often
triggered by this virus. Thus, studying this glycoprotein segment not only enhances our molecular
understanding of viral entry and pathogenesis but also serves as a foundation for broader investigations
aimed at controlling HSV-related diseases.
How does HSV-1 Glycoprotein (gB) (497-507) contribute
to the virus's mechanism of infection?
HSV-1 Glycoprotein (gB) (497-507) is integral to the complex
process of HSV-1 infection, as it is part of a protein that engages directly with host cells.
Glycoprotein B (gB) is one of the essential glycoproteins required for viral entry, and it works in
concert with other glycoproteins such as gD, gH, and gL to ensure the virus successfully penetrates the
host cell. The specific segment 497-507 is thought to contain critical amino acids that can either bind
directly to receptors on host cells or participate in conformational changes necessary for membrane
fusion. Once the viral envelope fuses with the cell membrane, the viral genome can enter the host cell,
initiating the infection cycle. Other factors such as cellular receptors and the host cell type also
influence gB's function in this process. Understanding the interaction between gB and cell receptors is
crucial for elucidating the initial stages of infection, which is the fundamental step in the life cycle
of any viral pathogen. Researchers can study this interaction to uncover targets for therapeutic
intervention, potentially disrupting the virus's ability to spread and cause disease. By inhibiting the
function of gB, researchers aim to develop antiviral drugs that can efficiently prevent the virus from
entering cells, thus blocking the onset of infection. Additionally, this segment's study may help refine
strategies for deploying inhibitors or vaccines that can elicit effective immune responses, further
curbing HSV-1's impact.
What role does HSV-1 Glycoprotein (gB) (497-507) play in immune system
activation, and how might this be used in vaccine development?
HSV-1 Glycoprotein (gB) (497-507) is
a key segment within the glycoprotein B that is recognized by the immune system. This particular
sequence can function as an epitope, a specific part of an antigen that is recognized by immune cells,
notably by B cells and T cells. When the immune system encounters this segment of gB, it mounts an
immune response by generating specific antibodies and activating T cells that can identify and
neutralize the virus. Antibodies that target gB can prevent the virus from binding to and entering host
cells, thus halting infection. Due to its role in provoking an immune response, this polypeptide
sequence is of great interest in vaccine design. By incorporating this segment into a vaccine, either as
part of a whole protein or as a synthetic peptide, researchers aim to induce a robust immune response
that provides protection against HSV-1 infection. Such a vaccine would prime the immune system to
recognize critical portions of the virus more effectively and efficiently upon actual exposure. As gB is
involved in viral entry, vaccines targeting this glycoprotein segment could potentially neutralize the
virus before it even enters host cells. This method of using key viral components to train the immune
system is a promising avenue, not just for primary prevention but also for reducing the severity of
recurrent infections that are characteristic of HSV-1. Thus, through ongoing research and clinical
trials, the gB segment can play a crucial role in achieving breakthroughs in vaccine-driven immunity
against HSV-1.
How does the understanding of HSV-1 Glycoprotein (gB) (497-507) influence the
development of antiviral therapies?
The understanding of HSV-1 Glycoprotein (gB) (497-507) has a
profound impact on the development of antiviral therapies. This specific peptide segment is a part of
the larger glycoprotein B, which is a critical component of the HSV-1 viral entry machinery. Any
disruption of gB function could potentially prevent the virus from successfully entering host cells,
thereby halting infection. By thoroughly studying this segment, researchers aim to delineate the
specific interactions between gB and host cell receptors that are necessary for membrane fusion and
viral entry. With this knowledge, pharmaceutical interventions can be designed to specifically target
and inhibit these interactions. This could be achieved through small molecule inhibitors, peptides, or
antibodies that bind to this segment of gB and block its function. Additional insights gained from
structure-function studies of gB can also guide the rational design of these inhibitors, ensuring they
are both effective and specific. Besides direct inhibition of the glycoprotein, understanding its role
in the virus's life cycle can illuminate other indirect therapeutic strategies. This includes the
development of therapeutics that enhance the host immune response against this glycoprotein or even
gene-editing technologies aimed at disrupting the viral genome's capacity to encode functional gB
proteins. The development of broadly applicable antivirals that inhibit gB could also reduce the impact
of resistance, a common challenge with current antiviral drugs. Overall, the extensive research into
HSV-1 Glycoprotein (gB) (497-507) offers a promising route for developing innovative antiviral therapies
that can drastically reduce the burden of HSV-1 infections worldwide.
What is the potential
impact of research on HSV-1 Glycoprotein (gB) (497-507) on public health?
Research on HSV-1
Glycoprotein (gB) (497-507) carries significant implications for public health due to the widespread
prevalence and recurring nature of HSV-1 infections. Herpes simplex virus type 1 is a common pathogen,
affecting a substantial portion of the global population, with primary infections often occurring in
childhood. While for many it results in mild or asymptomatic issues, such as cold sores, it can have
more severe implications, including complications in immunocompromised individuals and potential links
to neurodegenerative diseases. By advancing our understanding of this viral segment's structure,
function, and its interaction with the host immune system, we can develop effective vaccines and
therapeutics. The development and deployment of a vaccine targeting this glycoprotein could dramatically
reduce the incidence of primary infections and subsequent transmissions, benefiting individual and
public health. Furthermore, advances in therapeutic interventions that halt the virus's entry into host
cells may extend beyond just treating cold sores, potentially reducing episodes of reactivation and
transmission in infected individuals. Such measures would also alleviate the economic burden associated
with managing herpes infections and their complications, including direct medical costs and indirect
losses such as productivity. Given the persistent nature of herpes viruses in hosting, research into
effective management and prevention tools can ease the societal impacts of HSV-1, improving quality of
life and reducing the stigma associated with herpes-related diseases. Moreover, the knowledge gained
from studying HSV-1 Glycoprotein (gB) (497-507) could translate to broader antiviral research,
influencing strategies to combat other viral infections with similar mechanisms of cell entry, thereby
amplifying its impact on global health.