Synonym |
HIV-1 Envelope glycoprotein gp41 (1-23) |
Species |
HIV-1 |
Protein Accession |
NA |
Purity |
>95% |
Endotoxin Level |
<1.0 EU per 1 μg of protein |
Biological Activity |
NA |
Expression System |
BR product |
Fusion Tag |
Amide |
Predicted Molecular Mass |
2.8 kDa |
Formulation |
Supplied as a lyophilized powder |
Reconstitution |
Reconstitute in sterile distilled water |
Storage & Stability |
Store at -20°C. For long term storage, aliquot and store at -80°C |
FAQ
What is the function of the HIV-1 env Protein gp41 (1-23) amide in HIV research and vaccine
development?
The HIV-1 env Protein gp41 (1-23) amide represents a critical fragment of the HIV-1
virus, specifically part of the gp41 transmembrane glycoprotein. This segment plays a pivotal role in
the mechanism of viral fusion and entry into host cells. Understanding this process is essential for
revealing the lifecycle of HIV and deciphering how the virus exploits host mechanisms to propagate
infection. The gp41 protein is an essential component of the envelope spike on the HIV surface, and its
region spanning amino acids 1 to 23 includes the fusion peptide, a highly conserved region across
different HIV strains. This makes it a key target for therapeutic intervention and vaccine
strategies.
The fusion peptide is responsible for the insertion into the host cell membrane,
facilitating the fusion of the viral and host cell membranes, an essential step for the viral entry that
precedes the release of viral RNA into the host cell cytoplasm. Given its critical role, the GP41 region
has been a target for neutralizing antibodies and fusion inhibitor drugs. For researchers, targeting
gp41 involves both preventive and therapeutic dimensions. Strategies aimed at eliciting an antibody
response against gp41 can potentially neutralize the virus before it gains entry to host cells, thereby
functioning as a vaccine. Alternatively, small molecules or peptides that can interfere with gp41's
function might serve as therapeutic agents by preventing the virus from effectively entering and
replicating within host cells.
In vaccine development, this peptide region is vital as it
represents a site that can be targeted by broadly neutralizing antibodies (bNAbs), which have shown
promise in both preventing infection and in the context of therapeutic vaccination where the aim is to
enhance the immune response in infected individuals. Understanding the structure and dynamics of this
region can provide insights into the design of vaccine immunogens that stimulate the production of
effective bNAbs. Thus, HIV-1 env Protein gp41 (1-23) amide stands as a cornerstone in the exploration of
vaccine candidates that aim to confer immunity by disrupting a critical stage of the viral life
cycle.
How does HIV-1 env Protein gp41 (1-23) amide contribute to understanding host-pathogen
interactions?
The HIV-1 env Protein gp41 (1-23) amide is instrumental in understanding
host-pathogen interactions due to its integral role during the viral fusion process with host cells.
This segment of the gp41 protein is directly involved in the mechanics of viral entry, making it a focal
point for studying how HIV identifies, attaches, and enters host cells. At the molecular level, the
peptide sequence of HIV-1 env Protein gp41 facilitates membrane fusion, a quintessential step for viral
entry and infection. The protein interacts with the host cell's lipid bilayer, bringing the viral
envelope in close enough proximity to the host cell membrane to allow lipid mixing and
fusion.
This sequence serves as an ideal model for studying host-pathogen interactions because it
bridges the viral and host components at the cellular interface. By examining how this peptide operates,
researchers gain insights into the mechanisms HIV employs to breach frontline cellular defenses, opening
avenues for therapeutic and preventive strategies. Such studies involve elucidating the structural
conformations that the gp41 segment adopts during the fusion process, how these are facilitated by the
biochemical environment at the target cell membrane, and how these processes can be
interrupted.
In terms of therapeutic implications, this understanding can direct the development
of fusion inhibitors that mimic the structure of gp41 (1-23) but are designed to halt its function. For
instance, insights into the conformation and binding properties of gp41 can inform the design of
molecules that competitively inhibit the fusion process, thus offering a therapeutic blockade to viral
entry. Similarly, vaccine strategies can harness this knowledge by presenting gp41-like epitopes to the
immune system, aiming to generate a protective response specifically tailored to counteract the fusion
process.
Furthermore, the detailed study of gp41 (1-23) can unveil broader principles of viral
entry applicable to other enveloped viruses, enhancing the overall understanding of viral pathogenesis.
It not only deepens the understanding of HIV but also refines the broader discourse around viral entry
mechanisms, informing a cross-pathogen strategy in virology research. Recognizing the nuances of
host-pathogen interaction through the lens of gp41 offers a holistic view that integrates molecular
virology with host immune response, guiding innovative approaches to tackling HIV and other viral
infections.
What is the significance of the peptide sequence in HIV-1 env Protein gp41 (1-23)
amide?
The peptide sequence of HIV-1 env Protein gp41 (1-23) amide holds significant importance,
primarily due to its fundamental role in the HIV viral life cycle and its potential as a target for
therapeutic interventions. This sequence includes the fusion peptide of the gp41 subunit, which is
essential for facilitating the fusion of the HIV-1 virus with the host cell membrane, a crucial stage
that enables the virus to inject its genetic material into the host cell and initiate infection.
From a structural and functional perspective, the importance of this peptide sequence lies in
its conservation across different HIV strains, indicating that despite the high mutation rate of the
virus, this segment retains a configuration necessary for maintaining the integrity of viral entry
mechanisms. This makes the peptide an attractive target for neutralizing antibodies and small-molecule
inhibitors, offering potential routes for both therapeutic and preventive interventions.
In drug
discovery, understanding the sequence can provide a template for designing fusion inhibitors that mimic
the natural conformation of the fusion peptide but block its action. These inhibitors aim to interfere
with the normal fusion mechanism, effectively preventing viral entry and subsequent replication in host
cells. Such inhibitors could be employed as part of combination therapies for individuals living with
HIV to maintain low viral loads and prevent disease progression.
Meanwhile, in vaccine
development, the sequence is vital for its potential to elicit an immune response. The conservation of
the peptide offers a target for generating broadly neutralizing antibodies that can provide protection
across different viral clades. Designing immunogens that present this peptide epitope aims to train the
immune system to recognize and neutralize the virus effectively.
Research on gp41 (1-23) also
extends beyond its immediate role in membrane fusion. By studying this sequence, researchers can gain
insights into the structural transitions and dynamics involved in the fusion process, which are crucial
for both understanding viral pathogenesis and identifying points of intervention. These structural
insights help in crafting intervention strategies that can disrupt the sequence's function, thereby
halting the viral life cycle.
Overall, the significance of the HIV-1 env Protein gp41 (1-23)
amide sequence lies in its pivotal biological function, its evolutionary conservation, and its utility
as a target for interventions aimed at preventing HIV transmission and managing infections. Its roles in
both viral structure-function studies and applied biomedicine underscore its value in the ongoing battle
against HIV/AIDS.
How can HIV-1 env Protein gp41 (1-23) amide influence the design of HIV
diagnostic tools?
HIV-1 env Protein gp41 (1-23) amide can significantly influence the design and
enhancement of HIV diagnostic tools because its sequence and the role it plays in the virus's structure
and lifecycle provide advantageous targets for both identifying and monitoring HIV infections. As a
critical component of the viral fusion mechanism that facilitates host cell entry, the presence of gp41
sequences or antibodies against them in a sample can serve as a reliable marker of HIV infection. This
makes it a useful tool in serological assays aimed at detecting HIV-1.
The conservation and
functionality of the gp41 (1-23) region suggest that it could be used to develop more precise and early
HIV diagnostic assays. Many current diagnostic tests rely on detecting antibodies against HIV antigens
in a patient's blood, and since gp41 is a key antigenic site exposed during infection, it presents
itself as an ideal candidate for inclusion in these assays. Tests that focus on detecting antibodies
specific to conserved regions like gp41 can increase the sensitivity and specificity of HIV diagnostics,
reducing false positives or negatives that arise from the variability of other viral
regions.
Furthermore, the design of diagnostic tools involving gp41 could potentially aid in
distinguishing between recent and long-term infections, which has implications for epidemiological
tracking and managing the spread of HIV. By identifying markers that indicate the stage of infection,
public health efforts can better allocate resources and tailor strategies for prevention and
intervention.
The usage of HIV-1 env Protein gp41 (1-23) amide in diagnostics is not limited to
antibody detection. Advances in molecular diagnostics could also leverage this region for nucleic
acid-based tests, such as PCR, to detect viral genetic material. By identifying sequences unique to
gp41, tests can be developed to detect both the presence of the virus and measure viral loads in
infected individuals, providing clinicians with critical data on the infection’s progress and the
efficacy of treatment regimens.
Moreover, the interaction of gp41 with host cell membranes during
viral entry can be exploited to develop biosensor platforms that mimic the host environment, offering
real-time detection capabilities with potentially greater sensitivity and speed. These approaches can
significantly enhance the early detection of HIV, allowing for prompt initiation of therapeutic
strategies and better outcomes for infected individuals.
Overall, the inclusion of gp41 (1-23) in
the development of HIV diagnostic tools offers a promising avenue to improve current methods, enabling
early and accurate detection, monitoring of infection status, and a refined understanding of the
epidemiological dynamics at play within populations.