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S-HBsAg 分子别名

S-HBsAg, HBsAg

S-HBsAg 分子背景

Hepatitis B is a potentially life-threatening liver infection caused by the hepatitis B virus (HBV). The hepatitis B virus attacks the liver and can cause both acute and chronic disease that puts people at high risk of death from cirrhosis and liver cancer. The virus is most commonly transmitted from mother to child during birth and delivery, as well as through contact with blood or other body fluids. Hepatitis B virus (HBV) is a member of the hepadnavirus family. The virus particle (virion) consists of an outer lipid envelope and an icosahedral nucleocapsid core composed of core protein. The nucleocapsid encloses the viral DNA and a DNA polymerase that has reverse transcriptase activity. The outer envelope contains embedded proteins that are involved in viral binding of, and entry into, susceptible cells. The surface antigens (HBsAg) decorating the lipid envelope of HBV is produced in excess during the life cycle of the virus, and its presence in blood indicates current hepatitis B infection.

S-HBsAg 前沿进展

A novel method for recombinant mammalian-expressed S-HBsAg virus-like particle production for assembly status analysis and improved anti-HBs serology
Lehky, Moonian, Michel et al
Protein Sci (2025) 34 (1), e5251
Abstract: The Hepatitis B surface antigen (HBsAg) as the only lipid-associated envelope protein of the Hepatitis B virus (HBV) acts as cellular attachment and entry mediator of HBV making it the main target of neutralizing antibodies to provide HBV immunity after infection or vaccination. Despite its central role in inducing protective immunity, there is however a surprising lack of comparative studies examining different HBsAgs and their ability to detect anti-HBs antibodies. On the contrary, various time-consuming complex HBsAg production protocols have been established, which result in structurally and functionally insufficiently characterized HBsAg. Here, we present an easy-to-perform, streamlined and robust method for recombinant S-HBsAg virus-like particle (VLP) production by transient expression in mammalian cells and purification from the cell lysate with the aim of displaying uniform antigenic epitopes on the surface to improve serological detection of anti-HBs antibodies. We not only compare assembly status and particle composition by transmission electron microscopy and mass photometry of our S-HBsAg and of commonly used HBsAg reference samples, but also assess their antigenic quality and functional suitability for anti-HBs antibody detection to identify the best performing sample for serological screenings. While we found that serum-isolated and recombinant HBsAg VLPs are assembled differently, our S-HBsAg VLPs detected anti-HBs antibodies with the highest sensitivity and specificity in multiplex serology when compared to yeast or serum HBsAg making it the most suitable antigen for analysis of HBV immunity through anti-HBs serostatus.© 2024 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
Exchanges in the 'a' determinant of the hepatitis B virus surface antigen revisited
Pondé, Amorim
Virology (2024) 599, 110184
Abstract: The hepatitis B virus surface antigen's (HBsAg) 'a' determinant comprises a sequence of amino acid residues located in the major hydrophilic region of the S protein, whose exchanges are closely associated with compromising the antigenicity and immunogenicity of that antigen. The HBsAg is generally present in the bloodstream of individuals with acute or chronic hepatitis B virus (HBV) infection. It is classically known as the HBV infection marker, and is therefore the first marker to be investigated in the laboratory in the clinical hypothesis of infection by this agent. One of the factors that compromises the HBsAg detection in the bloodstream by the assays adopted in serological screening in both clinical contexts is the loss of S protein antigenicity. This can occur due to mutations that emerge in the HBV genome regions that encode the S protein, especially for its immunodominant region - the 'a' determinant. These mutations can induce exchanges of amino acid residues in the S protein's primary structure, altering its tertiary structure and the antigenic conformation, which may not be recognized by anti-HBs antibodies, compromising the infection diagnosis. In addition, these exchanges can render ineffective the anti-HBs antibodies action acquired by vaccination, compromise the effectiveness of the chronically HBV infected patient's treatment, and also the HBsAg immunogenicity, by promoting its retention within the cell. In this review, the residues exchange that alter the S protein's structure is revisited, as well as the mechanisms that lead to the HBsAg antigenicity loss, and the clinical, laboratory and epidemiological consequences of this phenomenon.Copyright © 2024 Elsevier Inc. All rights reserved.
Decreased expression of HBV surface antigen (HBsAg) with sK122R and sV96A co-mutation is associated with an ineffective antibody response in a chronic hepatitis B patient
Han, Hu, Nan et al
Infect Genet Evol (2023) 111, 105431
Abstract: Emergence and predominance of hepatitis B virus (HBV) variants carrying S gene mutations frequently occur in HBV-infected individuals. Here, coexistent serum anti-HBsAg antibody (HBsAb) and HBV surface antigen (HBsAg) were detected in a chronic HBV patient. The patient's HBsAg proteins possessed amino acid substitutions sK122R and sV96A. We reported this case and conducted relevant studies to investigate differences in expression levels and antibody neutralization of HBsAg proteins bearing sK122R and sV96A amino acid substitutions to explore causes of antigen-antibody coexistence in a chronic hepatitis B patient.We first sequenced the S gene from HBV present within the patient's serum. Based on the S gene sequence, we cloned wild-type and mutated S gene sequences via site-directed mutagenesis to construct expression plasmids pJW4303-WT (wild-type), pJW4303-sV96A, pJW4303-sK122R, and pJW4303-sV96A-sK122R. Plasmids were transfected into HEK 293 T cells then culture supernatants and cells were collected. Collected cells and supernatants were next subjected to a series of quantitative and functional tests to assess expression and neutralization characteristics of wild-type and mutant HBsAg proteins.Based on quantification of HBsAg expression in cells transfected with the four plasmids, HBsAg-sK122R-sV96A was more intracellularly retained and less secreted than HBsAg-sV96A single-mutant protein and WT. Neutralization ability of serum from chronic HBV patient against culture supernatants containing recombinant HBsAg proteins were ranked from highest to lowest as HBsAg-sV96A, HBsAg-sV96A-sK122R, and HBsAg-sK122R. However, no significant differences of neutralization efficiency by high-potency antibodies from HBV-vaccinees against these three mutant proteins were observed.The levels of HBsAg proteins with amino acid substitutions sV96A-sK122R were greatly reduced in culture supernatants but were apparently increased in the intracellular fraction. This may account for the higher levels of HBV replication in patients. HBsAg neutralization by HBsAb in this patient may have been compromised by the HBsAg sK122R amino acid substitution, suggesting that antibodies produced by the patient had lost their HBV-neutralizing effect.Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.
Showing 1-3 of 51 papers.
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