Immunochemical structure of the carboxy-terminal part of hepatitis B e antigen: identification of internal and surface-exposed sequences

Sällberg, Matti; Pushko, Peter; Berzinsh, Ivar; Bichko, V.; Sillekens, Peter; Noah, Michael; Pumpēns, Pauls; Grens, Elmars; Wahrén, Britta; Magnius, Lars O.

doi:10.1099/0022-1317-74-7-1335

Cited by 32 publications

(28 citation statements)

References 26 publications

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“…Traditional anti-HBc mouse monoclonal antibodies (mAbs) 32/312, recognizing amino acid residues 78-83, and HBe/ cAg-specific mAb 57/8, recognizing an epitope at residues 128-133, have been described in detail previously (Pushko et al, 1994;Sallberg et al, 1991Sallberg et al, , 1993.…”

Section: Methodsmentioning

confidence: 99%

“…The panel of HBcAg recombinant proteins was tested for recognition by previously characterized mAbs 35/312 (specific for residues 76-85 of HBcAg) and 57/8 (specific for residues 128-133 of HBc/eAg) (Pushko et al, 1994;Sallberg et al, 1993) by solid phase EIAs. In brief, recombinant proteins were coated overnight on microplates at 1 mg ml 21 in sodium bicarbonate buffer (pH 9?6) at 4˚C.…”

Section: Methodsmentioning

confidence: 99%

“…To characterize the particles further, all were tested for binding to the previously characterized mAbs 35/312, recognizing the HBc or HBe1 epitope LEDPASRDLV at residues 76-85 (Salfeld et al, 1989;Sallberg et al, 1991), and 57/8, recognizing the HBe2 epitope TPPAYR at positions 128-133 of HBcAg, by EIA (Pushko et al, 1994;Sallberg et al, 1993). As expected, mAb 35/312 was highly reactive against HBcAg and HBcAg-Ile but not reactive against particles HBcD79-85 and HBcD76-85 lacking the complete epitope region at positions 76-85 (Fig.…”

Section: Characterization Of Mutant Hbcag Particlesmentioning

confidence: 99%

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Priming of cytotoxic T cell responses to exogenous hepatitis B virus core antigen is B cell dependent

Lazdina

Alheim

Nyström

et al. 2003

Journal of General Virology

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The hepatitis B virus (HBV) core antigen (HBcAg) has a unique ability to bind a high frequency of naive human and murine B cells. The role of HBcAg-binding naive B cells in the immunogenicity of HBcAg is not clear. The HBcAg-binding properties of naive B cells were characterized using HBcAg particles with mutated spike region (residues 76-85) sequences. Deletion of residues 76-85 (HBcD76-85) destroyed naive B cell binding, whereas deletion of residues 79-85 did not. HBcAg particles with an Ile instead of the natural Ala at position 80 did not bind naive B cells, whereas reversion of Ile 80 RAla restored B cell binding. Destroying the B cell-binding ability of HBcAg had a marginal effect on the overall B cell immunogenicity of the different particles, suggesting that they were equally efficient in priming T helper cells. Therefore, the importance of HBcAg-binding B cells is studied with relation to the priming of HBcAg-specific cytotoxic T cells (CTLs). The role of HBcAg-binding B cells in the priming of HBcAg-specific CTLs was evaluated by immunization with endogenous HBcAg (DNA immunization) and exogenous recombinant HBcAg particles. Endogenous HBcAg primed HBcAg-specific CTLs in wild-type and B cell-deficient mice, whereas exogenous HBcAg primed HBcAg-specific CTLs only in wild-type mice. Importantly, HBcD76-85 did not prime CTLs despite the presence of B cells. Thus, the ability of exogenous HBcAg particles to prime specific CTLs is B cell dependent, suggesting a possible role for HBcAgbinding B cells in HBV infections.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Characterization Of Mutant Hbcag Particlesmentioning

confidence: 99%

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Priming of cytotoxic T cell responses to exogenous hepatitis B virus core antigen is B cell dependent

Lazdina

Alheim

Nyström

et al. 2003

Journal of General Virology

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“…After concentration, this material was subjected to sedimentation in a 10% to 60% sucrose gradient as described [35]. A total of 14 fractions were collected from the top, and aliquots were analyzed by SDS-PAGE and Western blotting using anti-core or anti-OspA Ab (mAb mc158 [46] and LA-2 [45], respectively) and appropriate secondary Ab -peroxidase conjugates, followed by chemiluminescence detection using ECL + reagent (Amersham). For an estimation of protein purity, the Coomassie Blue stained SDS-PAGE gels were scanned (Fuji LAS 3000 imager), and the distribution of Coomassie Bluestained material within one lane was densitometrically determined (Fuji AIDA software).…”

Section: Plasmid Construction and Protein Purificationmentioning

confidence: 99%

A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula

et al. 2005

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The immunogenicity of peptides and protein fragments can be considerably enhanced by their presentation on particulate carriers such as capsid‐like particles (CLP) from hepatitis B virus (HBV). Here we tested the suitability of the HBV capsid protein as a carrier for a relevant full‐length pathogen‐derived protein antigen. The entire 255‐amino acid ectodomain of the outer surface protein A (OspA) from Borrelia burgdorferi, the causative agent of Lyme disease, was inserted into the major B cell epitope of the HBV capsid, yielding a multimerization‐competent fusion protein, termed coreOspA. CoreOspA, consisting only in part of regular CLP, induced antibodies to OspA, including the Ig isotype profile and specificity for the protective epitope LA‐2, with an efficiency similar to that of recombinant lipidated OspA, the first generation vaccine against Lyme disease. Moreover, coreOspA actively and passively protected mice against subsequent challenge with B. burgdorferi. The data demonstrate the capacity of the HBV capsid protein to act as a potent immunomodulator even for full‐length and structurally complex polypeptide chains and thus opens new avenues for novel vaccine designs.

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“…Total IgG and IgG subclass distribution of murine anti-HBc and antiHBe antibodies were determined as previously described using rHBcAg or HBeAg-9n6 as the solid-phase ligands at 5 µg\ml and 1 µg\ml, respectively Sa$ llberg et al, 1993).…”

Section: Enzyme Immunoassays (Eias)mentioning

confidence: 99%

The antiviral compound ribavirin modulates the T helper (Th) 1/Th2 subset balance in hepatitis B and C virus-specific immune responses.

Hultgren¹,

Milich²,

Weiland

et al. 1998

Journal of General Virology

255

164

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Immunochemical structure of the carboxy-terminal part of hepatitis B e antigen: identification of internal and surface-exposed sequences

Cited by 32 publications

References 26 publications

Priming of cytotoxic T cell responses to exogenous hepatitis B virus core antigen is B cell dependent

Priming of cytotoxic T cell responses to exogenous hepatitis B virus core antigen is B cell dependent

A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula

The antiviral compound ribavirin modulates the T helper (Th) 1/Th2 subset balance in hepatitis B and C virus-specific immune responses.

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