Structure of hepatitis B surface antigen. Correlation of subtype with amino acid sequence and location of the carbohydrate moiety.

Peterson, Darrell L.; Nath, N; Gavilanes, Francisco

doi:10.1016/s0021-9258(18)34034-1

Cited by 83 publications

(12 citation statements)

References 24 publications

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“…Studies on HBsAg proteins derived from human plasma have provided direct evidence for diantennary A-acetyllactosamine-type A-glycans with and without sialic acid residues (Hanaoka et al, 1986;Gillece-Castro et al, 1987), and circumstantial evidence has been provided from glycosidase digestions (endo H and neuraminidase) for a mannose-rich iV-glycan and, surprisingly, terminal sialic acid residues (Stibbe & Gerlich, 1982). Peterson et al (1982) also have provided evidence from radiolabel incorporation studies (and selective removal of the label) that sialic acid is present in the carbohydrate moiety of the S protein of HBsAg derived from human plasma.…”

Section: Discussionmentioning

confidence: 99%

Structural characterization of the N-glycans of a recombinant hepatitis B surface antigen derived from yeast

Miller²,

Kubek³

et al. 1992

Biochemistry

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The N-glycans of purified recombinant middle surface protein (preS2+S) from hepatitis B virus, a candidate vaccine antigen expressed in a mnn9 mutant strain of Saccharomyces cerevisiae, have been characterized structurally. The glycans were released by N-glycanase treatment, isolated by size-exclusion chromatography on Sephadex G-50 and Bio-Gel P-4 columns, and analyzed by 500-MHz 1H NMR spectroscopy and fast atom bombardment mass spectrometry. The mixture of oligosaccharides was fractionated by HPLC, the major subfractions were isolated, and their carbohydrate compositions were determined by high-pH anion-exchange chromatography with pulsed amperometric detection. The combined results suggest that high-mannose oligosaccharides account for all the N-glycans released from preS2+S: structures include Man7GlcNAc2, Man8GlcNAc2, and Man9GlcNAc2 isomers in the ratios of 3:6:1. Approximately 80% of the oligosaccharides contain the C2,C6-branched trimannosyl structural element typical of yeast high-mannose oligosaccharides but not usually found in high-mannose oligosaccharides in animal glycoproteins.

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Section: Discussionmentioning

confidence: 99%

Structural characterization of the N-glycans of a recombinant hepatitis B surface antigen derived from yeast

Miller²,

Kubek³

et al. 1992

Biochemistry

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“…The observation that the B I 0.HTT strain (I-C k) responded to the d determinant and not the y determinant upon hyperimmunization is also of interest. It has been suggested that the d and y determinants of HBsAg may differ by as few as two amino acid residues (17,18), yet the I-C k allele permitted responsiveness to the d but not they determinant. This may provide insight into mechanisms of possible interaction between I-Cencoded molecules and restricted domains on HBsAg.…”

Section: Discussionmentioning

confidence: 99%

Genetic regulation of the immune response to hepatitis B surface antigen (HBsAg). IV. Distinct H-2-linked Ir genes control antibody responses to different HBsAg determinants on the same molecule and map to the I-A and I-C subregions.

Milich¹,

Leroux‐Roels²,

Louie³

et al. 1984

The Journal of Experimental Medicine

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We have previously demonstrated that the murine humoral immune responses to the group-specific a and subtype-specific d/y determinants of hepatitis B surface antigen (HBsAg) are controlled by H-2-linked immune response (Ir) genes. High responder (H-2d,q), intermediate responder (H-2a greater than b greater than k) and nonresponder (H-2f,s) haplotypes have been identified (8, 9). The kinetics and specificity of in vivo antibody production after HBsAg immunization in congeneic, H-2-recombinant strains was analyzed to further define relevant Ir genes and their influence on the immune response to distinct antigenic determinants. These studies indicate that the humoral anti-HBs response is regulated by at least two Ir genes, one in the I-A subregion (Ir-HBs-1) and one in the I-C subregion (Ir-HBs-2) of the murine H-2 complex. Ir-HBs-1 regulates the primary responses to all HBsAg determinants, whereas the influence of Ir-HBs-2 is determinant specific, affecting the responses to the d or y determinants. The anti-a response is regulated exclusively by Ir-HBs-1. Strains possessing only the Ir-HBs-2 gene [B10.S(9R) and B10.HTT] produce no anti-a response and a subtype-specific antibody response is detected only after secondary or tertiary immunization. In contrast, the influence of Ir-HBs-2 in the presence of Ir-HBs-1 is detected upon primary immunization and is additive rather than exclusive. There is also suggestive evidence that the presence of the Ek molecule, at least in the context of I-Ak, may have a suppressive influence on the anti-HBs response. Additionally, HBsAg-specific, T cell proliferative responses were H-2 restricted and the kinetics and specificity of T cell proliferative responses paralleled in vivo antibody production. These data indicate that, although the I-A subregion exerts a dominant influence, distinct Ir-HBs genes, mapping in separate I subregions, control immune responses to alternate HBsAg determinants on the same protein molecule.

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“…The S domain of all three envelope proteins becomes N-glycosylated at Asn-146 in the "a"determinant in about half of the molecules (33,34). This leads to the characteristic double band patterns in sodium dodecyl sulfate-polyacrylamide gel electrophoresis of HBV particles under reducing conditions (22,35).…”

Section: The Modular Architecture Of the Hepatitis B Virus Envelope Proteinsmentioning

confidence: 99%

“…Likewise, the M protein, unique to mammalian hepadnaviruses (41), is essential for neither morphogenesis nor infectivity (40), and M-deficient mutants frequently emerge during chronic infection (73)(74)(75). The S protein alone is sufficient to drive secretion of 20-nm HBsAg spheres (29,33,34,(76)(77)(78)(79), and thus heterologously expressed S became the first vaccine worldwide produced via recombinant DNA technology (80). The secretion competence of S is opposed by a secretion inhibitory effect of L (37,(81)(82)(83)(84)(85).…”

Section: The Modular Architecture Of the Hepatitis B Virus Envelope Proteinsmentioning

confidence: 99%

The Hepatitis B Virus Envelope Proteins: Molecular Gymnastics Throughout the Viral Life Cycle

et al. 2020

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New hepatitis B virions released from infected hepatocytes are the result of an intricate maturation process that starts with the formation of the nucleocapsid providing a confined space where the viral DNA genome is synthesized via reverse transcription. Virion assembly is finalized by the enclosure of the icosahedral nucleocapsid within a heterogeneous envelope. The latter contains integral membrane proteins of three sizes, collectively known as hepatitis B surface antigen, and adopts multiple conformations in the course of the viral life cycle. The nucleocapsid conformation depends on the reverse transcription status of the genome, which in turn controls nucleocapsid interaction with the envelope proteins for virus exit. In addition, after secretion the virions undergo a distinct maturation step during which a topological switch of the large envelope protein confers infectivity. Here we review molecular determinants for envelopment and models that postulate molecular signals encoded in the capsid scaffold conducive or adverse to the recruitment of envelope proteins. Expected final online publication date for the Annual Review of Virology, Volume 7 is September 29, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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Structure of hepatitis B surface antigen. Correlation of subtype with amino acid sequence and location of the carbohydrate moiety.

Cited by 83 publications

References 24 publications

Structural characterization of the N-glycans of a recombinant hepatitis B surface antigen derived from yeast

Structural characterization of the N-glycans of a recombinant hepatitis B surface antigen derived from yeast

Genetic regulation of the immune response to hepatitis B surface antigen (HBsAg). IV. Distinct H-2-linked Ir genes control antibody responses to different HBsAg determinants on the same molecule and map to the I-A and I-C subregions.

The Hepatitis B Virus Envelope Proteins: Molecular Gymnastics Throughout the Viral Life Cycle

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