Proteins of hepatitis B surface antigen

Shih, J. Wai-Kuo; Gerin, John L.

doi:10.1128/jvi.21.1.347-357.1977

Cited by 46 publications

(8 citation statements)

References 31 publications

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“…Relationship among the major polypeptides of HBsAg subtypes (adw, ayw, and adr). SDS-PAGE of HBsAg subtypes adw, ayw, and adr revealed that each had a pair of major polypeptides with apparent molecular weights of 24,000 (P-24) and 28,000 (P-28) (data not shown), as previously described (18). Peptide maps of the P-24 of each subtype are shown in Fig.…”

Section: -22supporting

confidence: 81%

Antigenic and structural relationships of the surface antigens of hepatitis B virus, ground squirrel hepatitis virus, and woodchuck hepatitis virus

Feitelson¹,

Marion²,

Robinson³

1981

J Virol

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The surface antigens of human hepatitis B (HBsAg), ground squirrel hepatitis (GSHsAg), and woodchuck hepatitis (WHsAg) viruses were compared serologically, and their major polypeptides were analyzed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis and tryptic peptide mapping. Results showed that both GSHsAg and WHsAg are antigenically cross-reactive, that their major pairs of polypeptides have identical mobilities on sodium dodecyl sulfate gels, and that the major polypeptides of GSHsAg and WHsAg migrate faster in sodium dodecyl sulfate-polyacrylamide gel electrophoresis than do the corresponding bands of HBsAg. The peptide maps of the major (P-22) surface antigen polypeptides of GSHsAg and WHsAg showed that they shared over half of their spots. Peptide mapping of HBsAg subtypes indicated a close relationship between the major polypeptides (P-24) of adw and adr and a more distal relationship to ayw. Only about 25% of the spots shared by the combined HBsAg subtypes were also found in the peptide maps of GSHsAg and WHsAg, indicating at least some structural homology among the major polypeptides of the human and animal virus surface antigen particles. This is also reflected in the serological crossreactivity among HBsAg, GSHsAg, and WHsAg. Further, the detection of ground squirrel and woodchuck antigens by Ausria II radioimmunoassay, combined with peptide mapping data indicating the common origin of these viruses, suggests that the common a determinant is shared by each and is restricted to approximately 25% of the sequences in their major polypeptides.

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Section: -22supporting

confidence: 81%

Antigenic and structural relationships of the surface antigens of hepatitis B virus, ground squirrel hepatitis virus, and woodchuck hepatitis virus

Feitelson¹,

Marion²,

Robinson³

1981

J Virol

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“…(The pre-S protein sequences of GSHV and HBV show only 17% identity, and they differ in length by 44 amino acids as a result of internal deletions or additions.) (iii) Proteins larger than mature sAg, with shared peptides and immunological reactivity, have been found in hepadnavirus particles (4,14,23,25). The most prominent of these proteins has a molecular weight of ca.…”

mentioning

confidence: 99%

Nucleotide sequence of an infectious molecularly cloned genome of ground squirrel hepatitis virus

Seeger¹,

Ganem²,

Varmus³

1984

J Virol

150

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We have determined the complete nucleotide sequence of an infectious cloned genome of ground squirrel hepatitis virus (GSHV), a nonpathogenic member of the hepadnavirus group. The genome is 3,311 base pairs long and contains the major open reading frames described for the related human and woodchuck hepatitis B viruses (HBV and WHV, respectively). These reading frames include genes for the major structural proteins (the surface and core antigens), unassigned open reading frames (A and B), the longer of which is presumed to encode the viral DNA polymerase, and an open reading frame preceding and continuous with the surface antigen gene. The arrangement of these open reading frames is similar to that encountered in the genomes of HBV and WHV: all of the reading frames are encoded on the same strand, they are positioned in the same fashion with respect to each other, and a large portion (at least 51%) of the genome can be translated in two reading frames. Comparisons of the predicted translational products of the three mammalian hepadnaviruses reveal 78% amino acid homology between the proteins of GSHV and WHV and 43% homology between those of GSHV and HBV. In addition, a perfect direct repeat of 10 to 11 base pairs, separated by ca. 46 to 223 base pairs, is present in the three mammalian viruses and in duck hepatitis B virus; the position of the repeats near the 5' termini of the two strands of virion DNA suggests a role in viral replication.

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“…apparent molecular weights by 6,500. Based on previous estimates for the carbohydrate content of HBSAg (10) and the pattern of periodic acid-Schiff stain reaction in polyacrylamide gels (14), carbohydrate should comprise no more than 25% by weight of the P-2 molecule and would account for an overestimate in molecular weight of about 2,500 (12). Therefore, the P-1 and P-2 polypeptides actually differ in molecular weight by at least 4,000.…”

mentioning

confidence: 96%

“…The approximately 22-nm form of hepatitis B surface antigen (HBAg) consists of at least seven polypeptides of which P-1 (23,000 daltons) and P-2 (29,500 daltons) are the major components (3,13,14). A third polypeptide, P-6 (72,000 daltons), is observed as a major polypeptide in some preparations.…”

mentioning

confidence: 99%

“…All of the polypeptides appear to contain the recognized group (a) and subtype (d or y) virus-specific determinants as part of their constituent structures (6,13). The P-2 component may be a glycoprotein on the basis of its reaction with periodic acid-Schiff reagent in sodium dodecyl sulfate (SDS)polyacrylamide gels (14). We report here a comparison of the major polypeptides by amino acid compositional analysis.…”

mentioning

confidence: 99%

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