Production of antibody to individual polypeptides derived from purified hepatitis B surface antigen

Dreesman, Gordon R.; Chairez, Ruben; Suárez, M; Hollinger, F. Blaine; Courtney, Richard J.; Melnick, Joseph L.

doi:10.1128/jvi.16.3.508-515.1975

Cited by 44 publications

(7 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The HBsAg preparation yielded two major polypeptides with apparent sizes of 25,000 and 29,000 daltons (Fig. 6a, lane 2), similar to the findings in previous studies (7,10,12,17,22). Two major polypeptides were also found in the GSHsAg preparation (Fig.…”

Section: Resultssupporting

confidence: 89%

“…Several minor components migrating more slowly in SDS-PAGE than the major polypeptides were also found in surface antigen preparations from both viruses when Coomassie blue staining or either method of radiolabeling was used to detect polypeptides. Minor polypeptide components have been repeatedly found in HBsAg preparations previously (7,10,12,17,22). Table 1 summarzes the findings from several SDS-PAGE experiments in which polypeptides were detected by Coomassie blue staining or by autoradiography of preparations radioiodinated by the iodogen procedure.…”

Section: Resultsmentioning

confidence: 86%

See 1 more Smart Citation

Structural relationships between the surface antigens of ground squirrel hepatitis virus and human hepatitis B virus

Gerlich¹,

Feitelson²,

Marion³

et al. 1980

J Virol

View full text Add to dashboard Cite

Federal Republic of Germany. HBsAg's from all sera appear to contain a groupspecific determinant a as well as d or y and w or r type-specific determinants (1, 15). Antigenic variation of some of these determinants and additional determinants such as x and q have also been described (4, 5). Several polypeptides isolated from purified preparations of 22-nm and filamentous HBsAg particles have been shown to contain the HBsAg specificities (7, 10, 12, 22). Recently it has become apparent, however, that HBV is not a unique virus. Viruses with similar ultrastructural, antigenic, molecular, and biological features have been found in eastern woodchucks (25), Beechey ground squirrels in northem California (16), and domestic ducks in China (J. Summers, personal communication). These viruses provide important animal models of HBV infection in humans, and it is of interest to determine how closely related they are. Although the surface antigens of woodchuck hepatitis virus (29) and ground squirrel hepatitis virus (GSHsAg) (16) clearly cross-react in serological tests with HBsAg, it is not known how 787

show abstract

Section: Resultssupporting

confidence: 89%

Section: Resultsmentioning

confidence: 86%

Structural relationships between the surface antigens of ground squirrel hepatitis virus and human hepatitis B virus

Gerlich¹,

Feitelson²,

Marion³

et al. 1980

J Virol

View full text Add to dashboard Cite

show abstract

“…Their cross reactivity with HBsAg determinants suggests that at least part of each of the proteins is virus coded, Recent studies suggest many of the peptides have antigenic cross reactivity (Gerin, 1974;Shih and Gerin, 1975;Gold et al, 1976;Shih and Gerin, J. Virol., in press;Sluh, Tan, and Gerin, submitted for publication;Dreesman et al, 1975) suggesting that they may share amino acid sequences and therefore not all be unique peptides. Thus, the amount of unique virus coded amino acid sequence in the proteins of HBJg particles is not known but it is probably less than 300,000 daltons.…”

Section: Discussionmentioning

confidence: 99%

The proteins of hepatitis B dane particle cores

Hruska

Robinson

1977

Journal of Medical Virology

View full text Add to dashboard Cite

Although several studies have been done to analyze the peptides of purified 22-nm HbsAg particles, no information has been published about the peptides of the core of the Dane particle which bears the other hepatitis B viral antigen. HbcAg. Dane particles and Dane particle cores (produced by NP-40 treatment of Dane particles) were purified by equilibrium centrifugation in CsCl density gradients. Two populations of Dane particles were observed at densities 1.27 and 1.24 g/ml, respectively. The higher buoyant density Dane particles yielded exclusively cores of buoyant density 1.38 g/ml in CsCl, and the lower buoyant density Dane particles yielded two kinds of cores with buoyant densities of 1.38 and 1.325 g/ml, respectively. Only the higher density Dane particles and cores manifested endogenously primed DNA polymerase activity. The peptides of density 1.38 g/ml Dane particle cores purified by equilibrium CsCl density gradient centrifugation and HBcAg particles from HBV infected chimpanzee liver purified in the same way were analyzed by SDS-polyacrylamide gel electrophoresis. Both kinds of particles were found to consistently contain 3 Coomassie blue staining peptides with approximate molecular weights of 19,000, 70,000 and 80,000 daltons (designated P-19, P-70 and P-80 respectively). In addition, the HBcAg particles from infected liver regularly yielded a protein component with molecular weight greater than 200,000 daltons. This component was occasionally present in electrophoresis runs of core peptides from only one of two patients. Its irregular appearance after gel electrophoresis suggests it may have been an aggregate not completely dissociated under the conditions used. The lower density core component consistently contained P-19, P-70, and P-80, and infrequently additional minor peptides of uncertain origin. The irregular occurrence of the minor peptides in varying amounts suggests they were not intrinsic core proteins.

show abstract

“…The two major ones are called : polypeptides I and II. The molecular weight of the polypeptide I was estimated between 22,000 and 26,000; the polypeptide II is glycosylated and its molecular weight was estimated between 28,000 and 30,000 (9)(10)(11)(12). The amino-acid compositions of the two polypeptides appear very similar.…”

Section: Introductionmentioning

confidence: 99%

Localization on the viral genome and nucleotide sequence of the gene coding for the two major polypeptides of the Hepatitis B surface antigen (HBs Ag)

Charnay¹,

Mandart²,

Hampe³

et al. 1979

Nucl Acids Res

View full text Add to dashboard Cite

The structural gene coding for both polypeptides I and II which are the two major polypeptides of the Hepatitis B surface antigen, is found to be localized on the viral genome. This gene, referred to as gene S, is located in the partially single stranded region. It maps between positions 73.6 and 95.1% of the genome length. It is composed of 678 nucleotides, which correspond to a theoretical polypeptide of 25,422 molecular weight.

show abstract

Production of antibody to individual polypeptides derived from purified hepatitis B surface antigen

Abstract: Purified preparations of hepatitis B surface antigen (HB. Ag) were solubilized with sodium dodecyl sulfate and urea under reducing conditions and subsequently fractionated by preparative sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis (PAGE).

Cited by 44 publications

References 25 publications

Structural relationships between the surface antigens of ground squirrel hepatitis virus and human hepatitis B virus

Structural relationships between the surface antigens of ground squirrel hepatitis virus and human hepatitis B virus

The proteins of hepatitis B dane particle cores

Localization on the viral genome and nucleotide sequence of the gene coding for the two major polypeptides of the Hepatitis B surface antigen (HBs Ag)

Contact Info

Product

Resources

About