Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019163 (hepatitis B)
 38,309 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We predicted the localization of a major hepatitis B surface antigen (HBsAg) determinant within residues 135-155 [Neurath, A.R., Strick, N. & Oleszko, W.R. (1981) J. Virol. Methods 3, 115-125]. A peptide corresponding to this sequence (P135-155) was synthesized, linked to macromolecular carriers, and used to immunize rabbits. In accordance with published data on shorter peptides within the same amino acid sequence, antibodies to HBsAg were elicited. A detailed analysis of the immune response to P135-155 revealed the following: A heterogeneous population of IgG and IgM antibodies reacting with P135-155 was detected in the antisera by a variety of radioimmunoassays and enzyme-linked fluorescence immunoassays. Only a subpopulation of these antibodies reacted with HBsAg. The equilibrium constant (K) for the reaction of the antibodies with HBsAg (K = 4 X 10(5) M-1) was approximately two orders of magnitude lower than K for the reaction with P135-155 and was below K for the reaction between HBsAg and antibodies elicited by HBsAg (K greater than 10(7) M-1). Preimmunization with P135-155 did not result in an enhanced response to subsequent immunization with HBsAg. Peptides more accurately mimicking determinants on HBsAg may have to be synthesized for possible application in antiviral prophylaxis.
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PMID:Specificity of antibodies elicited by a synthetic peptide having a sequence in common with a fragment of a virus protein, the hepatitis B surface antigen. 618 53

We predicted the localization of a major hepatitis B surface antigen (HBsAg) determinant within residues 135-155. A peptide corresponding to this sequence (P135-155) was synthesized, linked to macromolecular carriers and used to immunize rabbits. In accordance with published data on shorter peptides within the same amino acid sequence, antibodies to HBsAg were elicited. A detailed analysis of the immune response to P135-155 revealed the following: A heterogeneous population of IgG and IgM antibodies reacting with P135-155 was detected in the antisera by a variety of radioimmunoassays and enzyme linked fluorescence immunoassays. Only a subpopulation of these antibodies reacted with HBsAg. The equilibrium constant (K) for the reaction of the antibodies with HBsAg (K = 4 X 10(5) X M-1) was approximately two orders of magnitude lower than K for the reaction with P135-155, and was below K for the reaction between HBsAg and antibodies elicited by HBsAg (K greater than 10(7) X M-1). Preimmunization with P135-155 did not result in an enhanced response to subsequent immunization with HBsAg. Peptides more accurately mimicking determinants on HBsAg may have to be synthesized for possible application in antiviral prophylaxis.
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PMID:Specificity of antibodies elicited by a synthetic peptide having a sequence in common with a fragment of a virus protein--the hepatitis B surface antigen. 619 27

Peptides synthesized for potential application as antiviral vaccines have been mostly tested in the form of conjugates with carrier proteins. The possible use of several distinct synthetic vaccines in prophylaxis would be facilitated by the availability of fully synthetic immunogens. A synthetic peptide corresponding to residues 135 to 155 ( P135 -155) of hepatitis B surface antigen (HBsAg) failed to elicit in free form anti-peptide antibodies or anti-HBs. However, polymers of P135 -155 (prepared by linking to diaminoalkanes ) and synthetic conjugates prepared by binding P135 -155 to liposomes or polylysine were immunogenic. A poor correlation was observed between anti-peptide and anti-HBs responses elicited by these conjugates. Glutaraldehyde-fixed liposomes appeared to be the carriers of choice for inducing anti-HBs.
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PMID:Antibodies to hepatitis B surface antigen (HBsAg) elicited by immunization with a synthetic peptide covalently linked to liposomes. 620 27