Multiple epitopes of hepatitis B virus surface antigen targeted by human plasma-derived immunoglobulins coincide with clinically observed escape mutations.
Abstract: We then tested in binding assays HBsAg peptides containing clinically relevant mutations previously reported within these sites, such as Y134S, P142S, and G145R, and observed a significant reduction in anti-HBs binding activity to the mutated sites, suggesting a mechanism the virus may use to avoid HBIG-mediated neutralization.
Global prevalence and phylogeny of hepatitis B virus (HBV) drug and vaccine resistance mutations.
Method: We also considered eight VEMs (C139S, S/T140I, P142S, S/T143L/M, D144A/E/G/N, G145A/E/R, K141A/I/R and C147S) which are located within the epitope region neutralized by the HBV vaccine (aa139-147).
Detection of Q129H Immune Escape Mutation in Apparently Healthy Hepatitis B Virus Carriers in Southwestern Nigeria.
Introduction: In the following years, other mutations observed on the a-determinant, which are considered as immune escape variants, including T116N, P120S/E, I/T126A/N/I/S, Q129H/R, M133L, K141E, P142S, and D144A/E, have also been reported.
A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants.
Result: In contrast, the polyclonal anti-HBsAg antibody signal was severely reduced in several mutants within the 2nd loop of 'a' determinant, such as K141I, P142L/S, D144A/E, G145K/R, N146S and T148I.
Immune-escape mutations and stop-codons in HBsAg develop in a large proportion of patients with chronic HBV infection exposed to anti-HBV drugs in Europe.
Method: Among them, sP120S/T/A, sT126N/S, sQ129R/N, sT131I/N, sM133I/L, sP142S, sD144A/E, sG145A/R were known to act as vaccine-escape mutations.
Method: We determined the prevalence of 29 immune-associated escape mutations (sQ101K, sT114R, PMID: 27167598
2017
Antiviral therapy
Method: The sequences were examined for known vaccine escape mutations (sG145R/A, sP142S, sI/T126A/N/I/S, sQ129H/R, sM133L, sD144A/E, sP120S/E, sK141E, sP134I, and sT116N), immunoprophylaxis escape mutations (
Effects of amino acid substitutions in hepatitis B virus surface protein on virion secretion, antigenicity, HBsAg and viral DNA.
Introduction: However, some newly discovered SHBs mutations were under quantitated by the Architect assay, whereas sP142L, sP142S and sG145K mutations yielded lower results in the Elecsys system when compared with those obtained with the Architect system.
Investigation of a Novel Hepatitis B Virus Surface Antigen (HBsAg) Escape Mutant Affecting Immunogenicity.
Discussion: found no reactivity of HBsAg using two commercial diagnostic assays whose sequences had simultaneous mutations at various positions, including an amino acid at 100 (Y100S), and this may have been due to mutations at other sites (T118V/R122K/M133I/Y134N/P142S/S143L/G145K).
Molecular characterization of hepatitis B virus in Vietnam.
4Method: The S gene sequence was analyzed for mutations in the ""a"" determinant region (T116 N, P120S/T, I/T126S/A, Q129H/R, M133 L/T, K141E, P142S, D144E, and G145R), and other virulence associated mutations (N3S, V184A, and S204R)."
Occult hepatitis B virus infection in anti-HBs-positive infants born to HBsAg-positive mothers in China.
HBV mutation literature information.
PMID: 
2022
Journal of medical virology
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