HBV mutation literature information.


  A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants.
 PMID: 32790777       2020       PloS one
Result: N146S showed a comparable binding to both antibodies.
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.


  Occult HBV infection in Chinese blood donors: role of N-glycosylation mutations and amino acid substitutions in S protein transmembrane domains.
 PMID: 31516090       2019       Emerging microbes & infections
Result: Introduction of the N146D/S/Y mutations in plasmid M88 and P38.II by SDM did not significantly alter the EC and IC HBsAg production pattern, although a slight reduction in HBsAg secretion was observed for P38.II mutants, as reflected by the decreased HBsAg EC/IC ratio compared to that of wt HBsAg (5-8 versus 17) (Figure 3).
Result: Mutants N146D/S/Y showed an expected non-glycosylated profile.
Result: Particularly, mutations removing the N146 glycosylation site (N146D/S/Y) were found in 4.4% (2/45) and 6% (3/50) of OBI genotype B (OBIB) and genotype C (OBIC) sequences, respectively.


  Impact of immune escape mutations and N-linked glycosylation on the secretion of hepatitis B virus virions and subviral particles: Role of the small envelope protein.
 PMID: 29604477       2018       Virology
Introduction: Abolishing N-linked glycosylation in the S domain by either N146Q or N146S mutation prevented the secretion of virions but not subviral particles (HBsAg).
Introduction: Our previous study revealed that the M133T mutation, which creates a novel glycosylation site at N131 (131NST133), could rescue virion secretion of the N146Q and N146S mutants.
Result: Mutations that abolish N-linked glycosylation (N146Q and N146S) or create an extra glycosylation site (M133T) did not markedly affect HBsAg secretion.


  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.
 PMID: 29859062       2018       BMC infectious diseases
Method: We determined the prevalence of 29 immune-associated escape mutations (sQ101K, sT114R, sP120S/T/A, sT123A/N, sT126N/S, sP127L, sA128V, sQ129R/N, sG130N/R, sT131I, sM133I/L/T,


  "Construction and expression of hepatitis B surface antigen escape variants within the ""a"" determinant by site directed mutagenesis."
 PMID: 24076590       2013       Iranian journal of immunology
1Abstract: RESULTS: Ten HBsAg mutants having single mutation within the ""a"" determinant including P120E, T123N, Q129H, M133L, K141E, P142S, D144A, G145R, N146S and C147S together with a wt form were successfully constructed and expressed in CHO cells."


  Detection of a hepatitis B surface antigen variant emerging in a patient with chronic lymphocytic leukaemia treated with fludarabine.
 PMID: 16789016       2006       Journal of medical virology
Abstract: Amino-acid sequence comparisons over the alpha determinant region revealed the following substitutions: C124N, G130R, and N146S.


  Prevalence of naturally occurring surface gene variants of hepatitis B virus in nonimmunized surface antigen-negative Chinese carriers.
 PMID: 11679975       2001       Hepatology (Baltimore, Md.)
1Abstract: These changes involved 11 positions inside and 5 outside of the historical first and second loops of the ""a"" determinant, and included the following: Q101K, T115A, K122N, T123A, T126N, Q129N, G130R, T131I, M133T, F134L, C138Y, K141E, P142S, G145R, N146S, and C147F/R."



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