Result: These mutation positions corresponded with those of five isolates known to be associated wi
Table: T123N
Figure: Consensus of each of the three single mutation patterns and wt were aligned with five known variants frequently associated with problems in diagnostic assays and/or escape to vaccine/HBIg therapy: T123N, M133I, M133T, M133V, and T143L, together with M54923 sequence (genotype B/adw) retrieved from GenBank as a reference.
Discussion: Marked changes were also observed in T123N and T143L substitutions, which might be caused by both the shift from slightly small, polar Thr into either larger, more polar Asp or bulkier, non-polar Leu and the importance of their respective locations.
Biological significance of amino acid substitutions in hepatitis B surface antigen (HBsAg) for glycosylation, secretion, antigenicity and immunogenicity of HBsAg and hepatitis B virus replication.
PMID: 19812261
2010
The Journal of general virology
Abstract: Both T123N and K160N substitutions resulted in additional N-glycosylated forms of HBsAg, while the other mutations produced more glycosylated HBsAg compared with the wild type (wt).
Abstract: DNA immunization in BAL
Abstract: Detection of HBsAg by ELISA and immunofluorescence staining indicated that variant HBsAg (vtHBsAg) with K122I was not recognized by HBsAg immunoassays, while vtHBsAg with T123N, A159G, K160N and A159G/K160N had reduced antigenicity.
[Antigenicity of major hydrophilic region II of hepatitis B virus surface antigen].
Abstract: METHODS: Four recombinant plasmids expressing mutant HBsAg (mtHBsAg) P1120T, C121S, K122I and T123N were constructed.
Abstract: The immunoreactivity of the cells expressing mtHBsAg with P1120T, C121S, K122I, T123N and G145R were detected by immunofluorescence (IF) staining and ELISA with 4 antibodies and 7 HBsAg diagnostic kits respectively.
Abstract: mtHBsAg with T123N in lysates was recognized by mAb2, but not recognized in the supernatants.
Differential reactivity of mouse monoclonal anti-HBs antibodies with recombinant mutant HBs antigens.
PMID: 16981270
2006
World journal of gastroenterology
1Abstract: Mutations outside the ""a"" determinant at positions 120 (P-->S), 123(T-->N) and 161 (M-->T) were found to affect reactivity of these mAbs."
"Restoration of replication phenotype of lamivudine-resistant hepatitis B virus mutants by compensatory changes in the ""fingers"" subdomain of the viral polymerase selected as a consequence of mutations in the overlapping S gene."
Abstract: In contrast, the HBV a determinant HBIg/vaccine escape mutants sP120T, sT123N, sG145R, and sD144E/G145R (that produce rtT128N, Q130P, rtW153Q, and rtG153E respectively) yielded as much virus as wild-type HBV while the sM133L (rtY141S) mutant was replication i
Localization of hepatitis B surface antigen epitopes present on variants and specifically recognised by anti-hepatitis B surface antigen monoclonal antibodies.
HBV mutation literature information.
PMID: 
2010
Virology journal
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