Discussion: And the difference in viral replication capacity of pHBV4.1-HBs(wt), pHBV4.1-HBs(sW172L) and pHBV4.1-HBs(sW172*) should be an important cause of different expression of Smad3/2 and CREB in present study.
Discussion: Though the changes of key molecules in LEF/Wnt pathway and proteinase C (PKC)-dependent c-Raf-1/Erk2 pathway were not significant than key molecules in TGF-beta/Smad pathway, we coul
Discussion: Thus, the transcriptional activation of truncated mutant HBsAg may be related to the increased possibility of tumorigenesis in HBV-rtA181T/sW172* mutant.
Hepatitis B virus rtA181T/sW172non-stop mutation may increase resistance fold to adefovir- and entecavir-resistant mutants compared to rtA181T/sW172* mutation.
Abstract: 3.69-fold in half maximal effective concentration of wild-type strain); rtA181T/sW172L + rtS202G + rtM204V strain exhibited higher HBV DNA production and entecavir resistance fold than that of rtA181T/sW172* + rtS202G + rtM204V strain (50.98% vs.
Abstract: In conclusion, rtA181T/sW172non-stop mutation may increase res
Naturally occurring hepatitis B virus reverse transcriptase mutations related to potential antiviral drug resistance and liver disease progression.
PMID: 29713126
2018
World journal of gastroenterology
Method: The mutations rtA181T/V, rtM204I, and rtM204V also cause the simultaneous HBsAg mutations, sW172 stop, sW196S/L/Stop, and sI195M, respectively (Table 1).
Antiviral efficacy of entecavir for hepatitis B virus rtA181V/T mutants.
Result: After emergence of mutant, the serum HBV DNA, HBsAg and ALT levels did not differ significantly between the rtA181T/sW172* mutation group and other missense mutations group (4.16 versus 3.61 log10 IU/mL; P = 0.298, 3.52 versus 3.46 log10 IU/mL; P = 0.795, 142.5 versus 59.0 U/L; P = 0.524, respectively).
Result: The
Discussion: They found the serum levels of HBV DNA and HBsAg in pHBV-rtA181T/sW172* injected mice were significantly lower than that of pHBV-rtA181T/sW172L injected mice.
Small surface antigen variants of HBV associated with responses to telbivudine treatment in chronic hepatitis B patients.
Abstract: CONCLUSIONS: Our findings suggest that the decrease in viral population heterogeneity at an early stage of LdT treatment was associated with the subsequent optimal virological response, and the early appearance of some specific mutations, such as sG44E, sW172* and sW182*, is a potential indicator of a partial virological response in continuing therapy.
Abstract: RESULTS: Sequencing results revealed different dynamics of non-synonymous mutations, such as sL9P, sN40S, sG44E, sW172*, PMID: 27871021
2017
Virology
Abstract: Cell lines were transfected with infectious HBV clones encoding surface stop codons rtM204I/sW196*, rtA181T/sW172*, rtV191I/sW182*, and a panel of substitutions in the surface proteins.
Sequence analysis and functional characterization of full-length hepatitis B virus genomes from Korean cirrhotic patients with or without liver cancer.
Discussion: In our case, the sW172* mutation was silent at the P protein level and hence not selected by antiviral therapy.
Discussion: More distal nonsense mutations in the S region include W172*, W182*, W201*, and L209*.
Discussion: The W172* mutation is associated with resistance to nucleos(t)ide analogues and secondary to substitution in the reverse trancriptase (RT) domain of the P protein (rtA181T/ sW172*).
Occult hepatitis B virus infection in HIV positive patients at a tertiary healthcare unit in eastern India.
Result: Other diagnostic escape mutations found in the surface ORF were sR122K (5.9%), sG145A (5.9%), and sW172* (5.9%).
Table: W172stop
Discussion: Further sequence analysis revealed other mutations such as sR122K, sG145A andsW172* within the surface ORF of the OBI subjects (mainly belonging to HBV/D1 and D3) but at low frequencies.
Characterization of hepatitis B virus in Amerindian children and mothers from Amazonas State, Colombia.
Discussion: Similar mutations induced by antiviral treatment resulting in a truncated protein have been reported in other studies, such as W196* (31 amino acid deletion) and W172* (55 amino acid deletion).
Effects of amino acid substitutions in hepatitis B virus surface protein on virion secretion, antigenicity, HBsAg and viral DNA.
Introduction: reported that the rtA181T/sW172stop (sW172*) variant had a secretory defect and exerted a dominant negative effect on wild-type (WT) HBV virion secretion.
Discussion: This possibility is supported by experimental evidence from several previous reports showing that the mutant virion secretion could be rescued efficiently (i.e., sP127S) or moderately (i.e., sW172*) by co-expression of WT surface protein.
HBV mutation literature information.
PMID: 
2018
Virology journal
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