A Hyper-Glycosylation of HBV Surface Antigen Correlates with HBsAg-Negativity at Immunosuppression-Driven HBV Reactivation in Vivo and Hinders HBsAg Recognition in Vitro.
Abstract: These NLGSs are located in the major hydrophilic region of HBsAg (known to be the target of antibodies) and resulted from the single mutation T115N, T117N, T123N, N114ins, and from the triple mutant S113N+T131N+M133T.
Method: The following mutations associated with additional N-linked glycosylation sites were identified: 114N-ins, T115N, T117N, T123N, S113N+T131N+M133T.
Method: The newly identified mutations associated with additional N-linked glycosylation sites (114N-ins,
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.
Method: Mutations creating novel N-linked glycosylation, such as 112NG113, 114NT115, T115N, and G130N, were introduced to the 0.7mer construct by ClonExpress MultiS kit (Vazyme, China).
Result: To characterize their biological properties, we generated 0.7mer expression construct containing T115N, G130N, 112NG113 (insertion of the NG dipeptide between residues 112 and 113.
Result: with the 0.7mer construct harboring both G145R and T115N mutations, for example).
Discussion: In the current work we also performed limited study on four additional mutants creating novel N-linked glycosylation sites: T115N, G130N, 112NG113, and 114NT115.
HBV mutation literature information.
PMID: 
2022
PloS one
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