scholarly journals PURIFICATION OF RECOMBINANT PRES2-S PROTEIN, THE SURFACE ANTIGEN OF HUMAN HEPATITIS B VIRUS (HBV) EXPRESSED IN BOMBYX MORI LARVAE

2019 ◽  
pp. 7-10
Author(s):  
J. Abdurakhmanov ◽  
S. Sasmakov ◽  
O. Ashirov ◽  
S. Khasanov ◽  
F. Eshboev ◽  
...  
Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 967
Author(s):  
Qianru Wang ◽  
Shuwen Fu ◽  
Jing Zhang ◽  
Quan Yuan ◽  
Jisu Li ◽  
...  

Hepatitis B surface antigen (HBsAg) promotes persistent hepatitis B virus (HBV) infection. It primarily corresponds to small (S) envelope protein secreted as subviral particles. We previously found that genotype D clones expressed less S protein than genotype A clones but showed higher extracellular/intracellular ratio of HBsAg suggesting more efficient secretion. The current study aimed to characterize the underlying mechanism(s) by comparing a subgenotype A2 clone (geno5.4) with a subgenotype D2 clone (geno1.2). Five types of full-length or subgenomic constructs were transfected to Huh7 cells at different dosage. HBsAg was quantified by enzyme linked immunosorbent assay while envelope proteins were detected by Western blot. We found that ratio of extracellular/intracellular HBsAg decreased at increasing amounts of DNA transfected. Conflicting findings from two types of subgenomic construct confirmed stronger secretion inhibitory effect of the genotype D-derived large envelope protein. Chimeric constructs followed by site-directed mutagenesis revealed geno1.2 specific V118/T127 and F161/A168 in the S protein as promoting and inhibitory of HBsAg secretion, respectively. In conclusion, more efficient HBsAg secretion by subgenotype D2 than subgenotype A2 is attributed to lower level of S protein expression in addition to V118 and T127 in S protein, although its F161 and A168 sequences rather reduce HBsAg secretion.


2011 ◽  
Vol 19 (2) ◽  
pp. 120-127 ◽  
Author(s):  
Jung Sun Yum ◽  
Byung Cheol Ahn ◽  
Hyun Jin Jo ◽  
Dong Yeon Kim ◽  
Ki Hyun Kim ◽  
...  

ABSTRACTA hepatitis B virus (HBV) vaccine has been developed using a new adjuvant and HBV surface antigens produced from a CHO cell line. The purified HBV surface antigens are composed of L protein, M protein, and S protein in a mixture of 20- and 40-nm-diameter particles and filamentous forms. This HBV surface antigen, formulated with L-pampo, a proprietary adjuvant, induced 10 times more antibody than the same antigen with alum and was capable of inducing strong immune responses in three different HBV transgenic mice. In spite of the presence of a large amount of HBV antigen in the blood, no antibody against HBV surface antigen was normally detected in these transgenic mice. After immunization, the HBV antigen was also cleared from the blood.


2014 ◽  
Vol 14 (5) ◽  
pp. 3348-3355 ◽  
Author(s):  
Ningning Ma ◽  
Chao Ma ◽  
Nianyue Wang ◽  
Chuanyan Li ◽  
Sauli Elingarami ◽  
...  

1995 ◽  
Vol 76 (2) ◽  
pp. 301-308 ◽  
Author(s):  
I. Rodriguez-Crespo ◽  
E. Nunez ◽  
J. Gomez-Gutierrez ◽  
B. Yelamos ◽  
J. P. Albar ◽  
...  

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