Development of a pilot-scale production process and characterization of a recombinant Japanese encephalitis virus envelope domain III protein expressed in Escherichia coli

2012 ◽  
Vol 95 (5) ◽  
pp. 1179-1189 ◽  
Author(s):  
Nagesh K. Tripathi ◽  
Ambuj Shrivastava ◽  
Karttik C. Biswal ◽  
P. V. Lakshmana Rao
Keyword(s):  
Escherichia Coli ◽  
Production Process ◽  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Pilot Scale ◽  
Scale Production ◽  
Virus Envelope ◽  
Pilot Scale Production ◽  
Domain Iii

Characterization of Japanese encephalitis virus envelope protein expressed by recombinant baculoviruses

Virology ◽  
1989 ◽  
Vol 173 (2) ◽  
pp. 674-682 ◽  
Author(s):  
Yoshiharu Matsuura ◽  
Michiko Miyamoto ◽  
Takanori Sato ◽  
Chiharu Morita ◽  
Kotaro Yasui
Keyword(s):  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Envelope Protein ◽  
Encephalitis Virus ◽  
Recombinant Baculoviruses ◽  
Virus Envelope ◽  
Virus Envelope Protein

Pilot-scale production and purification of a staphylokinase-based fusion protein over-expressed in Escherichia coli

2008 ◽  
Vol 4 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Genshen Zhong ◽  
Aiping Yu ◽  
Bingxing Shi ◽  
Yang Liu ◽  
Chutse Wu
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Pilot Scale ◽  
Scale Production ◽  
Pilot Scale Production

Pilot-scale production process for high internal phase emulsions: Experimentation and modeling

2016 ◽  
Vol 148 ◽  
pp. 32-43 ◽  
Author(s):  
Arend Dubbelboer ◽  
Jo J.M. Janssen ◽  
Hans Hoogland ◽  
Edwin Zondervan ◽  
Jan Meuldijk
Keyword(s):  
Production Process ◽  
Pilot Scale ◽  
Scale Production ◽  
Internal Phase ◽  
Pilot Scale Production

Pilot-scale Production of Recombinant LeIBP from Arctic Yeast Glaciozyma sp. by Escherichia coli

KSBB Journal ◽  
2017 ◽  
Vol 32 (4) ◽  
pp. 300-305 ◽  
Author(s):  
Eun Jae Kim ◽  
Jun Hyuck Lee ◽  
Sung Gu Lee ◽  
Se Jong Han
Keyword(s):  
Escherichia Coli ◽  
Pilot Scale ◽  
Scale Production ◽  
Pilot Scale Production

Pilot-scale production and characterization of PEGylated human FGF-21 analog

2016 ◽  
Vol 228 ◽  
pp. 8-17 ◽  
Author(s):  
Xianlong Ye ◽  
Jianying Qi ◽  
Dan Yu ◽  
Shujie Li ◽  
Qiang Wu ◽  
...  
Keyword(s):  
Pilot Scale ◽  
Scale Production ◽  
Pilot Scale Production

scholarly journals Mutation analysis of the cross-reactive epitopes of Japanese encephalitis virus envelope glycoprotein

2012 ◽  
Vol 93 (6) ◽  
pp. 1185-1192 ◽  
Author(s):  
Shyan-Song Chiou ◽  
Yi-Chin Fan ◽  
Wayne D. Crill ◽  
Ruey-Yi Chang ◽  
Gwong-Jen J. Chang
Keyword(s):  
Amino Acid ◽  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Recombinant Expression ◽  
Encephalitis Virus ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Virus Envelope ◽  
E Protein ◽  
Domain Iii

Group and serocomplex cross-reactive epitopes have been identified in the envelope (E) protein of several flaviviruses and have proven critical in vaccine and diagnostic antigen development. Here, we performed site-directed mutagenesis across the E gene of a recombinant expression plasmid that encodes the Japanese encephalitis virus (JEV) premembrane (prM) and E proteins and produces JEV virus-like particles (VLPs). Mutations were introduced at I135 and E138 in domain I; W101, G104, G106 and L107 in domain II; and T305, E306, K312, A315, S329, S331, G332 and D389 in domain III. None of the mutant JEV VLPs demonstrated reduced activity to the five JEV type-specific mAbs tested. Substitutions at W101, especially W101G, reduced reactivity dramatically with all of the flavivirus group cross-reactive mAbs. The group and JEV serocomplex cross-reactive mAbs examined recognized five and six different overlapping epitopes, respectively. Among five group cross-reactive epitopes, amino acids located in domains I, II and III were involved in one, five and three epitopes, respectively. Recognition by six JEV serocomplex cross-reactive mAbs was reduced by amino acid substitutions in domains II and III. These results suggest that amino acid residues located in the fusion loop of E domain II are the most critical for recognition by group cross-reactive mAbs, followed by residues of domains III and I. The amino acid residues of both domains II and III of the E protein were shown to be important in the binding of JEV serocomplex cross-reactive mAbs.

Sign in / Sign up

Export Citation Format

Share Document