scholarly journals Two-Component Nanoparticle Vaccine Displaying Glycosylated Spike S1 Domain Induces Neutralizing Antibody Response against SARS-CoV-2 Variants

mBio ◽  
2021 ◽  
Author(s):  
Linda van Oosten ◽  
Jort J. Altenburg ◽  
Cyrielle Fougeroux ◽  
Corinne Geertsema ◽  
Fred van den End ◽  
...  
Keyword(s):  
Low Cost ◽  
Expression System ◽  
Neutralizing Antibody ◽  
System A ◽  
Virus Like Particle ◽  
Production Platform ◽  
Two Component ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression

Vaccines pave the way out of the SARS-CoV-2 pandemic. We have developed a virus-like particle (VLP)-based vaccine using the baculovirus-insect cell expression system, a robust production platform known for its scalability, low cost, and safety. Baculoviruses were constructed encoding SARS-CoV-2 spike proteins: full-length S, stabilized secreted S, or the S1 domain. This two-component nanoparticle vaccine can now be further developed to help alleviate the burden of COVID-19.

Modulating the Expression Strength of the Baculovirus/Insect Cell Expression System: A Toolbox Applied to the Human Tumor Suppressor SMARCB1/SNF5

2018 ◽  
Vol 60 (11) ◽  
pp. 820-832 ◽  
Author(s):  
Monika M. Golas ◽  
Sakthidasan Jayaprakash ◽  
Le T. M. Le ◽  
Zongpei Zhao ◽  
Violeta Heras Huertas ◽  
...  
Keyword(s):  
Tumor Suppressor ◽  
Insect Cell ◽  
Expression System ◽  
Human Tumor ◽  
System A ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression ◽  
Cell Expression System

Protein production using the baculovirus-insect cell expression system

2013 ◽  
Vol 30 (1) ◽  
pp. 1-18 ◽  
Author(s):  
A. Contreras-Gómez ◽  
A. Sánchez-Mirón ◽  
F. García-Camacho ◽  
E. Molina-Grima ◽  
Y. Chisti
Keyword(s):  
Insect Cell ◽  
Protein Production ◽  
Expression System ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression ◽  
Cell Expression System

Activation of recombinant trp by thapsigargin in Sf9 insect cells

1994 ◽  
Vol 267 (5) ◽  
pp. C1501-C1505 ◽  
Author(s):  
L. Vaca ◽  
W. G. Sinkins ◽  
Y. Hu ◽  
D. L. Kunze ◽  
W. P. Schilling
Keyword(s):  
Expression System ◽  
Cation Selectivity ◽  
Drosophila Protein ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression ◽  
Mammalian Protein ◽  
Entry Mechanism ◽  
Proline Rich Region ◽  
Cell Expression System

The mammalian protein responsible for Ca2+ release-activated current (Icrac) may be homologous to the Drosophila protein designated trp. Thus the activity of trp, and another Drosophila protein designated trp-like or trpl, may be linked to depletion of the internal Ca2+ store via the so-called capacitative Ca2+ entry mechanism. To test this hypothesis, the effect of thapsigargin, a selective inhibitor of the endoplasmic reticulum Ca2+ pump, on trp- and trpl-induced whole cell membrane current was determined using the baculovirus Sf9 insect cell expression system. The results demonstrate that trp and trpl form Ca(2+)-permeable cation channels. The trpl encodes a nonselective cation channel that is constitutively active under basal nonstimulated conditions and is unaffected by thapsigargin, whereas trp is more selective for Ca2+ than Na+ and is activated by depletion of the internal Ca2+ store. Although evaluation of cation selectivity suggests that trp is not identical to the channel responsible for Icrac, these channels must share some structural feature(s) since both are activated by thapsigargin. A unique proline-rich region in the COOH-terminal tail of trp, which is absent in trpl, may be necessary for capacitative Ca2+ entry.

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