Human DRA Functions as a Sulfate Transporter in Sf9 Insect Cells

1998 ◽  
Vol 12 (1) ◽  
pp. 67-74 ◽  
Author(s):  
Mee Kyeong Byeon ◽  
Arthur Frankel ◽  
Takis S. Papas ◽  
Kelly W. Henderson ◽  
Clifford W. Schweinfest
Keyword(s):  
Insect Cells ◽  
Sulfate Transporter ◽  
Sf9 Insect Cells

scholarly journals Expression and Immunogenicity of Two Recombinant Fusion Proteins Comprising Foot-and-Mouth Disease Virus Structural Protein VP1 and DC-SIGN-Binding Glycoproteins

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Xinsheng Liu ◽  
Jianliang Lv ◽  
Yuzhen Fang ◽  
Peng Zhou ◽  
Yanzhen Lu ◽  
...  
Keyword(s):  
Immune Responses ◽  
Disease Virus ◽  
Fusion Proteins ◽  
Insect Cells ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Vp1 Protein ◽  
Sf9 Insect Cells ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Improving vaccine immunogenicity by targeting antigens to dendritic cells has recently emerged as a new design strategy in vaccine development. In this study, the VP1 gene of foot-and-mouth disease virus (FMDV) serotype A was fused with the gene encoding human immunodeficiency virus (HIV) membrane glycoprotein gp120 or C2-V3 domain of hepatitis C virus (HCV) envelope glycoprotein E2, both of which are DC-SIGN-binding glycoproteins. After codon optimization, the VP1 protein and the two recombinant VP1-gp120 and VP1-E2 fusion proteins were expressed in Sf9 insect cells using the insect cell-baculovirus expression system. Western blotting showed that the VP1 protein and two recombinant VP1-gp120 and VP1-E2 fusion proteins were correctly expressed in the Sf9 insect cells and had good reactogenicity. Guinea pigs were then immunized with the purified proteins, and the resulting humoral and cellular immune responses were analyzed. The VP1-gp120 and VP1-E2 fusion proteins induced significantly higher specific anti-FMDV antibody levels than the VP1 protein and stronger cell-mediated immune responses. This study provides a new perspective for the development of novel FMDV subunit vaccines.

scholarly journals Sesquiterpene Lactones from Artemisia absinthium. Biotransformation and Rearrangement of the Insect Antifeedant 3α-hydroxypelenolide

Plants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 891
Author(s):  
Braulio M. Fraga ◽  
Carmen E. Díaz ◽  
María Bailén ◽  
Azucena González-Coloma
Keyword(s):  
Cytotoxic Activity ◽  
Leptinotarsa Decemlineata ◽  
Spodoptera Littoralis ◽  
Culture Medium ◽  
Insect Cells ◽  
Sesquiterpene Lactones ◽  
Enzymatic System ◽  
Artemisia Absinthium ◽  
Sf9 Insect Cells ◽  
New Compounds

Three new compounds, the sesquiterpenes absilactone and hansonlactone and the acetophenone derivative ajenjol, have been isolated from a cultivated variety of Artemisia absinthium. In addition, the major lactone isolated, 3α-hydroxypelenolide, was biotransformed by the fungus Mucor plumbeus affording the corresponding 1β, 10α-epoxide. A cadinane derivative was formed by an acid rearrangement produced in the culture medium, but not by the enzymatic system of the fungus. Furthermore, 3α-hydroxypelenolide showed strong antifeedant effects against Leptinotarsa decemlineata and cytotoxic activity to Sf9 insect cells, while the biotransformed compounds showed antifeedant postingestive effects against Spodoptera littoralis.

Purification of Recombinant p53 from Sf9 Insect Cells

p53 Protocols ◽  
2003 ◽  
pp. 17-28
Author(s):  
Xiu Zhu Sun ◽  
John Nguyen ◽  
Jamil Momand
Keyword(s):  
Insect Cells ◽  
Sf9 Insect Cells

scholarly journals Cold-active extracellular lipase: Expression in Sf9 insect cells, purification, and catalysis

2019 ◽  
Vol 21 ◽  
pp. e00295 ◽  
Author(s):  
Tang Li ◽  
Wenfa Zhang ◽  
Jianhua Hao ◽  
Mi Sun ◽  
Sheng-Xiang Lin
Keyword(s):  
Insect Cells ◽  
Extracellular Lipase ◽  
Sf9 Insect Cells ◽  
Cold Active ◽  
Lipase Expression

Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation

FEBS Letters ◽  
1997 ◽  
Vol 412 (3) ◽  
pp. 559-562 ◽  
Author(s):  
Thorsten Schinke ◽  
Takehiko Koide ◽  
Willi Jahnen-Dechent
Keyword(s):  
Insect Cells ◽  
Apatite Formation ◽  
Sf9 Insect Cells

Pharmacological and structural integrity of muscarinic M2 acetylcholine receptors produced in Sf9 insect cells

1997 ◽  
Vol 333 (2-3) ◽  
pp. 269-278 ◽  
Author(s):  
Claire Weill ◽  
François Autelitano ◽  
Chantal Guenet ◽  
Freddy Heitz ◽  
Maurice Goeldner ◽  
...  
Keyword(s):  
Acetylcholine Receptors ◽  
Structural Integrity ◽  
Insect Cells ◽  
Sf9 Insect Cells

scholarly journals Functional expression of a human thrombin receptor in Sf9 insect cells: evidence for an active tethered ligand

1996 ◽  
Vol 314 (2) ◽  
pp. 603-611 ◽  
Author(s):  
Xilin CHEN ◽  
Karen EARLEY ◽  
Weiping LUO ◽  
Sue-Hwa LIN ◽  
William P. SCHILLING
Keyword(s):  
Insect Cells ◽  
Recombinant Baculovirus ◽  
Sustained Response ◽  
Thrombin Receptor ◽  
Sf9 Cells ◽  
Thrombin Receptors ◽  
Sf9 Insect Cells ◽  
Human Thrombin ◽  
Hel Cells ◽  
Tethered Ligand

Desensitization of recombinant human thrombin receptors expressed in Sf9 insect cells was compared with native thrombin receptors in megakaryoblast erythroleukaemia (HEL) cells. Addition of thrombin (2 units/ml) or agonist peptide SFLLRN (10 μM) to HEL cells, or to Sf9 cells infected with recombinant baculovirus containing the thrombin receptor cDNA, produced an increase in the free cytosolic Ca2+ concentration ([Ca2+]i) as measured by fura-2. The response in HEL cells was transient, reflecting a rapid homologous desensitization. In contrast, [Ca2+]i in Sf9 cells expressing the thrombin receptor increased rapidly to a peak value that slowly declined, but remained elevated for at least 12 min following stimulation by thrombin. The sustained [Ca2+]i response to thrombin was not reversed by washout of thrombin or by subsequent addition of hirudin. Pretreatment of Sf9 cells with either thrombin (2 units/ml) or SFLLRN (10 or 50 μM) for 5 min produced a shift in the ED50 for SFLLRN (added 10 min after washout) from 0.4 μM to 20 and 7 μM, respectively. Thus, desensitization of thrombin receptors expressed in Sf9 cells occurs slowly and reflects a decrease in receptor affinity. The sustained [Ca2+]i response in Sf9 cells stimulated by thrombin may reflect continuous activation by the tethered ligand. To test this hypothesis, the effect of protease treatment during the sustained phase of the response was examined. Addition of either aminopeptidase M or thermolysin reversed the sustained response to SFLLRN, but only thermolysin reversed the sustained response to thrombin. Thermolysin had no effect on the change in [Ca2+]i observed following carbachol stimulation of Sf9 cells expressing the M5 muscarinic receptor. Furthermore, following thermolysin treatment, the cells remained responsive to a subsequent application of SFLLRN. These results demonstrate that the tethered ligand remains active for extended periods of time after thrombin stimulation and suggests that further hydrolysis by extracellular proteases may represent an important mechanism of rapid receptor deactivation.

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