Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT01586 (G418)
 2,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We constructed a retroviral vector, pLhIL-9RSN, containing CDNA encoding the human interleukin-9 receptor (IL-9R) along with a neomycin phosphotransferase gene (Neo). In order to study the biological effects of the IL-9R, high titer (1-5 x 10(5) CFU/ml) viral supernatant, generated from the packaging cell lines, ecotropic GPE86 and amphotropic PA317, was used to transduce the IL-9R gene into sorted populations of CD34++ CD33-cells from human cord blood which are highly enriched for erythroid progenitor cells (BFU-E). Colony formation by BFU-E transduced with the IL-9R gene and grown without selection in G418 and in the presence of erythropoietin (Epo) and interleukin (IL)-9 was significantly increased up to three-fold and the size of the erythroid colonies was significantly increased 50-100% compared to colony formation by mock virus transduced cells. Moreover, colony formation by IL-9R-transduced cells was more sensitive to stimulation with lower doses of IL-9 and Epo. Individual colonies formed with or without selection in G418 were evaluated. Proviral integration and mRNA expression were respectively assessed by polymerase chain reaction (PCR) and reverse transcriptase (RT) PCR analysis and were apparent in 93% and 84% of the G418-resistant colonies and 52% and 48% of the colonies grown in the absence of G418. Our study demonstrates that a functional human IL-9R gene can be efficiently transduced into human cord blood hematopoietic progenitors using retroviral vectors with increased cytokine-dependent erythroid colony formation.
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PMID:Transduction of human interleukin-9 receptor gene into human cord blood erythroid progenitors increases the number of erythropoietin-dependent erythroid colonies. 897 79

Rabies virus glycoprotein is a type I transmembrane protein exposed on the surface on the mature virus particle that induces virus neutralizing antibodies. In the present study, 60 amino acid C-terminal hydrophobic anchor (transmembrane) and cytoplasmic domains of glycoprotein were deleted from full-length glycoprotein and fused with polyhistidine tag. The N-terminal viral signal peptide was also replaced with CD33 signal peptide for efficient secretion in mammalian cells. Following transfection of Madin Darby bovine kidney (MDBK) cells with plasmid encoding this soluble form of glycoprotein, polyclonal populations of stably transfected resistant cells were obtained after G418 selection. The protein was expressed as a glycosylated protein and secreted outside the cells utilizing N-terminal CD33 signal peptide. The secreted soluble glycoprotein was purified from cell culture supernatant by Ni--agarose affinity chromatography utilizing C-terminal polyhistidine tag. Like full-length glycoprotein, the expressed recombinant soluble glycoprotein was found to be immunogenic when injected in rabbits. In this study, we have assessed the potential of recombinant soluble glycoprotein as diagnostic antigen in ELISA and found that this recombinant protein can be used as diagnostic antigen in ELISA for detecting anti-glycoprotein antibodies in immunized host.
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PMID:Immunogenic and antigenic properties of recombinant soluble glycoprotein of rabies virus. 1591 70