The human respiratory syncytial virus (Long strain) fusion protein contains six potential N-glycosylation sites: N27, N70, N116, N120, N126, and N500. Site-directed mutagenesis of these positions revealed that the mature fusion protein contains ...

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Aug 14, 2018 · The RSV F glycosylation mutants were obtained by changing the asparagine (N) codons (AAT/AAC) at position N27, N70, N116, N126 or N500 into a glutamine (Q) codon (CAA/CAG). A triple and penta mutant F protein was developed by replacing 3 asparagine codons (N27/70/500) and all 5 conserved N codons into Q codons (N27/70/116/126/500), respectively.

Site-directed mutagenesis of these positions revealed that the mature fusion protein contains three N-linked oligosaccharides, attached to N27, N70, and N500. By intro-ducing these mutations into the F gene in different combinations, four more mutants were generated.

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N27-A cells exhibit higher sensitivity to neurotoxins as compared to parental N27 cells, and release dopamine under both basal and depolarization conditions. These features make the N27-A cell line an improved model for Parkinson′s disease research.

The N27A cell line is a clonal derivative of the parental N27 cell - line selected for high expression of dopaminergic neural markers. The parental cell line was originally isolated from dopaminergic

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