Respiratory syncytial virus envelope glycoprotein (G) has a novel structure

Respiratory syncytial virus envelope glycoprotein (G) has a novel structure.

Amino acid sequence of human respiratory syncytial virus envelope glycoprotein (G) was deduced from the DNA sequence of a recombinant plasmid and confirmed by limited amino acid microsequencing of purified 90K G protein. The calculated molecular mass of the protein encoded by the only long open reading frame of 298 amino acids was 32,588 daltons and was somewhat smaller than the 36K polypeptide...

Antigenic structure of human respiratory syncytial virus fusion glycoprotein.

New series of escape mutants of human respiratory syncytial virus were prepared with monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes, and previously identified antigenic si...

After Respiratory Syncytial Virus Challenge Virus G Glycoprotein-Induced Eosinophilia IL-13 Is Sufficient for Respiratory Syncytial

Virus Attachment Glycoprotein G Domain for Human Respiratory Syncytial Identification of a Linear Heparin Binding

Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G.

Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract disease in infants and young children worldwide. Infection is mediated, in part, by an initial interaction between attachment protein (G) and a highly sulfated heparin-like glycosaminoglycan (Gag) located on the cell surface. Synthetic overlapping peptides derived from consensus sequences of the G protein ectodoma...