Anti-Respiratory Syncytial Virus (Clone: RSV-17E10) Biotin

Specificity: RSV-17E10 activity is directed against antigenic site IV of the RSV and hMPV fusion (F) proteins and binds to pre- and post-fusion F proteins of RSV A strain A2 and RSV B strain 18537. Antibody RSV-17E10 is also capable of neutralizing RSV A2, RSV Long viruses (subgroup A), RSV 18537 B, and RSV WV/401R viruses (subgroup B) . Competition-binding assay shows that RSV-17E10 targets antigenic site IV. The mode of action is independent of R429. RSV-17E10 is cross-reactive with hMPV F at antigenic site IV and neutralizes hMPV better than RSV. Cross-neutralization of RSV and hMPV is associated with recognition of the G430 and I432 residues, which are shared between RSV and hMPV F proteins. RSV-17E10 binds at a unique ~56? tilt, which may be a determinant of cross-reactivity with hMPV F. Antigen Distribution: F protein is a surface glycoprotein. Background: Respiratory syncytial virus (RSV) is a common respiratory virus that infects the majority of children by two years old1, 2. While usually mild, RSV can be serious in infants and older adults and is the leading cause of bronchiolitis and pneumonia in children less than one year of age in the United States1. A related pneumovirus, human metapneumovirus (hMPV), also significantly contributes to hospitalizations resulting from lower respiratory tract infection2. Antibodies have been described that bind and neutralize both RSV and hMPV fusion (F) proteins. RSV F protein is a type I integral membrane protein that is synthesized as a 574 amino acid inactive precursor, assembled into a trimer, post-translationally modified, then cleaved to produce F1, F2, and intervening peptide pep273. Functional F protein has both pre- and post-fusion conformations. RSV F protein is highly conserved among RSV isolates from both A and B subgroups3 and is the primary target for antiviral drug development3 with several antigenic regions capable of introducing neutralizing antibodies2. RSV and hMPV F protein share ~36% sequence similarity. Human monoclonal antibody (mAb) RSV-17E10 was generated against post-fusion RSV F using human hybridoma technology2. RSV-17E10 binds to pre- and post-fusion F proteins of RSV A strain A2 and RSV B strain 18537 and is capable of neutralizing RSV A2, RSV Long viruses (subgroup A), RSV 18537 B, and RSV WV/401R viruses (subgroup B) . Competition-binding assay shows that RSV-17E10 targets antigenic site IV. The mode of action is independent of R429. RSV-17E10 is cross-reactive with hMPV F at antigenic site IV and neutralizes hMPV better than RSV. Cross-neutralization of RSV and hMPV is associated with recognition of the G430 and I432 residues, which are shared between RSV and hMPV F proteins. RSV-17E10 binds at a unique ~56o tilt, which may be a determinant of cross-reactivity with hMPV F.