Anti-Respiratory Syncytial Virus (Clone: RSV-3M3) Biotin

Specificity: RSV-3M3 activity is directed against antigenic site IV of the RSV fusion (F) protein and binds to pre- and post-fusion F proteins of RSV A strain A2 and RSV B strain 18537. Clone RSV-3M3 is potent at neutralizing RSV A2, RSV Long viruses (subgroup A), RSV 18537 B, and RSV WV/401R viruses (subgroup B) . Competition-binding assay shows that RSV-3M3 targets antigenic site IV. Mutagenesis experiments have revealed RSV-3M3 requires arginine residue R429 for binding and neutralization. EM reconstruction shows that RSV-3M3 binds close to a 0? tilt. RSV-3M3 does not neutralize hMPV. 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.