Anti-Rotavirus [Clone RV6-25] — Purified No Carrier Protein - 1.0 mg

Primary Monoclonal Antibodies>Infectious Diseases|Monoclonal Antibodies|Recombinant Antibodies

Standard Overnight on Blue Ice.

Rotaviruses (RV) are double-stranded, non-enveloped, icosahedral RNA viruses in the Reoviridae family1 that cause severe dehydrating diarrhea in infants and children2. RV particles are composed of concentric viral protein (VP) layers3. The triple-layered particle has an inner capsid layer (VP2), an intermediate capsid layer (VP6), and an outer capsid layer (VP7, VP4). The transcriptionally active double-layered particle (DLP) consists of VP2 and VP6. VP6 is the most antigenic RV protein in humans4.Rotaviruses (RV) are double-stranded, non-enveloped, icosahedral RNA viruses in the Reoviridae family1 that cause severe dehydrating diarrhea in infants and children2. RV particles are composed of concentric viral protein (VP) layers3. The triple-layered particle has an inner capsid layer (VP2), an intermediate capsid layer (VP6), and an outer capsid layer (VP7, VP4). The transcriptionally active double-layered particle (DLP) consists of VP2 and VP6. VP6 is the most antigenic RV protein in humans4.RV6-25 was generated from RV-specific IgD- B cells isolated from the blood of a healthy immune donor5, 6 and exhibits moderate affinity5. Mutations that alter residues in the HCDR2 loop exhibit lower affinity than wildtype but result in limited changes in binding kinetics5. RV6-25 and RV6-26 are encoded by the same heavy chain variable segment6, but unlike RV6-26, RV6-25 is unable to inhibit RV5. Three-dimensional structural analyses of DLP:Fab complexes show that RV6-25 Fab molecules attach to the tops of VP6 trimers, at one VP6 subunit, with the epitope positioned along the edge and in close contact with the VP6 surface loop5. The RV6-25 Fab protrudes from the VP6 trimers and extends away from the viral surface in a regular pattern depending on the position of the VP6 trimer in the VP6 layer1. Additionally, RV6-25 binds to the apical surface of the DLP VP6 head domain and does not obstruct the transcription pore1. The Fab binds to epitopes on the distinct P, P′, T, T′, or D VP6 trimers. Combined DXMS and cryo-EM data show that the epitope is within two apical loops of the VP6 structure and that residues 197 to 214 and 308 to 316 in the loops between βB-βC and the short αA helix and βI are directly involved binding.

≥1.0 mg/ml

VP6 is a viral protein in the intermediate capsid layer of RV.

Anti-Rotavirus, RV6-25