Anti-Rotavirus (Clone: RV6-26) (LT581-GRP)

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. RV6-26 was generated from RV-specific IgD- B cells isolated from the blood of a healthy immune donor5,6 and exhibits high affinity that is mediated primarily by somatic mutations in the HCDR2 region5. Mutations that alter residues in or near the HCDR2 loop exhibit lower binding affinity than wildtype5. Three-dimensional structural analyses of DLP:Fab complexes show that RV6-26 Fab molecules occupy Type I, II, and III channels5,7. The Fabs are centered inside each of the 132 channels that penetrate the VP6 layer5, bind at both the 5- and 6-fold points of symmetry7, completely block the Type I channel7, but do not make contact with the VP6 subunits surrounding the channels5,7. Two separate regions of the VP6 trimer are recognized within a β-sheet that lies on the exposed side of VP6, part of which is exposed inside the transcriptional pore7. The epitope region requires a quaternary structure that forms a continuous surface of two protomers of the same VP6 trimer7.