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Isolation and production of highly specific protein-based binding molecules are crucial to the ever expanding diagnostics, therapeutics and protein array fields. Traditionally, such reagents have been sourced from vertebrate immune systems, where antibodies have evolved over millennia into highly effective molecules of immune surveillance capable of targeting a huge range of targets in response to infection and disease. Now, a growing number of alternative protein scaffolds are being investigated as specific binding molecules incorporating a diverse and powerful range of binding and recognition interfaces. These are being sourced from human proteins, from alternative immune molecules present in evolutionarily old vertebrates, and from highly evolved binding proteins in prokaryotic systems.

Segment 10 genes from a short (RV-5, serotype G2) and a supershort (B37, a new G serotype) strain were cloned and their sequences compared to the (corresponding) segment 11 sequences of Wa, SA11, and UK rotaviruses. The determined nucleotide sequences were 817 (RV-5) and 947 (B37) bases in length and showed extensively conserved 5' noncoding and protein coding regions. The major open reading frame codes for a protein of 200 (RV-5) or 198 (B37) amino acids, and the newly proposed second open reading frame can code for a protein of 92 amino acids. Compared to long strain gene segments, the base sequences of the short and supershort strains were found to contain extended, AT-rich 3' noncoding regions which were not significantly homologous to each other, to other parts of the VP9 gene, or to other rotavirus genes that have been sequenced. The function(s) of these 3' regions is not apparent.