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Paralytic peptide binding proteins (PP-BP) are 30KP proteins that show similarity to ENFbinding proteins. The ENF-BP act as active regulators of ENF peptides. ENF peptides aremultifunctional insect cytokines. The comparison of gene expression in diapause inducedand non-diapause eggs at different time intervals after oviposition showed an upregulation ofPP at 18h as well as PP-BP at 12 and 18h after oviposition along with few other genes. Thecurrent study has been taken up to investigate the role of PP as well as PP-BP in diapauseinduction in polyvoltine silkworms and to study the multigene organization of PP-BP in theBombyx mori genome. The tissue specific expression analysis revealed that, PP-BP is highlyexpressed in fat body followed by egg and brain while no expression was observed in midgut. The expression levels of PP and PP-BP in diapause and non-diapause eggs from 0h to48h after oviposition, validated through realtime PCR revealed that PP is highly expressed at18 and 24h while PP-BP expression is higher at 12 and 18h time intervals suggesting theirpossible role in diapause induction. The whole genome survey of the PP-BP paralogous sequencesrevealed a total of 46 B. mori PP-BP homologs that are classified into 3 categoriesviz., ENF-BP, Typical 30KPs and serine/threonine rich 30KPs. These paralogous sequencesare distributed on chromosomes 7, 20, 22 and 24, all 30KP and S/T rich 30KP proteins arepresent in the same locus of chromosome 20.

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