INSILCO CHARACTERIZATION OF NOVEL PH20 HYALURONIDASE PROTEIN SEQUENCES OF MURRAH BULLS (Bubalus bubalis)

Abstract

PH20 hyaluronidase proteins are members of Zona Pellucida Binding Protein family. PH20 hyaluronidase is bifunctional i.e. have hyaluronidase as well as sperm-zona binding activity reportedly. In this study, we performed in silico characterization of novel PH20 protein using partial nucleotide sequences obtained from SNP genotyping of Bubalus bubalis bulls by Sanger dideoxy sequencing method. Possible glycosylation and mannosylation patterns were also predicted in both the PH20 hyaluronidase sequences which may be responsible for its hyaluronidase activity. Further, the potential tertiary structure of PH20 was deduced using Swiss-Model server. The tertiary structure models of PH20 were validated by ProSA server and ramachandran plots. These structural models were assigned PMDB identifiers PM0080458 and PM0080459. Physicochemical characterization revealed that B. bubalis PH20 hyaluronidase are more thermostable and more hydrophobic than that of the cattle PH20 hyaluronidase. The functional annotations were further inferred using gene oOntology based predictions. Present work on structural elucidation of PH20 predicts a reference model for functional genomics studies related to multifunctionality of PH20 hyaluronidase proteins in other species.