作者: Tania Pal Choudhury , Lalita Gupta , Sanjeev Kumar
DOI: 10.1016/J.ACTATROPICA.2018.10.008
关键词: Anopheles stephensi 、 Innate immune system 、 Amino acid 、 Integrin binding 、 Heme binding 、 Peroxidase 、 Gene 、 Chemistry 、 Binding site 、 Biochemistry
摘要: Peroxidases catalyze the reduction of peroxides and that, in turn, oxidize various substrates. They have been widely reported to play an important role mosquito innate immunity against pathogens. Here, we characterized double heme peroxidase (AsDBLOX) gene from Indian malaria vector Anopheles stephensi. It is a true ortholog An. gambiae DBLOX. This 4209 bp AsDBLOX encodes for protein 1402 amino acids that has two duplicated domains, domain I (from acid 61 527) II 714 1252). The first only substrate binding sites lacks all other motifs functional (e.g. site, calcium site homodimer interface). Instead, it integrin motifs-LDV (Leu-Asp-Val) RGD (Arg-Gly-Asp). second domain, however, features complete along with motif LDI (Leu-Asp-Ile). Thus, unique type peroxinectin as these groups proteins are by domain. We also observed expressed life cycle stages highly induced pupal stage development which indicates its possible development.