Structure of Aedes aegypti procarboxypeptidase B1 and its binding with Dengue virus for controlling infection.

ABSTRACT: Metallocarboxypeptidases play critical roles in the development of mosquitoes and influence pathogen/parasite infection of the mosquito midgut. Here, we report the crystal structure of Aedes aegypti procarboxypeptidase B1 (PCPBAe1), characterized its substrate specificity and mechanism of binding to and inhibiting Dengue virus (DENV). We show that the activated PCPBAe1 (CPBAe1) hydrolyzes both Arg- and Lys-substrates, which is modulated by residues Asp²⁵¹ and Ser²³⁹ Notably, these residues are conserved in CPBs across mosquito species, possibly required for efficient digestion of basic dietary residues that are necessary for mosquito reproduction and development. Importantly, we characterized the interaction between PCPBAe1 and DENV envelope (E) protein, virus-

SUBMITTER: Gavor E 

PROVIDER: S-EPMC8605224 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature