Evidence of an Antimicrobial Peptide Signature Encrypted in HECT E3 Ubiquitin Ligases.

ABSTRACT: The ubiquitin-proteasome pathway (UPP) is a hallmark of the eukaryotic cell. In jawed vertebrates, it has been co-opted by the adaptive immune system, where proteasomal degradation produces endogenous peptides for major histocompatibility complex class I antigen presentation. However, proteolytic products are also necessary for the phylogenetically widespread innate immune system, as they often play a role as host defense peptides (HDPs), pivotal effectors against pathogens. Here, we report the identification of the arachnid HDP oligoventin, which shares homology to a core member of the UPP, E3 ubiquitin ligases. Oligoventin has broad antimicrobial activity and shows strong synergy with lysozymes. Using computational and phylogenetic approaches, we show high conservation of the oligoventin

SUBMITTER: Candido-Ferreira IL 

PROVIDER: S-EPMC5220581 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature