Donor strand complementation, isopeptide bonds and glycosylation reinforce highly resilient archaeal thread filaments

Abstract

AbstractPili are ubiquitous filamentous surface extensions that play crucial roles for bacterial and archaeal cellular processes such as adhesion, biofilm formation, motility, cell-cell communication, DNA uptake and horizontal gene transfer to name a few. Here we report on the discovery and structure of the archaeal thread – a remarkably stable archaeal pilus that belongs to a so-far largely unknown class of protein filaments. We find that the filament is highly glycosylated and interconnected via donor strand complementation, as well as isopeptide bonds, reminiscent of bacterial type I pili. Despite striking structural similarity with bacterial type-1 pili, archaeal threads appear to have evolved independently and are likely assembled by a markedly distinct mechanism.