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Significance Covalently linked pili are produced by many gram-positive bacteria; these heteropolymers in various lengths are assembled on the bacterial peptidoglycan by conserved cysteine transpeptidase enzymes named sortases. How the sortase machine controls pilus length and whether pilus length is crucial for bacterial interactions remain elusive. We discover herein that the housekeeping sortase ofActinomyces oris utilizes 2 structural elements for recognition of pilin substrates to control pilus length, hence positioning of pilus tip adhesins. Importantly, we show that optimal positioning of pilus tip adhesins is critical for interspecies interactions, or coaggregation, a prerequisite for the development of oral biofilms.

Cell-to-cell interaction requires optimal positioning of a pilus tip adhesin modulated by gram-positive transpeptidase enzymes