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Nicotinamide adenine dinucleotide (NAD) is a key molecule in cellular bioenergetics and signalling. Various bacterial pathogens release NADase enzymes into the host cell that deplete the host’s NAD +  pool, thereby causing rapid cell death. Here, we report the identification of NADases on the surface of fungi such as the pathogen  Aspergillus fumigatus  and the saprophyte  Neurospora crassa . The enzymes harbour a tuberculosis necrotizing toxin (TNT) domain and are predominately present in pathogenic species. The 1.6 Å X-ray structure of the homodimeric  A. fumigatus  protein reveals unique properties including N-linked glycosylation and a Ca 2+ -binding site whose occupancy regulates activity. The structure in complex with a substrate analogue suggests a catalytic mechanism that is distinct from those of known NADases, ADP-ribosyl cyclases and transferases. We propose that fungal NADases may convey advantages during interaction with the host or competing microorganisms.

Discovery of fungal surface NADases predominantly present in pathogenic species