Structure of the immunoregulatory sialidase NEU1

Gorelik, Alexei; Illes, Katalin; Mazhab-Jafari, Mohammad T.; Nagar, Bhushan

doi:10.1126/sciadv.adf8169

Structure of the immunoregulatory sialidase NEU1

Journal Article · Fri May 19 00:00:00 EDT 2023 · Science Advances

DOI:https://doi.org/10.1126/sciadv.adf8169· OSTI ID:2423660

^[1]; Illes, Katalin ^[1]; ^[2]; ^[1]

McGill Univ., Montreal, QC (Canada)
Univ. of Toronto, ON (Canada); University Health Network, Toronto, ON (Canada). Princess Margaret Cancer Center

Sialic acids linked to glycoproteins and glycolipids are important mediators of cell and protein recognition events. These sugar residues are removed by neuraminidases (sialidases). Neuraminidase-1 (sialidase-1 or NEU1) is a ubiquitously expressed mammalian sialidase located in lysosomes and on the cell membrane. Because of its modulation of multiple signaling processes, it is a potential therapeutic target for cancers and immune disorders. Genetic defects in NEU1 or in its protective protein cathepsin A (PPCA, CTSA) cause the lysosomal storage diseases sialidosis and galactosialidosis. To further our understanding of this enzyme’s function at the molecular level, we determined the three-dimensional structure of murine NEU1. The enzyme oligomerizes through two self-association interfaces and displays a wide substrate-binding cavity. A catalytic loop adopts an inactive conformation. We propose a mechanism of activation involving a conformational change in this loop upon binding to its protective protein. These findings may facilitate the development of selective inhibitor and agonist therapies.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 2423660

Journal Information:: Science Advances, Journal Name: Science Advances Journal Issue: 20 Vol. 9; ISSN 2375-2548

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: English

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