Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE

Mikel García-Alija, Jonathan J. Du, Izaskun Ordóñez, Asier Diz-Vallenilla, Alicia Moraleda-Montoya, Nazneen Sultana, Chau G. Huynh, Chao Li, Thomas Connor Donahue, Lai-Xi Wang, Beatriz Trastoy (), Eric J. Sundberg () and Marcelo E. Guerin ()
Additional contact information
Mikel García-Alija: Cruces University Hospital
Jonathan J. Du: Emory University School of Medicine
Izaskun Ordóñez: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park
Asier Diz-Vallenilla: Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park
Alicia Moraleda-Montoya: Cruces University Hospital
Nazneen Sultana: Emory University School of Medicine
Chau G. Huynh: Emory University School of Medicine
Chao Li: University of Maryland
Thomas Connor Donahue: University of Maryland
Lai-Xi Wang: University of Maryland
Beatriz Trastoy: Cruces University Hospital
Eric J. Sundberg: Emory University School of Medicine
Marcelo E. Guerin: Cruces University Hospital

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Bacteria produce a remarkably diverse range of glycoside hydrolases to metabolize glycans from the environment as a primary source of nutrients, and to promote the colonization and infection of a host. Here we focus on EndoE, a multi-modular glycoside hydrolase secreted by Enterococcus faecalis, one of the leading causes of healthcare-associated infections. We provide X-ray crystal structures of EndoE, which show an architecture composed of four domains, including GH18 and GH20 glycoside hydrolases connected by two consecutive three α-helical bundles. We determine that the GH20 domain is an exo-β-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-β-1,4-N-acetylglucosaminidase that exclusively processes the central core of complex-type or high-mannose-type N-glycans. Both glycoside hydrolase domains act in a concerted manner to process diverse N-glycans on glycoproteins, including therapeutic IgG antibodies. EndoE combines two enzyme domains with distinct functions and glycan specificities to play a dual role in glycan metabolism and immune evasion.

Date: 2022
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DOI: 10.1038/s41467-022-28722-w

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