7pul

Publication Abstract from PubMed

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 alpha-helical bundles. We determine that the GH20 domain is an exo-beta-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-beta-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.

Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE.,Garcia-Alija M, Du JJ, Ordonez I, Diz-Vallenilla A, Moraleda-Montoya A, Sultana N, Huynh CG, Li C, Donahue TC, Wang LX, Trastoy B, Sundberg EJ, Guerin ME Nat Commun. 2022 Mar 3;13(1):1137. doi: 10.1038/s41467-022-28722-w. PMID:35241669^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.