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J. Biol. Chem., Vol. 279, Issue 21, 22558-22570, May 21, 2004

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A Novel Secreted Endoglycosidase from Enterococcus faecalis with Activity on Human Immunoglobulin G and Ribonuclease B^*

Mattias Collin and Vincent A. Fischetti

From the Laboratory of Bacterial Pathogenesis, The Rockefeller University, New York, New York 10021

The human pathogen Enterococcus faecalis can degrade the N-linked glycans of human RNase B to acquire nutrients, but no gene or protein has been associated with this activity. We identified an 88-kDa secreted protein, endoglycosidase (Endo) E, which is most likely responsible for this activity. EndoE, encoded by ndoE, consists of an -domain with a family 18 glycosyl hydrolase motif and a -domain similar to family 20 glycosyl hydrolases. Phylogenetic analysis of EndoE indicates that the -domain is related to human chitobiases, and the -domain is related to bacterial and human hexosaminidases. Recombinant expression of full-length EndoE or EndoE, site-directed mutagenesis of the catalytic residues, mass spectroscopy, and homology modeling shows that EndoE hydrolyzes the glycan on human RNase B, whereas EndoE hydrolyzes the conserved glycan on IgG. Denaturation experiments indicate that the chitinase activity on RNase B is not dependent on the tertiary structure, although it is on IgG. The ndoE gene and secreted EndoE are present in most E. faecalis but not in Enterococcus faecium isolates. Correspondingly, E. faecalis, but not E. faecium, degrades the glycan on RNase B during growth. Thus, we have identified a secreted enzyme from E. faecalis, EndoE, which by two distinct activities hydrolyzes the glycans on RNase B and IgG. Both activities could be important for the molecular pathogenesis and persistence of E. faecalis during human infections.

Received for publication, February 26, 2004

^* This work was supported in part by United States Public Health Service Grant AI11822 (to V. A. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a fellowship from the Wenner-Gren Foundations, Sweden. To whom correspondence may be addressed. Tel.: 212-327-8170; Fax: 212-327-7584; E-mail: collinm{at}mail.rockefeller.edu.

To whom correspondence may be addressed. Tel.: 212-327-8166; Fax: 212-327-7584; E-mail: vaf{at}rockefeller.edu.

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