HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by ROBERTS, G. Articles by BEIGHTON, D. Search for Related Content PubMed PubMed Citation Articles by ROBERTS, G. Articles by BEIGHTON, D. Agricola Articles by ROBERTS, G. Articles by BEIGHTON, D.

Distribution of endo-ß-N-acetylglucosaminidase amongst enterococci

Oral Microbiology, Guy's, King's and St Thomas’ Dental Institute, King's College London, London, SE5 9RW, UK and *Faculty of Veterinary Medicine, University of Gent, Gent, Belgium

Corresponding author: Dr K.A. Homer (e-mail: karen.a.homer{at}kcl.ac.uk).

Received 9 Nov. 2000; revised version accepted 5 Jan. 2001.

Abstract

Enterococci are becoming increasingly important nosocomial pathogens, a fact mainly attributed to their antimicrobial resistance profiles. However, the enzymic activities required for these organisms to proliferate in vivo have received little attention. Enterococcus faecalis has been shown previously to produce an endo-ß-N-acetylglucosaminidase activity which cleaves high mannose-type glycans in glycoproteins between the N-acetylglucosamine residues of the pentasaccharide core. This study investigated the distribution of this endoglycosidase activity amongst the other enterococcal species. Ribonuclease B, a high mannose-type glycoprotein, was used as a substrate and endoglycosidase activity was demonstrated by a combination of matrix-assisted laser desorption ionisation time-of-flight mass spectrometry and high pH anion-exchange chromatography. Endo-ß-N-acetylglucosaminidase activity was present in 10 of the 18 enterococcal species isolated from both human and animal sources, including all E. faecalis strains. The most notable exception was the lack of this activity in all E. faecium isolates tested. All enterococcal species possessing endoglycosidase activity utilised the liberated glycans to support bacterial growth.

This article has been cited by other articles:

				M. Collin and V. A. Fischetti A Novel Secreted Endoglycosidase from Enterococcus faecalis with Activity on Human Immunoglobulin G and Ribonuclease B J. Biol. Chem., May 21, 2004; 279(21): 22558 - 22570. [Abstract] [Full Text] [PDF]