An endo-ß-N-acetylglucosaminidase from Enterococcus faecalis V583 responsible for the hydrolysis of high-mannose and hybrid-type N-linked glycans

被引：26

作者：

Bohle, Liv Anette ^{[1
]}

Mathiesen, Geir ^{[1
]}

Vaaje-Kolstad, Gustav ^{[1
]}

Eijsink, Vincent G. H. ^{[1
]}

机构：

[1] Norwegian Univ Life Sci, Dept Chem Biotechnol & Food Sci, N-1432 As, Norway

来源：

FEMS MICROBIOLOGY LETTERS | 2011年 / 325卷 / 02期

关键词：

endo-ss-N-acetylglucosaminidase; Enterococcus faecalis V583; glycoprotein; N-linked glycan; PROTEIN GLYCOSYLATION; MUCIN DEGRADATION; SIGNAL PEPTIDES; HUMAN-COLON; OLIGOSACCHARIDES; ENDOGLYCOSIDASE; PREDICTION; STRAINS; ENZYMES; GROWTH;

D O I：

10.1111/j.1574-6968.2011.02419.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain. We have analyzed the other candidate, EF2863, and show that this predicted single domain GH18 protein is an endo-beta-N-acetylglucosaminidase. EF2863 hydrolyzes the glycosidic bond between two N-acetylglucosamines (GlcNAc) in N-linked glycans of the high-mannose and hybrid type, releasing the glycan and leaving one GlcNAc attached to the protein. The activity of EF2863 is similar to that of the well known deglycosylating enzyme EndoH from Streptomyces plicatus. According to the CAZy nomenclature, the enzyme is designated EfEndo18A.

引用

页码：123 / 129

页数：7

共 37 条

[1] Determination of N-glycosylation sites and site heterogeneity in glycoproteins [J].

An, HJ ;

Peavy, TR ;

Hedrick, JL ;

Lebrilla, CB .

ANALYTICAL CHEMISTRY, 2003, 75 (20) :5628-5637

[2] On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database [J].

Apweiler, R ;

Hermjakob, H ;

Sharon, N .

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1999, 1473 (01) :4-8

[3] Mucin structure, aggregation, physiological functions and biomedical applications [J].

Bansil, Rama ;

Turner, Bradley S. .

CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 2006, 11 (2-3) :164-170

[4] Improved prediction of signal peptides: SignalP 3.0 [J].

Bendtsen, JD ;

Nielsen, H ;

von Heijne, G ;

Brunak, S .

JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (04) :783-795

[5] The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics [J].

Cantarel, Brandi L. ;

Coutinho, Pedro M. ;

Rancurel, Corinne ;

Bernard, Thomas ;

Lombard, Vincent ;

Henrissat, Bernard .

NUCLEIC ACIDS RESEARCH, 2009, 37 :D233-D238

[6] Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry [J].

Chu, Caroline S. ;

Ninonuevo, Milady R. ;

Clowers, Brian H. ;

Perkins, Patrick D. ;

An, Hyun Joo ;

Yin, Hongfeng ;

Killeen, Kevin ;

Miyamoto, Suzanne ;

Grimm, Rudolf ;

Lebrilla, Carlito B. .

PROTEOMICS, 2009, 9 (07) :1939-1951

[7] A novel secreted endoglycosidase from Enterococcus faecalis with activity on human immunoglobulin G and ribonuclease B [J].

Collin, M ;

Fischetti, VA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (21) :22558-22570

[8] Extracellular enzymes with immunomodulating activities:: Variations on a theme in Streptococcus pyogenes [J].

Collin, M ;

Olsén, A .

INFECTION AND IMMUNITY, 2003, 71 (06) :2983-2992

[9] EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG [J].

Collin, M ;

Olsén, A .

EMBO JOURNAL, 2001, 20 (12) :3046-3055

[10] MUCIN DEGRADATION IN THE HUMAN COLON - PRODUCTION OF SIALIDASE, SIALATE O-ACETYLESTERASE, N-ACETYLNEURAMINATE LYASE, ARYLESTERASE, AND GLYCOSULFATASE ACTIVITIES BY STRAINS OF FECAL BACTERIA [J].

CORFIELD, AP ;

WAGNER, SA ;

CLAMP, JR ;

KRIARIS, MS ;

HOSKINS, LC .

INFECTION AND IMMUNITY, 1992, 60 (10) :3971-3978

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