Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis

Goda, Hatsumi M.; Ushigusa, Kota; Ito, Hiromi; Okino, Nozomu; Narimatsu, Hisashi; Ito, Makoto

doi:10.1016/j.bbrc.2008.08.065

Cited by 27 publications

(18 citation statements)

References 15 publications

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“…Molecular cloning, expression, and characterization (Goda, et al, 2008) Endo-β -N-acetylglucosaminidase (endo A)…”

Section: Littorina Kurila (Mollusc) Tof (Dhb)mentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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“…Molecular cloning, expression, and characterization (Goda, et al, 2008) Endo-β -N-acetylglucosaminidase (endo A)…”

Section: Littorina Kurila (Mollusc) Tof (Dhb)mentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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“…Other examples from Propionibacterium acnes and Enterococcus faecalis are active on the core 3 O-glycan (GlcNAc␤1-3GalNAc␣1-Ser/Thr) (6,7).…”

mentioning

confidence: 99%

Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism

Gregg

Suits

Deng

et al. 2015

Journal of Biological Chemistry

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Background:The endo-␣-D-N-acetylgalactosaminidase SpGH101 from Streptococcus pneumoniae hydrolyzes the O-linked T-antigen from proteins. Results: SpGH101 displays an unusual conformational change on substrate binding and a distinctive arrangement of its catalytic machinery. Conclusion: Substrate hydrolysis proceeds through a retaining mechanism with a proton shuttle. Significance: This is the first evidence of proton shuttle in a retaining glycoside hydrolase.

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“…Like most previously described bacterial PGHs (13,18,35), Acp has a modular organization with three main domains consisting of a signal peptide, an N-terminal domain characterized by repeated sequences, and a C-terminal catalytic domain conferring the hydrolytic activity. The first 30 amino acid residues of the N-terminal domain of Acp might constitute a putative signal sequence and probably a retention site with a transmembrane domain, as described for cell wall hydrolases in B. subtilis (56).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Acp, a Peptidoglycan Hydrolase of Clostridium perfringens with N -Acetylglucosaminidase Activity That Is Implicated in Cell Separation and Stress-Induced Autolysis

et al. 2010

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This work reports the characterization of the first known peptidoglycan hydrolase (Acp) produced mainly during vegetative growth of Clostridium perfringens. Acp has a modular structure with three domains: a signal peptide domain, an N-terminal domain with repeated sequences, and a C-terminal catalytic domain. The purified recombinant catalytic domain of Acp displayed lytic activity on the cell walls of several Gram-positive bacterial species. Its hydrolytic specificity was established by analyzing the Bacillus subtilis peptidoglycan digestion products by coupling reverse phase-high-pressure liquid chromatography (RP-HPLC) and matrixassisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis, which displayed an N-acetylglucosaminidase activity. The study of acp expression showed a constant expression during growth, which suggested an important role of Acp in growth of C. perfringens. Furthermore, cell fractionation and indirect immunofluorescence staining using anti-Acp antibodies revealed that Acp is located at the septal peptidoglycan of vegetative cells during exponential growth phase, indicating a role in cell separation or division of C. perfringens. A knockout acp mutant strain was obtained by using the insertion of mobile group II intron strategy (ClosTron). The microscopic examination indicated a lack of vegetative cell separation in the acp mutant strain, as well as the wild-type strain incubated with anti-Acp antibodies, demonstrating the critical role of Acp in cell separation. The comparative responses of wild-type and acp mutant strains to stresses induced by Triton X-100, bile salts, and vancomycin revealed an implication of Acp in autolysis induced by these stresses. Overall, Acp appears as a major cell wall N-acetylglucosaminidase implicated in both vegetative growth and stress-induced autolysis.Autolysins are endogenous peptidoglycan hydrolases (PGHs) that can break covalent bonds in the bacterial cell wall peptidoglycan (16,58). Various PGHs are distinguished on the basis of their specific cleavage site in the peptidoglycan: N-acetylmuramidases, N-acetylglucosaminidases, N-acetylmuramoyl-Lalanine amidases, and endopeptidases. PGHs are involved in different physiological functions that require cell wall remodeling such as cell wall expansion, peptidoglycan turnover, daughter cell separation, or sporulation (53, 54, 60). These enzymes may also be implicated in antibiotic-induced lysis (39) and may contribute to bacterial pathogenesis by generating inflammatory cell wall degradation products (32, 40), by releasing virulence factors (4), or by mediating bacterial adherence (1,20,21). The roles of PGHs in bacterial physiology, and probably in bacterial pathogenicity, further reinforce the importance of understanding bacterial autolysis.Autolytic systems of several Gram-positive low-GϩC bacteria have been studied (5,13,34,43,54,55). Belonging to this phylum is Clostridium perfringens, a common agent of food poisoning and implicated in infectious diseases initiating fr...

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Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis

Cited by 27 publications

References 15 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism

Characterization of Acp, a Peptidoglycan Hydrolase of Clostridium perfringens with N -Acetylglucosaminidase Activity That Is Implicated in Cell Separation and Stress-Induced Autolysis

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