Purification and characterization of lysozyme from plasma of the eastern oyster (Crassostrea virginica)

Xue, Qinggang; Schey, Kevin L.; Volety, Aswani K.; Chu, Fu‐Lin E.; Peyre, Jérôme F. La

doi:10.1016/j.cbpc.2004.05.011

Cited by 100 publications

(101 citation statements)

References 38 publications

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“…In the lysozyme and chitinase families, enzymes are expected to act as monomers, and until now, no report has shown lysozyme activity that is regulated by the quaternary structure of the enzyme. As similar with TJL activity, oyster and blue mussel lysozyme activities are modulated by salt concentration (14,15,45). Therefore, in the i-type lysozyme family, modulation of activity because of changes in the quaternary structure may be a common feature.…”

Section: Discussionmentioning

confidence: 94%

“…3). Some i-type lysozymes have been shown to exhibit different salt-concentration sensitivities (14,15,45), which may reflect variations in dimer interactions between catalytic sites and helix 6, because of low sequence homology among enzymes at helix 6.…”

Section: Discussionmentioning

confidence: 99%

“…With increasing salt concentrations, oyster and blue mussel lysozyme activity against Micrococcus lysodeikticus was activated and increased until exposure to a 0.1 M salt solution had been reached; at higher salt concentrations, lysozymatic activity then decreased (13)(14)(15). The latter, decreasing activity under higher salt conditions, might have been introduced by the weakness of the electrostatic interactions between negative charges on the bacterial cell surface and the positive charges of the lysozyme.…”

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confidence: 99%

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Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue

Goto¹,

Abe²,

Kakuta

et al. 2007

Journal of Biological Chemistry

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Tapes japonica lysozyme (TJL) is classified as a member of the recently established i-type lysozyme family. In this study, we solved the crystal structure of TJL complexed with a trimer of N-acetylglucosamine to 1.6 Å resolution. Based on structure and mutation analyses, we demonstrated that Glu-18 and Asp-30 are the catalytic residues of TJL. Furthermore, the present findings suggest that the catalytic mechanism of TJL is a retaining mechanism that proceeds through a covalent sugar-enzyme intermediate. On the other hand, the quaternary structure in the crystal revealed a dimer formed by the electrostatic interactions of catalytic residues (Glu-18 and Asp-30) in one molecule with the positive residues at the C terminus in helix 6 of the other molecule. Gel chromatography analysis revealed that the TJL dimer remained intact under low salt conditions but that it dissociated to TJL monomers under high salt conditions. With increasing salt concentrations, the chitinase activity of TJL dramatically increased. Therefore, this study provides novel evidence that the lysozyme activity of TJL is modulated by its quaternary structure.A known bacteriolytic enzyme, lysozyme (EC 3.2.1.17), is widely distributed throughout the animal and plant kingdom. Several types of lysozyme have been described to date as follows: chicken, goose, bacteria, plant, and phage. Recently, there has been increasing interest in a new type of lysozyme, i.e. invertebrate-type (i-type) 4 lysozyme. The existence of this new type of lysozyme was proposed as early as 1975 (1). A lysozyme composed of 123 amino acids (13.8 kDa) was recently isolated from the marine bivalve Tapes japonica and was shown to be an i-type lysozyme (2). This was the first lysozyme to be identified as an i-type lysozyme based on determination of the complete amino acid sequence at the protein level. Furthermore, several lysozymes have been identified, including those from the following organisms: two coastal bivalves belonging to the genus Mytilus (3), four deep-sea bivalves belonging to the genera Bathymodiolus and Calyptogena (3), a bivalve belonging to Chamys islandica (4, 5), and a starfish belonging to Asterias rubens (6). In 2002, alignment and phylogenic analyses using six bivalve lysozymes suggested that i-type lysozymes form a monophyletic family (7). The tertiary structures of representative lysozymes from chickens (8), geese (9), bacteria (10), plants (11), and phages (12) have already been determined but that of the i-type lysozymes has not. Because the primary sequences of i-type lysozymes are not homologous to those of any other types of lysozyme, the tertiary structure cannot be constructed. Interestingly, the lytic activity of bivalve lysozymes has been shown to be very sensitive to the ionic strength of a solution. With increasing salt concentrations, oyster and blue mussel lysozyme activity against Micrococcus lysodeikticus was activated and increased until exposure to a 0.1 M salt solution had been reached; at higher salt concentrations, lysozymatic activity t...

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue

Goto¹,

Abe²,

Kakuta

et al. 2007

Journal of Biological Chemistry

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“…At higher salt concentrations, the lytic activity decreased. 21,31) This decreasing activity at higher salt conditions might have been caused by a weakness of the electrostatic interactions between the negative charges on the bacterial cell surface and the positive charges of the lysozyme, but the mechanism of salt-dependent activation remains unclear.…”

Section: The Complete Amino Acid Sequence and Enzymatic Properties Ofmentioning

confidence: 99%

“…12,13) The existence of invertebrate lysozyme was first reported by Jollès and Jollès in 1975, 14) and the complete structure was first determined for marine bivalve Venerupis philippinarum lysozyme (VPL), to be composed of 123 amino acids (13.8 kDa) of a size similar to that of c-type lysozyme. 12,[15][16][17] In addition, several lysozymes have been identified in shellfish, including ones from coastal bivalves belonging to the genus Mytilus, 18,19) freshwater bivalve mollusk, 20) sea bivalves belonging to the genera Bathymodiolus and Calyptogena, [21][22][23] and a bivalve belonging to Chlamys islandica. 24,25) Furthermore, lysozymes from the starfish Asterias ruben, 26) Eisenia andrei, 27) Hirudo medicinalis, 28,29) and Stichopus japonicas 30) have also been reported.…”

Section: The Complete Amino Acid Sequence and Enzymatic Properties Ofmentioning

confidence: 99%

The Complete Amino Acid Sequence and Enzymatic Properties of an i-Type Lysozyme Isolated from the Common Orient Clam (Meretrix lusoria)

Kuwano

Yoneda

Kawaguchi

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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Development and characterization of a novel bioactive polymer with antibacterial and lysozyme‐like activity

et al. 2014

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The development and characterization of a novel bioactive polymer based on the immobilization of glucose oxidase enzyme (GOx) in a polyvinyl alcohol (PVA) film showing antibacterial activity is presented. The PVA-GOx composite material was extensively characterized by UV-vis, X-ray Photoelectron (XPS) spectroscopy and by Fourier Transform Infrared (FTIR) spectroscopy to verify the preservation of enzyme structural integrity and activity. The antimicrobial activity of this composite material against Escherichia coli and Vibrio alginolyticus was assessed. Furthermore the lysozyme-like activity of PVA-GOx was highlighted by a standard assay on Petri dishes employing Micrococcus lysodeikticus cell walls. The findings from this study have implications for future investigations related to the employment of PVA-GOx system as a composite material of pharmaceutical and technological interest.

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Purification and characterization of lysozyme from plasma of the eastern oyster (Crassostrea virginica)

Cited by 100 publications

References 38 publications

Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue

Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue

The Complete Amino Acid Sequence and Enzymatic Properties of an i-Type Lysozyme Isolated from the Common Orient Clam (Meretrix lusoria)

Development and characterization of a novel bioactive polymer with antibacterial and lysozyme‐like activity

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