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Jean S. Deutsch - One of the best experts on this subject based on the ideXlab platform.
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The Lysozyme of the starfish Asterias rubens. A paradigmatic type i Lysozyme.
European journal of biochemistry, 2004Co-Authors: Sana Bachali, Jacqueline Jollès, Pierre Jollès, Xavier Bailly, Jean S. DeutschAbstract:On the basis of a partial N-terminal sequence, Jolles and Jolles [Jolles, J., & Jolles, P. (1975) Eur. J. Biochem.54, 19–23] previously proposed that the Lysozyme from the starfish Asterias rubens represents a new form of Lysozyme, called type i (invertebrate) Lysozyme. Indeed, it differed from both the types c (chicken) and g (goose) known in other animals, as well as from plant and phage Lysozymes. Recently, several proteins belonging to the same family have been isolated from protostomes. Here we report the complete mature protein sequence and cDNA sequence of the Lysozyme from Asterias. These sequences vindicate the previously proposed homology between the starfish, a deuterostome, and protostome Lysozymes. In addition, we present a structural analysis that allows us to postulate upon the function of several conserved residues.
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The Lysozyme of the starfish Asterias rubens. A paradigmatic type i Lysozyme.
European Journal of Biochemistry, 2004Co-Authors: Sana Bachali, Jacqueline Jollès, Pierre Jollès, Xavier Bailly, Jean S. DeutschAbstract:On the basis of a partial N-terminal sequence, Jollès and Jollès [Jollès, J., & Jollès, P. (1975) Eur. J. Biochem.54, 19–23] previously proposed that the Lysozyme from the starfish Asterias rubens represents a new form of Lysozyme, called type i (invertebrate) Lysozyme. Indeed, it differed from both the types c (chicken) and g (goose) known in other animals, as well as from plant and phage Lysozymes. Recently, several proteins belonging to the same family have been isolated from protostomes. Here we report the complete mature protein sequence and cDNA sequence of the Lysozyme from Asterias. These sequences vindicate the previously proposed homology between the starfish, a deuterostome, and protostome Lysozymes. In addition, we present a structural analysis that allows us to postulate upon the function of several conserved residues.
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Phylogenetic analysis of invertebrate Lysozymes and the evolution of Lysozyme function.
Journal of molecular evolution, 2002Co-Authors: Sana Bachali, Pierre Jollès, Françoise Schoentgen, Muriel Jager, Alexandre Hassanin, Aline Fiala-médioni, Jean S. DeutschAbstract:We isolated and sequenced the cDNAs coding for Lysozymes of six bivalve species. Alignment and phylogenetic analysis showed that, together with recently described bivalve Lysozymes, the leech destabilase, and a number of putative proteins from extensive genomic and cDNA analyses, they belong to the invertebrate type of Lysozymes (i type), first described by Jolles and Jolles (1975). We determined the genomic structure of the gene encoding the Lysozyme of Mytilus edulis, the common mussel. We provide evidence that the central exon of this gene is homologous to the second exon of the chicken Lysozyme gene, belonging to the c type. We propose that the origin of this domain can be traced back in evolution to the origin of bilaterian animals. Phylogenetic analysis suggests that i-type proteins form a monophyletic family.
Sana Bachali - One of the best experts on this subject based on the ideXlab platform.
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The Lysozyme of the starfish Asterias rubens. A paradigmatic type i Lysozyme.
European journal of biochemistry, 2004Co-Authors: Sana Bachali, Jacqueline Jollès, Pierre Jollès, Xavier Bailly, Jean S. DeutschAbstract:On the basis of a partial N-terminal sequence, Jolles and Jolles [Jolles, J., & Jolles, P. (1975) Eur. J. Biochem.54, 19–23] previously proposed that the Lysozyme from the starfish Asterias rubens represents a new form of Lysozyme, called type i (invertebrate) Lysozyme. Indeed, it differed from both the types c (chicken) and g (goose) known in other animals, as well as from plant and phage Lysozymes. Recently, several proteins belonging to the same family have been isolated from protostomes. Here we report the complete mature protein sequence and cDNA sequence of the Lysozyme from Asterias. These sequences vindicate the previously proposed homology between the starfish, a deuterostome, and protostome Lysozymes. In addition, we present a structural analysis that allows us to postulate upon the function of several conserved residues.
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The Lysozyme of the starfish Asterias rubens. A paradigmatic type i Lysozyme.
European Journal of Biochemistry, 2004Co-Authors: Sana Bachali, Jacqueline Jollès, Pierre Jollès, Xavier Bailly, Jean S. DeutschAbstract:On the basis of a partial N-terminal sequence, Jollès and Jollès [Jollès, J., & Jollès, P. (1975) Eur. J. Biochem.54, 19–23] previously proposed that the Lysozyme from the starfish Asterias rubens represents a new form of Lysozyme, called type i (invertebrate) Lysozyme. Indeed, it differed from both the types c (chicken) and g (goose) known in other animals, as well as from plant and phage Lysozymes. Recently, several proteins belonging to the same family have been isolated from protostomes. Here we report the complete mature protein sequence and cDNA sequence of the Lysozyme from Asterias. These sequences vindicate the previously proposed homology between the starfish, a deuterostome, and protostome Lysozymes. In addition, we present a structural analysis that allows us to postulate upon the function of several conserved residues.
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The Lysozyme of the starfish Asteriasrubens
European Journal of Biochemistry, 2004Co-Authors: Sana Bachali, Jacqueline Jollès, Pierre Jollès, Xavier Bailly, Jean S. DeutschAbstract:On the basis of a partial N-terminal sequence, Jolle`s and Jolle`s [Jolle`s, J., & Jolle`s, P. (1975) Eur. J. Biochem. 54, 19–23] previously proposed that the Lysozyme from the starfish Asterias rubens represents a new form of Lysozyme, called type i (invertebrate) Lysozyme. Indeed, it differed from both the types c (chicken) and g (goose) known in other animals, as well as from plant and phage Lysozymes. Recently, several proteins belonging to the same family have been isolated from protostomes. Here we report the com- plete mature protein sequence and cDNA sequence of the Lysozyme from Asterias. These sequences vindicate the previously proposed homology between the starfish, a deuterostome, and protostome Lysozymes. In addition, we present a structural analysis that allows us to postulate upon the function of several conserved residues.
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Phylogenetic analysis of invertebrate Lysozymes and the evolution of Lysozyme function.
Journal of molecular evolution, 2002Co-Authors: Sana Bachali, Pierre Jollès, Françoise Schoentgen, Muriel Jager, Alexandre Hassanin, Aline Fiala-médioni, Jean S. DeutschAbstract:We isolated and sequenced the cDNAs coding for Lysozymes of six bivalve species. Alignment and phylogenetic analysis showed that, together with recently described bivalve Lysozymes, the leech destabilase, and a number of putative proteins from extensive genomic and cDNA analyses, they belong to the invertebrate type of Lysozymes (i type), first described by Jolles and Jolles (1975). We determined the genomic structure of the gene encoding the Lysozyme of Mytilus edulis, the common mussel. We provide evidence that the central exon of this gene is homologous to the second exon of the chicken Lysozyme gene, belonging to the c type. We propose that the origin of this domain can be traced back in evolution to the origin of bilaterian animals. Phylogenetic analysis suggests that i-type proteins form a monophyletic family.
Chris W Michiels - One of the best experts on this subject based on the ideXlab platform.
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Invertebrate Lysozymes: Diversity and distribution, molecular mechanism and in vivo function
2014Co-Authors: Joris M Van Herreweghe, Chris W MichielsAbstract:Lysozymes are antibacterial enzymes widely distributed among organisms. Within the animal kingdom, mainly three major Lysozyme types occur. Chicken (c)-type Lysozyme and goose (g)-type Lysozyme are predominantly, but not exclusively, found in vertebrate animals, while the invertebrate (i)-type Lysozyme is typical for invertebrate organisms, and hence its name. Since their discovery in 1975, numerous research articles report on the identification of i-type Lysozymes in a variety of invertebrate phyla. This review describes the current knowledge on i-type Lysozymes, outlining their distribution, molecular mechanism and in vivo function taking the representative from Venerupis philippinarum (formerly Tapes japonica) (Vp-ilys) as a model. In addition, invertebrate g-type and ch-type (chalar-opsis) Lysozymes, which have been described in molluscs and nematodes, respectively, are also briefly discussed. [Van Herreweghe JM and Michiels CW 2012 Invertebrate Lysozymes: Diversity and distribution, molecular mechanism and in vivo function. J. Biosci. 37 327–348] DOI 10.1007/s12038-012-9201-y 1
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Invertebrate Lysozymes: Diversity and distribution, molecular mechanism and in vivo function
Journal of Biosciences, 2012Co-Authors: Joris M Herreweghe, Chris W MichielsAbstract:Lysozymes are antibacterial enzymes widely distributed among organisms. Within the animal kingdom, mainly three major Lysozyme types occur. Chicken (c)-type Lysozyme and goose (g)-type Lysozyme are predominantly, but not exclusively, found in vertebrate animals, while the invertebrate (i)-type Lysozyme is typical for invertebrate organisms, and hence its name. Since their discovery in 1975, numerous research articles report on the identification of i-type Lysozymes in a variety of invertebrate phyla. This review describes the current knowledge on i-type Lysozymes, outlining their distribution, molecular mechanism and in vivo function taking the representative from Venerupis philippinarum (formerly Tapes japonica ) (Vp-ilys) as a model. In addition, invertebrate g-type and ch-type (chalaropsis) Lysozymes, which have been described in molluscs and nematodes, respectively, are also briefly discussed.
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Lysozymes in the animal kingdom
Journal of Biosciences, 2010Co-Authors: Lien Callewaert, Chris W MichielsAbstract:Lysozymes (EC 3.2.1.17) are hydrolytic enzymes, characterized by their ability to cleave the β -(1,4)-glycosidic bond between N -acetylmuramic acid and N -acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. In the animal kingdom, three major distinct Lysozyme types have been identified — the c-type ( c hicken or c onventional type), the g-type ( g oose-type) and the i-type ( i nvertebrate type) Lysozyme. Examination of the phylogenetic distribution of these Lysozymes reveals that c-type Lysozymes are predominantly present in the phylum of the Chordata and in different classes of the Arthropoda. Moreover, g-type Lysozymes (or at least their corresponding genes) are found in members of the Chordata, as well as in some bivalve mollusks belonging to the invertebrates. In general, the latter animals are known to produce i-type Lysozymes. Although the homology in primary structure for representatives of these three Lysozyme types is limited, their three-dimensional structures show striking similarities. Nevertheless, some variation exists in their catalytic mechanisms and the genomic organization of their genes. Regarding their biological role, the widely recognized function of Lysozymes is their contribution to antibacterial defence but, additionally, some Lysozymes (belonging to different types) are known to function as digestive enzymes.
Fatma Denizli - One of the best experts on this subject based on the ideXlab platform.
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affinity microspheres and their application to Lysozyme adsorption cibacron blue f3ga and cu ii with poly hema egdma
Polymer International, 1999Co-Authors: Fatma Denizli, Adil Denizli, Yakup M AricaAbstract:Lysozyme adsorption onto Cibacron Blue F3GA attached and Cu(II) incorporated poly(2-hydroxyethyl methacrylate-ethylene glycol dimethacrylate) [poly(HEMA-EGDMA)] microspheres was investigated. The microspheres were prepared by suspension polymerization. Various amounts of Cibacron Blue F3GA were attached covalently onto the microspheres by changing the initial concentration of dye in the reaction medium. The microspheres with a swelling ratio of 65%, and carrying different amounts of dye (between 1.4 and 22.5 μmol/g -1 ) were used in the Lysozyme adsorption studies. Lysozyme adsorption on these microspheres from aqueous solutions containing different amounts of Lysozyme at different pH values was investigated in batch reactors. The Lysozyme adsorption capacity of the dye-metal chelated microspheres (238.2 mg g -1 ) was greater than that of the dye-attached microspheres (175.1 mg g -1 ). The maximum lyzozyme adsorption capacities (q m and the dissociation constant (k d ) values were found to be 204.9 mg g -1 and 0.0715 mg ml -1 with dye-attached and 270.7 mg g -1 and 0.0583 mg ml -1 with dye-metal chelated microspheres, respectively. More than 90% of the adsorbed Lysozyme were desorbed in 60min in the desorption medium containing 0.5M KSCN at pH 8.0 or 25 mM EDTA at pH 4.9.
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Affinity microspheres and their application to Lysozyme adsorption: Cibacron Blue F3GA and Cu(II) with poly(HEMA‐EGDMA)
Polymer International, 1999Co-Authors: Fatma Denizli, Adil Denizli, M. Yakup AricaAbstract:Lysozyme adsorption onto Cibacron Blue F3GA attached and Cu(II) incorporated poly(2-hydroxyethyl methacrylate-ethylene glycol dimethacrylate) [poly(HEMA-EGDMA)] microspheres was investigated. The microspheres were prepared by suspension polymerization. Various amounts of Cibacron Blue F3GA were attached covalently onto the microspheres by changing the initial concentration of dye in the reaction medium. The microspheres with a swelling ratio of 65%, and carrying different amounts of dye (between 1.4 and 22.5 μmol/g -1 ) were used in the Lysozyme adsorption studies. Lysozyme adsorption on these microspheres from aqueous solutions containing different amounts of Lysozyme at different pH values was investigated in batch reactors. The Lysozyme adsorption capacity of the dye-metal chelated microspheres (238.2 mg g -1 ) was greater than that of the dye-attached microspheres (175.1 mg g -1 ). The maximum lyzozyme adsorption capacities (q m and the dissociation constant (k d ) values were found to be 204.9 mg g -1 and 0.0715 mg ml -1 with dye-attached and 270.7 mg g -1 and 0.0583 mg ml -1 with dye-metal chelated microspheres, respectively. More than 90% of the adsorbed Lysozyme were desorbed in 60min in the desorption medium containing 0.5M KSCN at pH 8.0 or 25 mM EDTA at pH 4.9.
Qinggang Xue - One of the best experts on this subject based on the ideXlab platform.
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An i-type Lysozyme from the Asiatic hard clam Meretrix meretrix potentially functioning in host immunity.
Fish & Shellfish Immunology, 2010Co-Authors: Xin Yue, Baozhong Liu, Qinggang XueAbstract:Lysozymes function in animal immunity. Three types of Lysozyme have been identified in animal kingdom and most Lysozymes identified from bivalve molluscs belong to the invertebrate (i) type. In this research, we cloned and sequenced a new i-type Lysozyme, named MmeLys, from the Asiatic hard clam Meretrix meretrix. MmeLys cDNA was constituted of 552 bp, with a 441 bp open reading frame encoding a 146 amino acid polypeptide. The encoded polypeptide was predicted to have a 15 amino acid signal peptide, and a 131 amino acid mature protein with a theoretical mass of 14601.44 Da and an isoelectric point (pI) of 7.14. MmeLys amino acid sequence bore 64% identity with the Manila clam (Venerupis philippinarum) i-type Lysozyme and was grouped with other veneroid i-type Lysozymes in a bivalve Lysozyme phylogenetic tree predicted using Neighbor-Jointing method. Recombinantly expressed MmeLys showed Lysozyme activity and strong antibacterial activity against Gram positive and Gram negative bacteria. MmeLys mRNA and protein were detected to be mainly produced in hepatopancreas and gill by the methods of semi-quantitative RT-PCR and western blotting. In addition, MmeLys gene expression increased following Vibrio parahaemolyticus challenge. Results of this research indicated that MmeLys represents a new i-type Lysozyme that likely functions in M. meretrix immunity.
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A new Lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type Lysozymes.
Cellular and molecular life sciences : CMLS, 2006Co-Authors: Qinggang Xue, Kevin L Schey, Naoki Itoh, Richard K Cooper, J. F. La PeyreAbstract:A new Lysozyme (cv-Lysozyme 2) with a MALDI molecular mass of 12 984.6 Da was purified from crystalline styles and digestive glands of eastern oysters (Crassostrea virginica) and its cDNA sequenced. Quantitative real time RT-PCR detected cv-Lysozyme 2 gene expression primarily in digestive gland tissues, and in situ hybridization located cv-Lysozyme 2 gene expression in basophil cells of digestive tubules. Cv-Lysozyme 2 showed high amino acid sequence similarity to other bivalve mollusk Lysozymes, including cv-Lysozyme 1, a Lysozyme recently purified from C. virginica plasma. Differences between cv-Lysozyme 2 and cv-Lysozyme 1 molecular characteristics, enzymatic properties, antibacterial activities, distribution in the oyster body and site of gene expression indicate that the main role of cv-Lysozyme 2 is in digestion. While showing that a bivalve mollusk employs different Lysozymes for different functions, findings in this study suggest adaptive evolution of i type Lysozymes for nutrition.
