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1.
J Proteomics ; 144: 87-98, 2016 07 20.
Article in English | MEDLINE | ID: mdl-27321578

ABSTRACT

UNLABELLED: Mussels attach to various submerged surfaces by using the byssus, which contains different proteins and is a promising source of water-resistant bio-adhesives for potential use in biotechnological and medical applications. The protein composition of the byssus has not yet been fully understood although at least eleven byssal proteins were characterized previously. In order to increase genomic resources and identify new byssal proteins from mussel Mytilus coruscus, high-throughput Illumina sequencing was undertaken on the foot, and 79,997,776 paired-ends reads were generated, yielding a library containing 88,825ft unigenes. The M. coruscus byssus was divided into three parts, the proximal thread, the distal thread, and the plaque. Byssal proteins from each part of the byssus were analyzed by shotgun-LTQ analysis. The MS/MS spectra were searched against the foot unigenes dataset and 48 byssal proteins were identified from the M. coruscus byssus. From the whole set, 17, 5, and 11 proteins were exclusive to the proximal thread, the distal thread, and the plaque, respectively. These data can be used as a resource for further studies on the roles of byssal proteins in the deposition of different byssus parts (thread vs. plaque) or in the different mechanical properties (tenacity vs. adhesion). BIOLOGICAL SIGNIFICANCE: Byssal proteins are the major component that controls different aspects of the byssal formation process and thus a source of bioactive molecules that would offer interesting perspectives in biomaterials and bio-adhesive fields. In this paper, we characterized the protein set from different partsof Mytilus coruscus byssus by a combination of transcriptome/proteome technical. A whole set of 48 byssal proteins were described here, including proteins of collagen-like, C1q domain-containing, protease inhibitor-like, tyrosinase-like, SOD, and others. Thread (the distal portion and the proximal portion) and plaque showed distinct protein composition. Of the whole byssal protein set, 11 are exclusive to the plaque, 17 are exclusive to the proximal thread, and 5 are exclusive to the distal thread. Only four proteins are shared by all the three parts of the byssus. The new byssal proteins reported here represent a significant expansion of the knowledge base of Mytilus byssal proteins, and are important for further exploring the mechanism of adhesion in mussel.


Subject(s)
Mytilus/anatomy & histology , Proteins/analysis , Proteomics/methods , Tissue Adhesives/chemistry , Animals , Mytilus/chemistry , Proteome/analysis , Tandem Mass Spectrometry
2.
J Proteomics ; 122: 26-40, 2015 Jun 03.
Article in English | MEDLINE | ID: mdl-25857279

ABSTRACT

Mytilus is an economically important bivalve and its shell is a biomineralized tissue with various microstructures/layers. In the present study, the shell of marine mussel, Mytilus coruscus, was analyzed and three shell layers with different morphologies and polymorphs were observed, which includes nacre, fibrous prism, and myostracum strongly attached by adductor muscles to the interior of the shell surface. In order to understand whether these different shell layers contain different shell matrix proteins (SMPs), the transcriptome sequencing of M. coruscus mantle and a parallel proteomic analysis of SMPs in the three shell layers were performed. A combination of LC-MS/MS analysis with the mantle transcriptome dataset search resulted in the identification of a total of 63 proteins from M. coruscus shell. From this protein set, fifteen, fourteen, and eight proteins were found to be unique to nacre, fibrous prism, and myostracum layers, respectively. In addition, many novel shell proteins were also identified. The data in this study could be used as a background to explore the roles of SMPs in the deposition of different shell layers (nacre vs. fibrous prism vs. myostracum), the different polymorphisms of calcium carbonate (aragonite vs. calcite); and further, the identified proteins from the myostracum could provide candidates for studying the mechanism of adductor muscle-shell attachment. BIOLOGICAL SIGNIFICANCE: In this paper, we characterized for the first time the protein set from different shell layers in Mytilus. Shell matrix proteins are the major component that controls different aspects of the shell formation process and thus a source of bioactive molecules that would offer interesting perspectives in biomaterials and biomedical fields. Our data can be used as a resource for further exploring the roles of shell matrix proteins in the deposition of different shell layers (nacre vs. fibrous prism vs. myostracum) or different polymorphisms of calcium carbonate (aragonite vs. calcite), and the identified protein set of myostracum provided candidates for studying the mechanism of adductor muscle-shell attachment.


Subject(s)
Animal Shells/metabolism , Databases, Protein , Mytilus/metabolism , Proteome/metabolism , Proteomics , Amino Acid Sequence , Animals , Molecular Sequence Data , Mytilus/genetics , Proteome/genetics
3.
Fish Shellfish Immunol ; 41(2): 362-70, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25245621

ABSTRACT

Using reverse phase high performance liquid chromatography (RP-HPLC), a novel antimicrobial peptide with 55 amino acid residues was isolated from the hemolymph of Mytilus coruscus. This new antimicrobial peptide displays predominant antimicrobial activity against fungi and Gram-positive bacteria. The molecular mass and the N-terminal sequence of this peptide were analyzed by Mass Spectrometry and Edman degradation, respectively. This antimicrobial peptide, with molecular mass of 6621.55 Da, is characterized by a chitin-biding domain and by 6 Cysteine residues engaged in three intra-molecular disulfide bridges. The full-length of cDNA sequence of this new peptide was obtained by rapid amplification of cDNA ends (RACE) and the encoded precursor was turn out to be a chitotriosidase-like protein. Therefore, we named the precursor with mytichitin-1 and the new antimicrobial peptide (designated as mytichitin-CB) is the carboxyl-terminal part of mytichitin-1. The mRNA transcripts of mytichitin-1 are mainly detected in gonad and the expression level of mytichitin-1 in gonad was up-regulated and reached the highest level at 12 h after bacterial challenge, which was 9-fold increase compared to that of the control group. These results indicated that mytichitin-1 was involved in the host immune response against bacterial infection and might contribute to the clearance of invading bacteria.


Subject(s)
Antimicrobial Cationic Peptides/genetics , Antimicrobial Cationic Peptides/immunology , Chitin/metabolism , Hemolymph/metabolism , Mytilus/chemistry , Amino Acid Sequence , Animals , Antimicrobial Cationic Peptides/metabolism , Antimicrobial Cationic Peptides/pharmacology , Base Sequence , Chromatography, High Pressure Liquid , Cloning, Molecular , DNA Primers/genetics , DNA, Complementary/genetics , Fungi/drug effects , Gonads/metabolism , Gram-Positive Bacteria/drug effects , Likelihood Functions , Mass Spectrometry , Models, Genetic , Molecular Sequence Data , Protein Structure, Tertiary , Real-Time Polymerase Chain Reaction , Sequence Alignment , Sequence Analysis, DNA , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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