A bifunctional invertebrate-type lysozyme from the disk abalone, Haliotis discus discus: Genome organization, transcriptional profiling and biological activities of recombinant protein

Bathige, S.D.N.K.; Umasuthan, Navaneethaiyer; Kasthuri, Saranya Revathy; Whang, Ilson; Lim, Bong-Soo; Nam, Bo‐Hye

doi:10.1016/j.dci.2013.06.009

Cited by 29 publications

(12 citation statements)

References 60 publications

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“…C‐type lysozyme was found in Haliotis discus discus ; its gene was upregulated after bacterial and virus challenge indicating that it is involved in abalone immune response (Bathige et al . ). Up to three different lysozymes were found in oysters C. virginica , all of them inhibit the growth of Gram‐positive and Gram‐negative bacteria (Xue et al .…”

Section: Discussionmentioning

confidence: 97%

Protein expression profiling in haemocytes and plasma of the Manila clam Ruditapes philippinarum in response to infection with Perkinsus olseni

Fernández-Boo

Villalba

Cao

2016

Journal of Fish Diseases

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The protein expression profiling in clam haemocytes and plasma in response to Perkinsus olseni was addressed. Adult Manila clams from a P. olseni-free bed were experimentally challenged with parasite zoospores to analyse immune response. In another experiment, the effects of longer term infection were assessed in adult clams collected from a P. olseni-affected bed, by comparing moderate to very heavily infected clams with non-infected ones. Haemocyte and plasma proteins were separated by two-dimensional electrophoresis; spot patterns were qualitatively compared between treatments within each experiment and the spots indicating differential protein expression associated with P. olseni challenge or with field infection were processed for protein identification. Fifteen clam proteins (four in haemocytes and eleven in plasma) of which expression was markedly affected by P. olseni were identified. Some of the identified proteins have a well-known role in clam immune response against the parasite, such as lysozyme and lectins. Rho GTPase-activating protein 6 could be a marker of resistance against P. olseni, which should be further studied.

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Section: Discussionmentioning

confidence: 97%

Protein expression profiling in haemocytes and plasma of the Manila clam Ruditapes philippinarum in response to infection with Perkinsus olseni

Fernández-Boo

Villalba

Cao

2016

Journal of Fish Diseases

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“…The optimal temperature for relative enzyme activity of the three recombinant lysozymes from Branchiostoma japonicum is 50°C, all three lysozymes displaying maximum activity at pH 5.0 . A lysozyme from H. discus discus has been shown to exert optimal lysozyme activity at pH 4.0 and the optimal temperatures for purified lysozyme are 60°C and 75°C . The relative optimal enzyme activity of recombinant CpLYZ1 from C. plicata is reportedly at pH 5.5 and 50°C .…”

Section: Discussionmentioning

confidence: 97%

Molecular cloning and functional characterization of a novel i‐type lysozyme in the freshwater mussel Cristaria plicata

Dai

Zhang³

et al. 2015

Microbiology and Immunology

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The freshwater bivalve Cristaria plicata, which is widely distributed in Eastern Asia, is a key species in the pearl culture industry. In this study, a novel invertebrate-type lysozyme, designated as CpLYZ2, was cloned from hemocytes of C. plicata. This lysozyme shares high sequence identity and is homologous to a previously identified lysozyme CpLYZ1 isolated from C. plicata and with HcLyso3 isolated from Hyriopsis cumingii. The full-length cDNA of CpLYZ2 is 913 bp long, which includes an open reading frame (ORF) of 486 bp, a 3 0 untranslated region (UTR) of 389 bp and a 5 0 UTR of 38 bp. The ORF encodes a putative polypeptide of 161 amino acids with a predicted molecular mass of 18.2 kDa and a theoretical isoelectric point of 6.56. CpLYZ2 mRNA transcripts can be detected in hemocytes, hepatopancreas, muscle, gills and mantle tissues, the greatest expression being observed in the gills. CpLYZ2 expression in hemocytes, hepatopancreas and gills increased significantly after the mussel was challenged with Aeromonas hydrophila. Furthermore, the optimal pH and temperature for enzyme activity of the recombinant CpLYZ2 were 5.5 and 50°C, respectively. The recombinant lysozyme protein exhibited bacteriolytic activity against Escherichia coli, A. hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis. The findings of this study help to elucidate immune responses in molluscs and will thus expedite disease management of these key freshwater species, in turn boosting pearl culture in eastern Asia.

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“…The molecular basis for this difference is unknown. Furthermore, lysozymes also exhibit isopeptidase activity (Josková et al, 2009;Bathige et al, 2013). The difference in optimum pH for lysozyme and isopeptidase activity may indicate that these activities are executed by independent active sites within the molecule.…”

Section: Lysozymesmentioning

confidence: 95%

Mucosal Immunity in Invertebrates

Bilej

2015

Mucosal Immunology

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A bifunctional invertebrate-type lysozyme from the disk abalone, Haliotis discus discus: Genome organization, transcriptional profiling and biological activities of recombinant protein

Cited by 29 publications

References 60 publications

Protein expression profiling in haemocytes and plasma of the Manila clam Ruditapes philippinarum in response to infection with Perkinsus olseni

Protein expression profiling in haemocytes and plasma of the Manila clam Ruditapes philippinarum in response to infection with Perkinsus olseni

Molecular cloning and functional characterization of a novel i‐type lysozyme in the freshwater mussel Cristaria plicata

Mucosal Immunity in Invertebrates

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