Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins

Zhang, Shu H.; Zhu, Dan; Chang, Ming Xian; Zhao, Qin; Jiao, Ran; Huang, Bei; Fu, Jian; Liu, Zhi X.; Nie, Pin

doi:10.1016/j.dci.2011.06.014

Cited by 23 publications

(14 citation statements)

References 30 publications

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“…G-type lysozyme in Asian seabass possesses a GEWL domain with conserved residues essential for catalytic activity, which exists in most fish species, bivalves as well as birds and mammals [8,44]. However, it has been discovered that g-type lysozyme in molluscs shared one conserved cysteine with those from birds and mammals, and six conserved cysteines were observed in molluscs g-type lysozymes, with two unique cysteines in the g-type lysozyme of O. hupensis [18]. Thus, the conserved residues in the lysozymes of Asian seabass are expected to have similar catalytic activity with those of other fish and avian species.…”

Section: Discussionmentioning

confidence: 99%

“…The expressions of the lysozyme genes were positively regulated by bacterial infection, which suggests an involvement of lysozymes in the anti-microbial defense in fish [12,15]. The recombinant proteins of two types of lysozymes purified from Escherichia coli show antimicrobial activity against Vibrio anguillarum [14] in Japanese flounder, Aeromonas hydrophila , Vibrio fluvialis , Aeromonas sobria and Micrococcus lysodeikticus , in gastropod Oncomelania hupensis [18], V. anguillarum or M lysodeikticus in Mediterranean mussel [19], V. splendidus and V.parahaemolyticus in Chlamys farreri [8], as well as Vibrio alginolyticus and Vibrio parahemolyticus in shrimp [20]. …”

Section: Introductionmentioning

confidence: 99%

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Analysis of Two Lysozyme Genes and Antimicrobial Functions of Their Recombinant Proteins in Asian Seabass

Bai

Xia

et al. 2013

PLoS ONE

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Lysozymes are important proteins of the innate immune system for the defense against bacterial infection. We cloned and analyzed chicken-type (c-type) and goose-type (g-type) lysozymes from Asian seabass (Lates calcarifer). The deduced amino acid sequence of the c-type lysozyme contained 144 residues and possessed typical structure residues, conserved catalytic residues (Glu50 and Asp67) and a “GSTDYGIFQINS” motif. The deduced g-type lysozyme contained 187 residues and possessed a goose egg white lysozyme (GEWL) domain containing three conserved catalytic residues (Glu71, Asp84, Asp95) essential for catalytic activity. Real time quantitative PCR (qRT-PCR) revealed that the two lysozyme genes were constitutively expressed in all the examined tissues. The c-type lysozyme was most abundant in liver, while the g-type lysozyme was predominantly expressed in intestine and weakly expressed in muscle. The c-type and g-type transcripts were up-regulated in the kidney, spleen and liver in response to a challenge with Vibrio harveyi. The up-regulation of the c-type lysozyme was much stronger than that of the g-type lysozyme in kidney and spleen. The recombinant proteins of the c-type and g-type lysozymes showed lytic activities against the bacterial pathogens Vibrio harveyi and Photobacterium damselae in a dosage-dependent manner. We identified single nucleotide polymorphisms (SNPs) in the two lysozyme genes. There were significant associations of these polymorphisms with resistance to the big belly disease. These results suggest that the c- and g-type genes play an important role in resistance to bacterial pathogens in fish. The SNP markers in the two genes associated with the resistance to bacterial pathogens may facilitate the selection of Asian seabass resistant to bacterial diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Analysis of Two Lysozyme Genes and Antimicrobial Functions of Their Recombinant Proteins in Asian Seabass

Bai

Xia

et al. 2013

PLoS ONE

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“…The g-type lysozyme (gLYZ) was initially identified in geese egg white [19]–[21], and was later found to exist in fishes, mammals, urochordates and invertebrates [2], [22]–[25]. Most of the investigated animals were reported to possess only one type of gLYZ.…”

Section: Introductionmentioning

confidence: 99%

“…Most of the investigated animals were reported to possess only one type of gLYZ. Recently, multiple gLYZ genes had been reported in mouse and human, zebra fish, larvacean Oikopleura dioica and gastropod Oncomelania hupensis [22]–[23], [25]. Nelson et al speculated that the multiple gLYZs in urochordates had been specialized, and the biochemically significant wide range of pI of the gLYZs in these animals may support this assumption [23].…”

Section: Introductionmentioning

confidence: 99%

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

Wang¹,

Zhang²,

Zhao

et al. 2012

PLoS ONE

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Two goose-type lysozymes (designated as MGgLYZ1 and MGgLYZ2) were identified from the mussel Mytilus galloprovincialis. MGgLYZ1 mRNA was widely expressed in the examined tissues and responded sensitively to bacterial challenge in hemocytes, while MGgLYZ2 mRNA was predominately expressed and performed its functions in hepatopancreas. However, immunolocalization analysis showed that both these lysozymes were expressed in all examined tissues with the exception of adductor muscle. Recombinant MGgLYZ1 and MGgLYZ2 could inhibit the growth of several Gram-positive and Gram-negative bacteria, and they both showed the highest activity against Pseudomonas putida with the minimum inhibitory concentration (MIC) of 0.95–1.91 µM and 1.20–2.40 µM, respectively. Protein sequences analysis revealed that MGgLYZ2 had lower isoelectric point and less protease cutting sites than MGgLYZ1. Recombinant MGgLYZ2 exhibited relative high activity at acidic pH of 4–5, while MGgLYZ1 have an optimum pH of 6. These results indicated MGgLYZ2 adapted to acidic environment and perhaps play an important role in digestion. Genomic structure analysis suggested that both MGgLYZ1 and MGgLYZ2 genes are composed of six exons with same length and five introns, indicating these genes were conserved and might originate from gene duplication during the evolution. Selection pressure analysis showed that MGgLYZ1 was under nearly neutral selection while MGgLYZ2 evolved under positive selection pressure with three positively selected amino acid residues (Y102, L200 and S202) detected in the mature peptide. All these findings suggested MGgLYZ2 perhaps served as a digestive lysozyme under positive selection pressure during the evolution while MGgLYZ1 was mainly involved in innate immune responses.

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“…The g-type lysozyme was initially identified as an antibacterial enzyme in egg whites from the Embden goose (Canfield and McMurry, 1967), but it was later found to exist in the egg whites of several other bird species (Prager et al, 1974). More recently, the g-type lysozyme has been identified in vertebrate species, including mammals (Nakano and Graf, 1991), fish (Mohanty and Sahoo, 2010), urochordates (Nilsen et al, 2003) and molluscs (Zhao et al, 2007;Zhang et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis

Falco

Cammarata

Vizzini

2017

Developmental & Comparative Immunology

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a b s t r a c tLysozyme is an important defense molecule of the innate immune system. Known for its bactericidal properties, lysozyme catalyzes the hydrolysis of b-(1,4)-glycosidic bonds between the N-acetyl glucosamine and N-acetyl muramic acid in the peptidoglycan layer of bacterial cell walls. In this study, the complete coding sequence of four g-type lysozymes were identified in Ciona intestinalis. Phylogenetic analysis and modelling supported the hypothesis of a close relationship with the vertebrate g-type lysozymes suggesting that the C. intestinalis g-type lysozyme genes (CiLys-g1, Cilys-g2, CiLys-g3, CiLys-g4) share a common ancestor in the chordate lineage. Protein motif searches indicated that C. intestinalis gtype lysozymes contain a GEWL domain with a GXXQ signature, typical of goose lysozymes. Quantitative Real-Time PCR analysis results showed that transcripts are expressed in various tissues from C. intestinalis. In order to determine the involvement of C. intestinalis g-type lysozymes in immunity, their expression was analyzed in the pharynx, showing that transcripts were significantly up-regulated in response to a challenge with lipopolysaccharide (LPS). These data support the view that CiLys g-type are molecules with potential for immune defense system against bacterial infection.

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Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins

Cited by 23 publications

References 30 publications

Analysis of Two Lysozyme Genes and Antimicrobial Functions of Their Recombinant Proteins in Asian Seabass

Analysis of Two Lysozyme Genes and Antimicrobial Functions of Their Recombinant Proteins in Asian Seabass

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis

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