Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.)

Savan, Ram; Aman, Azumi; Sakai, Masahiro

doi:10.1016/s1050-4648(02)00159-6

Cited by 50 publications

(33 citation statements)

References 9 publications

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“…Fish, in addition to mammals and birds, also synthesise lysozyme g [16]. The lysozyme g protein synthesised by the Japanese flounder, orange-spotted grouper and common carp shows similarity to the predicted protein sequence for chicken lysozyme g2 reported here, in that they lack a signal peptide and the cysteines necessary for disulphide bond formation [19][20][21]. Chicken g2, together with flounder and grouper lysozyme g, retains the triad of conserved glutamic and aspartic acid residues critical to lysozyme catalytic activity, and recombinant flounder and grouper lysozyme g demonstrate classical lysozyme lytic activity against Micrococcus lysodeikticus and other bacteria [19,20].…”

Section: Discussionsupporting

confidence: 51%

“…The protein includes the triad of conserved glutamic and aspartic acid residues critical to lysozyme catalytic activity, but the four conserved cysteines involved in disulphide bond formation of the mammalian and bird lysozyme g proteins are absent. Chicken lysozyme g2 shows considerable homology with type-G lysozymes isolated from fish [19][20][21] and in particular lacks a predicted signal peptide sequence.…”

Section: In Silico Identification Of a Novel Chicken Lysozyme G2mentioning

confidence: 99%

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Identification of chicken lysozyme g2 and its expression in the intestine

Nile

Townes

Michailidis

et al. 2004

CMLS, Cell. Mol. Life Sci.

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Lysozyme is an important component of the innate immune system, protecting the gastrointestinal tract from infection. The aim of the present study was to determine if lysozyme is expressed in the chicken ( Gallus gallus) intestine and to characterise the molecular forms expressed. Immunohistochemical staining localised lysozyme to epithelial cells of the villous epithelium along the length of the small intestine. There was no evidence for lysozyme expression in crypt epithelium and no evidence for Paneth cells. Immunoblots of chicken intestinal protein revealed three proteins: a 14-kDa band consistent with lysozyme c, and two additional bands of approximately 21 and 23 kDa, the latter consistent with lysozyme g. RT-PCR analyses confirmed that lysozyme c mRNA is expressed in 4-day, but not older chicken intestine and lysozyme g in 4- to 35-day chicken intestine. A novel chicken lysozyme g2 gene was identified by in silico analyses and mRNA for this lysozyme g2 was identified in the intestine from chickens of all ages. Chicken lysozyme g2 shows similarity with fish lysozyme g, including the absence of a signal peptide and cysteines involved in disulphide bond formation of the mammalian and bird lysozyme g proteins. Analyses using SecretomeP predict that chicken lysozyme g2 may be secreted by the non-classical secretory pathway. We conclude that lysozyme is expressed in the chicken small intestine by villous enterocytes. Lysozyme c, lysozyme g and g2 may fulfil complimentary roles in protecting the intestine.

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Section: Discussionsupporting

confidence: 51%

Section: In Silico Identification Of a Novel Chicken Lysozyme G2mentioning

confidence: 99%

Identification of chicken lysozyme g2 and its expression in the intestine

Nile

Townes

Michailidis

et al. 2004

CMLS, Cell. Mol. Life Sci.

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“…Based on primary structure, three major classes of animal lysozymes have been identified. Although the overall sequence similarity between lysozymes of different classes is low, they share a similar overall three-dimensional structure [1,2], and they have been proposed to have common ancestry [3][4][5]. Phylogenetic studies indicate that several major groups of animals produce lysozymes of two different classes, or at least have the open reading frames potentially encoding them [6].…”

Section: Introductionmentioning

confidence: 99%

Identification of a bacterial inhibitor against g-type lysozyme

Vanderkelen

Herreweghe

Vanoirbeek

et al. 2010

Cell. Mol. Life Sci.

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Lysozymes are antibacterial effectors of the innate immune system in animals that hydrolyze peptidoglycan. Bacteria have evolved protective mechanisms that contribute to lysozyme tolerance such as the production of lysozyme inhibitors, but only inhibitors of chicken (c-) and invertebrate (i-) type lysozyme have been identified. We here report the discovery of a novel Escherichia coli inhibitor specific for goose (g-) type lysozymes, which we designate PliG (periplasmic lysozyme inhibitor of g-type lysozyme). Although it does not inhibit c- or i-type lysozymes, PliG shares a structural sequence motif with the previously described PliI and MliC/PliC lysozyme inhibitor families, suggesting a common ancestry and mode of action. Deletion of pliG increased the sensitivity of E. coli to g-type lysozyme. The existence of inhibitors against all major types of animal lysozyme and their contribution to lysozyme tolerance suggest that lysozyme inhibitors may play a role in bacterial interactions with animal hosts.

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“…These restricted distribution patterns in birds and mammals contrasted with the broad expression patterns of g-type lysozymes in fish and invertebrate species. G-type lysozymes have been detected in the spleen, kidneys, gills, skin, heart, intestines and blood of Japanese flounder, orange-spotted grouper, large yellow croaker, Atlantic cod and grass carp (Hikima et al, 2001;Savan et al, 2003;Yin et al, 2003;Zheng et al, 2007), as well as in the gills, mantle, hepatopancreas, hemocytes and muscles in Mytilus galloprovincialis (Wang et al, 2012). Real-Time analysis has shown that C. intestinalis g-type lysozymes are upregulated in the pharynx after LPS challenge, in particular, CiLys-g1, CiLys-g2 and CiLys-g3 gene expression were significantly boosted at 24e72 h, while CiLys-g4 gene expression was significantly boosted at 1 h and 2e4 h and decreased at 8e48 h, supporting a defensive role for CiLys-g lysozymes.…”

Section: Discussionmentioning

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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Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.)

Cited by 50 publications

References 9 publications

Identification of chicken lysozyme g2 and its expression in the intestine

Identification of chicken lysozyme g2 and its expression in the intestine

Identification of a bacterial inhibitor against g-type lysozyme

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

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