Purification and Characterization of Glycoprotein from the Skin Mucus of the Rainbow Trout,<i>Salmo gaivdneri</i>

Sumi, Toshihisa; Hama, Yoichiro; Maruyama, Daisuke; Asakawa, Makio; Nakagawa, Hiroki

doi:10.1271/bbb.61.675

Cited by 10 publications

(14 citation statements)

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“…This result is clearly related to previous studies on epizootiology of VSE, which demonstrated that gills are the main portal of entry (Marco‐Noales et al ., 2001) as well as representing the organ where bacteria persist after infection (Valiente and Amaro, 2006). From the different proteins present in mucus surrounding epithelial tissues, mucin is one of the most conserved and abundant (Sumi et al ., 1997). In fact, the gill mucin from eels has been chemically characterized as a glycoprotein, similar to other mammalian mucins (Sumi et al ., 2004).…”

Section: Discussionmentioning

confidence: 99%

Role of the metalloprotease Vvp and the virulence plasmid pR99 of Vibrio vulnificus serovar E in surface colonization and fish virulence

Valiente¹,

Lee²,

Hor³

et al. 2007

Environmental Microbiology

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The virulence for eels of Vibrio vulnificus biotype 2 serovar E (VSE) is conferred by a plasmid that codifies ability to survive in eel serum and cause septicaemia. To find out whether the plasmid and the selected chromosomal gene vvp plays a role in the initial steps of infection, the VSE strain CECT4999, the cured strain CT218 and the Vvp-deficient mutant CT201 (obtained in this work by allelic exchange) were used in colonization and virulence experiments. The eel avirulent biotype 1 (BT1) strain YJ016, whose genome has been sequenced, was used for comparative purposes. The global results demonstrate that the plasmid does not play a significant role in surface colonization because (i) CECT4999 and CT218 were equally chemoattracted towards and adherent to eel mucus and gills, and (ii) CT218 persisted in gills from bath-infected eels 2 weeks post infection. In contrast, mutation in vvp gene reduced significantly chemoattraction and attachment to eel mucus and gills, as well as virulence degree by immersion challenge. Co-infection experiments by bath with CECT4999 and CT201 confirmed that Vvp was involved in eel colonization and persistence in gills, because CECT4999 was recovered at higher numbers compared with CT201 from both internal organs of moribund fish (ratio 4:1) and gills from survivors (ratio 50:1). Interestingly, YJ016 also showed chemoattraction and attachment to mucus, and complementation of CT201 with BT1-vvp gene restored both activities together with virulence degree by immersion challenge. Additional experiments with algae mucus and purified mucin gave similar results. In conclusion, the protease Vvp of V. vulnificus seems to play an essential role in colonization of mucosal surfaces present in aquatic environments. Among the V. vulnificus strains colonizing fish mucus, only those harbouring the plasmid could survive in blood and cause septicaemia.

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Section: Discussionmentioning

confidence: 99%

Role of the metalloprotease Vvp and the virulence plasmid pR99 of Vibrio vulnificus serovar E in surface colonization and fish virulence

Valiente¹,

Lee²,

Hor³

et al. 2007

Environmental Microbiology

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“…Mucous glycoproteins that are mucin‐type glycoproteins are considered to be the most important constituent of the mucous coat. In previous studies rainbow trout skin mucous glycoprotein was shown to have many NeuAc‐containing disaccharide chains (Sumi et al ., 1997, 2002) and in contrast loach skin mucous glycoprotein had many KDN‐containing oligosaccharide chains (Kimura et al ., 1994).…”

Section: Discussionmentioning

confidence: 99%

“…The existence of the carbohydrate chain suggested that the substrate specificity of NeuAc transferase was not so strict. NeuAcα2→6(GalNAcα1→3)GalNAc which was the original trisaccharide of E‐2‐I was detected from human rectal adenocarcinoma (Kurosaka et al ., 1983), bovine submaxillary mucin (Savage et al ., 1990), human menconium (Capon et al ., 1989) and rainbow trout skin mucous glycoprotein (Sumi et al ., 2002). The existence of NeuAcα2→6(GalNAcα1→3) GalNAc in EGP is interesting, because the same carbohydrate chain was isolated from human cancer tissues despite no detection in normal human tissues.…”

Section: Discussionmentioning

confidence: 99%

“…Carbohydrate components were determined as trimethylsilyl derivatives by GLC after methanolysis under strong or mild conditions as described by Yu & Ledeen (1970) and Sumi et al . (1997).…”

Section: Methodsmentioning

confidence: 99%

“…It has been shown that the fish mucous secretions contain mucin‐type glycoproteins with carbohydrate compositions similar to that of the mammalian epithelial secretions (Buddecke, 1972; Faillard & Schauer, 1972). Previous studies on the mucous glycoproteins of loach Misgumus anguillicaudatus (Cantor)(Kimura et al ., 1994), Japanese eel Anguilla japonica Temminck & Schlegel (Asakawa, 1974, 1977, 1983), rainbow trout Oncorhynchus mykiss (Walbaum)(Sumi et al ., 1997, 2002) and several other species of fishes (Nakagawa et al ., 1988) revealed that different species of fishes secrete specific mucous glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Purification and further characterization of a glycoprotein from the skin mucus of Japanese eels

Sumi¹,

Hama²,

Nakagawa³

et al. 2004

Journal of Fish Biology

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A glycoprotein (EGP) was purified from the skin mucus of Japanese eel Anguilla japonica. Apparent average molecular mass of the EGP was estimated to be 500 000. The EGP was found to contain 30Á8% NeuAc, 26Á4% GalNAc, 6Á4% Gal, 0Á4% NeuGc and 25Á1% Thr-rich protein.EGP was treated with alkaline borohydride for the release of carbohydrate chains (oligosaccharide alditols). Three carbohydrate chains were isolated from the released carbohydrate chains by Sephadex G-25 (superfine) gel filtration and HPLC. Using 1 H-NMR spectroscopy, methylation analysis and glycosidase digestion, the structures of the three carbohydrate chains were determined to be NeuAca2!6GalNAc-ol, NeuAca2!3GalNAc-ol and NeuAca2!6(GalNAca1!3)GalNAc-ol. An overall structure for the sialoglycoprotein from the skin mucus is proposed: the molecule is considered to consist of highly glycosylated 10 glycopeptide units (containing >40 carbohydrate chains) that are linked to the hydroxyl amino acids and spaced on average two amino acids apart. # 2004 The Fisheries Society of the British Isles

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Kdn-Containing Glycoprotein from Loach Skin Mucus

Nakagawa

Hama

Sumi

et al. 2001

The Molecular Immunology of Complex Carbohydrates —2

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Purification and Characterization of Glycoprotein from the Skin Mucus of the Rainbow Trout,Salmo gaivdneri

Cited by 10 publications

References 1 publication

Role of the metalloprotease Vvp and the virulence plasmid pR99 of Vibrio vulnificus serovar E in surface colonization and fish virulence

Role of the metalloprotease Vvp and the virulence plasmid pR99 of Vibrio vulnificus serovar E in surface colonization and fish virulence

Purification and further characterization of a glycoprotein from the skin mucus of Japanese eels

Kdn-Containing Glycoprotein from Loach Skin Mucus

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