Functional and structural characterization of multiple galectins from the skin mucus of conger eel, Conger myriaster

Muramoto, Koji; Kagawa, D; Satō, Takashi; Ogawa, Tomoya; Nishida, Yoshihiro; Kamiya, Hisao

doi:10.1016/s0305-0491(99)00037-1

Cited by 71 publications

(41 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Analyses of mucus from several fish species, including eel, conger and rainbow trout, have revealed various lectin activities, suggesting a defensive role is played by some of the component molecules of the mucus (Hosono et al 1999, Muramoto et al 1999, Honda et al 2000, Buchmann 2001, although the specific functions of these lectin activities have not been fully elucidated. Epitopes from Myxobolus cerebralis myxospores contain so-called bisected N-acetyl-D-glucosamine.…”

Section: Discussionmentioning

confidence: 99%

“…Yet given the wide variety of environmental conditions faced and host adaptation over time to ward off parasite attack, the proteins and glycoconjugates of the parasite must also adapt over time if the organism is to survive. Fish immune systems are mainly based on non-specific immune responses (Ingram 1980) and frequently involve lectin activity in microbial defence (Hosono et al 1999, Muramoto et al 1999, Honda et al 2000. The immune system has to be able to effectively recognise parasite glycan epitopes, in order to provide some resistance to infection.…”

Section: Resale or Republication Not Permitted Without Written Consenmentioning

confidence: 99%

See 1 more Smart Citation

Lectin blot studies on proteins of Myxobolus cerebralis, the causative agent of whirling disease

Knaus¹,

El‐Matbouli²

2005

Dis. Aquat. Org.

View full text Add to dashboard Cite

It is known that Myxobolus cerebralis antigens, both surficial and secreted, are key modulators for, or targets of, host immune system compounds. We undertook SDS-PAGE glycoprotein characterisation of M. cerebralis developmental stages isolated from infected rainbow trout and Western blot analyses using selected biotin-labelled plant lectins (GSA-I, PHA-E, SJA, GSA-II) and anti-triactinomyxon polyclonal antibodies. Glycoproteins were isolated with lectin-affinity chromatography, and prominent bands were characterised by matrix-assisted laser desorption/ionisationmass spectrometry (MALDI/MS). We identified glycoproteins of M. cerebralis myxospores that contained carbohydrate motifs reactive with Phaseolus vulgaris erythroagglutinin (proteins 20 to 209 kDa, PHA-E), Sophora japonica agglutinin (proteins 7 to 70 kDa, SJA), Griffonia simplicifolia Agglutinin I (proteins 10 to 209 kDa, GSA-I) and G. simplicifolia Agglutinin II (proteins 5 to 40 kDa, GSA-II). Mcgp33, a glycoprotein isolated by lectin-affinity chromatography, was reactive with SJA (about 33 kDa). Antiserum produced against M. cerebralis triactinomyxons was found to have differences in the antigenicity of isolated glycoproteins from both M. cerebralis myxospores and actinospores. We also demonstrated modified antigen expression, especially involving the glycoprotein Mcgp33, in different developmental stages of M. cerebralis. KEY WORDS: Myxobolus cerebralis · Glycoprotein · Lectin · MALDI/MS · Lectin blotting · Oncorynchus mykiss · Myxozoa · Interaction Resale or republication not permitted without written consent of the publisherDis Aquat Org 65: [227][228][229][230][231][232][233][234][235] 2005 ments, both in host-tissue and in free-spore stages. The survival strategies of these parasites frequently involve the participation of glycoconjugates, which can be used to build protective structures and to facilitate hostparasite interactions. Yet given the wide variety of environmental conditions faced and host adaptation over time to ward off parasite attack, the proteins and glycoconjugates of the parasite must also adapt over time if the organism is to survive. Fish immune systems are mainly based on non-specific immune responses (Ingram 1980) and frequently involve lectin activity in microbial defence (Hosono et al. 1999, Muramoto et al. 1999, Honda et al. 2000. The immune system has to be able to effectively recognise parasite glycan epitopes, in order to provide some resistance to infection. To counter the host response, protozoans rely on antigen mimicry (Damian 1987, Inal 2004) and antigen variation (Borst et al. 1996, Rudenko et al. 1998, processes which involve surface glycoproteins such as glycoepitopes of N-glycosides (Burghaus et al. 1999, Yang et al. 1999 and O-glycosides (Dieckmann-Schuppert et al. 1993, Khan et al. 1997. In Trypanosoma brucei (Borst et al. 1996, Ferguson 1997, 1999 and Giardia lamblia (Gillin et al. 1990, Gillin & Reiner 1996, Nash 1992, a variant surface glycoprotein (VSG) is expressed sequentially to evade the ...

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Resale or Republication Not Permitted Without Written Consenmentioning

confidence: 99%

Lectin blot studies on proteins of Myxobolus cerebralis, the causative agent of whirling disease

Knaus¹,

El‐Matbouli²

2005

Dis. Aquat. Org.

View full text Add to dashboard Cite

show abstract

“…In the conger eel, the amino acid sequences of congerins I and II found in the skin mucus were determined as ␤-galactosidespecific lectins (24,25). Congerins I and II belong to the galectin family based on primary structure and thus show no homology with AJL-2.…”

Section: Discussionmentioning

confidence: 99%

“…Purification of skin mucus lectins has been performed for many species of fish including the windowpane flounder Lophopsetta maculata (17), the Arabian Gulf catfish Arius thalassinus (18), the conger eel Conger myriaster (19,20), the dragonet Repomucenus richardsonii (21), the loach Misgurnus anguillicaudatus (22), and the kingklip Genypterus capensis (23). Among these lectins, the primary structures were determined in the conger eel only for galectins referred to as congerins I and II (24,25). The structural sequences for skin mucus lectins in animal groups other than fish are also limited and have been reported in only two species, the land slug Incilaria fruhstorferi (26) and the African clawed frog Xenopus laevis (27).…”

mentioning

confidence: 99%

Primary Structure and Characteristics of a Lectin from Skin Mucus of the Japanese Eel Anguilla japonica

Tasumi¹,

Ohira²,

Kawazoe³

et al. 2002

Journal of Biological Chemistry

160

View full text Add to dashboard Cite

Two types of lactose-binding lectins, AJL-1 and AJL-2, were purified from the skin mucus extract of the Japanese eel Anguilla japonica by lactose affinity chromatography and subsequent gel filtration. The molecular masses of AJL-1 and AJL-2 were 16,091 and 31,743 Da, respectively. Intact AJL-1 was comprised of two identical 16-kDa subunits having blocked N termini and no disulfide bonds. AJL-2 was a homodimer with disulfide bonds. Based on the N-terminal amino acid sequence of the AJL-2 monomer, the nucleotide sequence of cDNA encoding this lectin was determined by 3-and 5-rapid amplification of cDNA ends. The deduced amino acid sequence showed ϳ30% homology with C-type lectins, which bind to carbohydrates in a Ca 2؉ -dependent manner. In addition, AJL-2 exhibited highly conserved consensus amino acid residues of the C-type carbohydrate recognition domain, although this lectin showed Ca 2؉ -independent activity. Gene expression of AJL-2 was detected only in the skin by Northern blot analysis, and this lectin localization was demonstrated in the club cells by immunohistochemistry. These results indicate that AJL-2 is secreted on the body surface and function as a component of skin mucus. AJL-2 agglutinated Escherichia coli and suppressed its growth, suggesting that this lectin is involved in host defense.Lectins, which are carbohydrate-binding proteins that are not antibodies and enzymes (1, 2), are found widely distributed in bacteria, plants, and animals. Based on the structure of the carbohydrate recognition domain (CRD), 1 animal lectins are classified as C-type (3), galectin (4, 5), P-type (6), or I-type (7); in addition, heparin-binding proteins (8) and pentraxin (9, 10) have been identified. Among these, C-type lectins form a diverse group of proteins including collectins (11, 12) and selectins and are characterized by their Ca 2ϩ -dependent activity. The functioning of animal lectins vary widely because they are involved in cell-cell interactions, protein trafficking, and primitive defense reactions (6, 13-16).Most known animal lectins are found to exist internally, but some are also found in the skin mucus of several animal species, especially in fish. However, knowledge concerning the structure and functioning of such molecules remains limited. Purification of skin mucus lectins has been performed for many species of fish including the windowpane flounder Lophopsetta maculata (17), the Arabian Gulf catfish Arius thalassinus (18), the conger eel Conger myriaster (19,20), the dragonet Repomucenus richardsonii (21), the loach Misgurnus anguillicaudatus (22), and the kingklip Genypterus capensis (23). Among these lectins, the primary structures were determined in the conger eel only for galectins referred to as congerins I and II (24, 25). The structural sequences for skin mucus lectins in animal groups other than fish are also limited and have been reported in only two species, the land slug Incilaria fruhstorferi (26) and the African clawed frog Xenopus laevis (27). The precise biological roles of skin mu...

show abstract

“…So far, sequences of mucosal lectins have been determined in only two species of the Anguilliformes, namely the conger (congerin I and II) and the Japanese eel (AJL-2). Congerin I and II were classified as galectins (18,19); this class probably dominates among the skin mucus lectins because many of them interact specifically with galactose or lactose. On the other hand, AJL-2 has a sequence typical of C-type lectins (16).…”

mentioning

confidence: 99%

Lectins Homologous to Those of Monocotyledonous Plants in the Skin Mucus and Intestine of Pufferfish, Fugu rubripes

Tsutsui

Tasumi²,

Suetake

et al. 2003

Journal of Biological Chemistry

101

View full text Add to dashboard Cite

We have characterized pufflectin, a novel mannosespecific lectin, from the skin mucus of the pufferfish, Fugu rubripes. Molecular mass estimations by gel filtration and matrix-assisted laser desorption ionization time-of-flight mass spectrometry and the SDS-PAGE pattern suggest that pufflectin is a homodimer composed of non-covalently associated subunits of 13 kDa. The full-length pufflectin cDNA consists of 527 bp, with 116 amino acid residues deduced from the open reading frame. The amino acid sequence of pufflectin shows no homology with any known animal lectin. Surprisingly, pufflectin shares sequence homology with mannosebinding lectins of monocotyledonous plants and has conserved two of three carbohydrate recognition domains of these plant lectins. The pufflectin gene is expressed in gills, oral cavity wall, esophagus, and skin. In addition, an isoform occurs exclusively in the intestine. Pufflectin differs from mannose-binding lectins purified from the blood plasma of Fugu. Whereas pufflectin did not agglutinate five bacterial species tested, it was demonstrated to bind to the parasitic trematode, Heterobothrium okamotoi. This finding suggests that pufflectin contributes to the parasite-defense system in Fugu.

show abstract

Functional and structural characterization of multiple galectins from the skin mucus of conger eel, Conger myriaster

Cited by 71 publications

References 50 publications

Lectin blot studies on proteins of Myxobolus cerebralis, the causative agent of whirling disease

Lectin blot studies on proteins of Myxobolus cerebralis, the causative agent of whirling disease

Primary Structure and Characteristics of a Lectin from Skin Mucus of the Japanese Eel Anguilla japonica

Lectins Homologous to Those of Monocotyledonous Plants in the Skin Mucus and Intestine of Pufferfish, Fugu rubripes

Contact Info

Product

Resources

About