• Fisheries and Aquatic Sciences
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• v.1 no.2
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• pp.250-254
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• 1998

Harmful micro algae isolated from Korean coastal waters, were tested with FITC-conjugated lectins and observed by epifluorescent microscopy to distinguish each other. Strain-specific sugar composition at the cell surface was suggested by the affinity of lectins to different microalgae. The micro algae Cochlodinium polykrikoides (CP-1) and Gymnodinium $A_3\;(GA_{3-1}\;1)$, are morphologically similar, but exhibited different binding activity with the lectins ECA, HPA and WGA. In Peridiniales, the micro alga Alexandrium tamarense (AT) bound HPA and WGA, but Scrippsiella trochoidea (ST-1) did not bind those lectins. Three species of Prorocentrum also exhibited different binding specificity with HPA, PHA and SBA. A non­toxic Korean isolate of Heterosigma akashiwo (HA-2) bound ConA, PEA and UEA. These results suggest that lectins are useful in discriminating morphologically similar species, as well as different species or strains within the same genus.

• Archives of Pharmacal Research
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• v.9 no.4
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• pp.201-203
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• 1986

Forty species of marine shells were collected from Korean coasts and studied extensively for their lectin activities by using erythrocytes of human blooc A, AB, B. O group and rabbit blood. In total, 7 species contained lectines :Neptunea intersculpta, Omphalius nigerrimus and Scapharca subcrenata, blood group nonspecific; Saxidomus purpuratus, human blood A and AB group specific; Lepidozona coreana, Tegilarca granosa and Neptunea polycosta, rabbit blood specific.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.213.2-214
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• 2003

Three mistletoe lectins (ML -I, ML -IIU, ML -IIL) have been identified in Europe based on sugar specificities for galactose(Gal) and N-acetyl galactosamine(GalNAc). Korean mistletoe lectins have been known as mainly ML -II type. In previous results, we suggested that there are two lectins, 64 KDa and 60 KDa, in Korean mistletoe lectin (KML -C). (omitted)

• BMB Reports
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• v.38 no.3
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• pp.370-372
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• 2005

A cross-linked leucaena (Leucaena leucocephala) seed gum (CLLSG) matrix was prepared for the isolation of galactose-specific lectins by affinity chromatography. The matrix was evaluated for affinity with a known galactose-specific lectin from the seeds of snake gourd (Trichosanthes anguina). The matrix preparation was simple and inexpensive when compared to commercial galactose-specific matrices (i.e. about 1.5 US$/100 ml of matrix). The current method is also useful for the demonstration of the affinity chromatography technique in laboratories. Since leucaena seeds are abundant and inexpensive, and the matrix preparation is easy, CLLSG appears to be a promising tool for the separation of galactose-specific lectins.

• Journal of fish pathology
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• v.29 no.1
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• pp.13-23
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• 2016

Lectins play significant roles in the innate immune responses through binding to pathogen-associated molecular patterns (PAMPs) on the surfaces of microorganisms. In the present study, tissue distribution and expression analysis of olive flounder lectins were performed after viral hemorrhagic septicemia virus (VHSV) challenge. Fish egg lectin and serum lectin were found to be predominantly expressed in the gills and liver, these results indicate that the transcript expression of olive flounder lectins is concentrated in immune-related tissues. Following a VHSV challenge, an overall increase in the transcript levels of the genes was observed and the expression patterns were distinctly divided into early and later responses during VHSV infection. In conclusion, olive flounder lectins are specifically expressed in immune-related organs and induced in both the immediate and long-lasting immune responses to VHSV in the olive flounder. These results indicate that lectins may be play important roles in the host defense mechanism and involved in the innate and adaptive immune response to viruses in fish.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2000.05a
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• pp.530-530
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• 2000

The host defense system or immune system of all modern animals has their roots in very ancient organisms. After analyzing literature data concerning properties of invertebrates and vertebrates lectins we suggest that mechanism of mannans recognition may exist in marine invertebrates, as a universal mechanism for homeostasis maintenance and host defense, and mannan-binding lectins family of vertebrates has ancient precursor, as was shown for another S-type lectins family. We carried out the screening of mannan-binding type lectin among different species of echinoderms inhabiting in Piter the Grate Bay, the sea of Japan. As a result, the C-type lectins (SJL-32) specific for high mannose glycans was isolated from the coelomic plasma of the sea cucumbers Stichopus japonicus by ion-exchange chromatography on a DEAE-Toyopearl 650M, affinity chromatography on a mannan-Sepharose 6B and gel filtration on a Sephacryl S-200. SJL-32 is homodimer with molecular mass about 32 kDa on SDS-PAGE under non-reducing conditions. Protein part of the lectin has high conteins Asn, Glu, Ser. Hemagglutination of trypsin-treated O blood group human erythrocytes by SJL-32 was competitively inhibited by high-branched -D-mannan composed of -1,2 and -1,6 linked D-mannopyranose residues. In contrast, a variety of mono-, oligo-, and polysaccharides composed of residues of galactose and fucose showed absence or little inhibitory activities. The lectin activity strong depends on Ca2+ concentration, temperature and pH. Monospecific polyclonal antibodies were obtained to the lectin. As was shown by ELISA assay, antibodies to SJL-32 cross-reacted with human serum mannan-binding lectin. This data allows making conclusion about common antigenic determinants and structural homology of both lectins. In our opinion, SJL-32 belongs to evolutionary high conservative mannan-binding lectins (MBLs) family and takes part in the host defense against pathogenic microorganisms.

• Current Research on Agriculture and Life Sciences
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• v.15
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• pp.25-32
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• 1997

This study was carried out to research the biological characteristics among rhizobia and soybean seed and root lectins, and to obtain a basic imformation of host specificity in biological nitrogen symbiosis system. The results obtained were as follows: Purified seed lectin from soybean varieties of paldal, backwoon and hwangkeum formed immunoprecipitin lines with standard soybean seed lectin and the root lectins from soybean seedlings immunoelectrophoretically. Soybean seed and root lectins interacted with Rhizobium japonicum and Bradyrhizobium japonicum, but didn't interacted with Rhizobium. viceae, whereas pea lectin conjugated with R. viceae, but didn't bind with R. japonicum and B. japonicum. Lipopolysaccharides of B. japonicum and R. viceae were fractionated into LPS I and LPS II on the sephadox G-50. Lipopolysaccharides from B. japonicum showed rhe binding acitivity both with soybean seed lectin and root lectin, but those from R. viceae didn't show it with soybean seed and root lectins.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2001.11a
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• pp.69-70
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• 2001

Lectins have great potential as to determine the alternation of the distribution of cell surface carbohydrates during cellular development and differentiation. Here, we investigated the presence and distribution of cell surface carbohydrates on chicken primordial germ cells (PGCs) during the migration and gonadal stages using a variety of lectins. A total of six FITC-labelled lectins from several specificity classes were used: ConA (glucose/mannose), WGA (N-acetylglucosamine), STA (N-acetylglucosamine), DBA (N-acetylgalactosamine/galactose), UEA-I (fucose) and PHA-E (oilgosaccharide). As a results, PGC-specific binding was observed in STA. PGCs of migration stage (2.5- and 5.5-day embyos) were STA-positive whereas PGCs of 10-day embryonic gonad were not. The results suggest that N-acetylglucosamine residuse are present specifically in migrating chicken PGCs and changes during development.

• YAKHAK HOEJI
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• v.47 no.3
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• pp.176-179
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• 2003

A library of unlimited number of novel lectins with diverse specificities has been previously generated by randomly mutating the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH). To establish the experimental environment capable of selecting high affinity mutant lectins in E. coli, phage display system was adapted. Carbohydrate binding capacity of two phagemid vectors, pComb3 and pComb8 displaying wild-type MAH lectin was assessed. Specific bindings of pComb3 and pComb8 phages expressing w.t. MAH to affinity-purified polyclonal anti-MAH antibody and to glycophorin was demonstrated. Both phages also showed strong hemagglutinating activity to intact but not sialidase-treated human erythrocytes, which is consistent to the specificity of native MAH. Taken together, two different phage display vectors successfully allowed the expression of active MAH as a fusion protein on the surface of bacteriophage, which will lead to preparation of unique plant lectins with high affinity toward a variety of carbohydrate chains.

• YAKHAK HOEJI
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• v.31 no.4
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• pp.213-218
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• 1987

Twenty species of higher fungi growing in the wild were collected and studied extensively for their lectin activities by using erythrocytes of human, rabbit and mouse blood. In total, 14 species demonstrated hemagglutination with some kinds of erythrocytes. Of twenty species, eight (Boletus edulis, B. splendidus, Clavaria zollingeri, Lactaritis subzonarius, L. volemus, Russula cutefracta, Pholiota squarrosa, and P. aspera) were shown lymphoagglutination with murine splenic lymphocytes. Protein contents were estimated from the crude lectin fraction. Above mentioned eight species contained relatively high amounts of proteins than other mushrooms. Since these species had coincidently, hiig emagglutinating activity as well, we could define them as lectin-containeing mushrooms. Some species also contained mitogenic lectins toward murine splenic lymphocytes.