Biological activity, cDNA cloning and primary structure of lectin KSA-2 from the cultivated red alga Kappaphycus striatum (Schmitz) Doty ex Silva

Hung, Le Dinh; Hirayama, Makoto; Lý, Bùi Minh; Hori, Kazuaki

doi:10.1016/j.phytol.2015.09.012

Cited by 26 publications

(22 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ORF coded a polypeptide of 269 amino acids including the initiating methionine amino acid. The calculated molecular mass of the deduce amino acid sequence from EDA cDNA was 27.834.19 Da, similar to that of EDA-2 (27,834.2 Da) determined by ESI-MS methods (Hung et al, 2015). Thus we can concluded that the isolated cDNA encoding EDA-2.…”

Section: Resultssupporting

confidence: 74%

“…The significance difference in biological and evolutionary of the number of repeated domains is currently unknown. However, their sequence similarities suggest that these proteins may also share lectin domains that have a binding affinity for high-mannose N-glycans, as ESA-2 (Hori et al, 2007), KSA-2 (Hung et al, 2011), EDA-2 (Hung et al, 2015), KAA-2 (Sato et al, 2011a;Hirayama et al, 2016), OAA (Sato et al, 2007), BOA (Whitley et al, 2013), PFA and MBHA (Sato et al, 2012;Koharudin et al, 2012), which showed strong anti-HIV and anti-influenza virus activities. From sequence comparison, it is also speculated that the highly conserved segments in both N-terminal and C-terminal regions may be involved in the carbohydrate binding.…”

Section: Resultsmentioning

confidence: 99%

“…Apart from carrageenan source, these cultivated algae may provide bioactive compounds for biochemical and medicinal uses. Lectins from algae of Eucheuma and Kappaphycus genera have been isolated and well characterized and showed the novel properties in carbohydrate binding specificity with high-mannose type N-glycans (Hori et al, 2007;Hung et al, 2009Hung et al, , 2011Hung et al, , 2015Sato et al, 2011a;Hirayama et al, 2016), which were distinct from those of other organisms. Therefore, they are promising sources for the development of new reagents using in biochemistry and biomedicine.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cloning and characterizing cDNA sequences coding high-mannose n-glycan binding lectins from cultivated red algae Eucheuma denticulatum and Kappaphycus striatum

Hung

Hirayama

Hori

2016

Vietnam J. Biotechnol.

Self Cite

View full text Add to dashboard Cite

The red algae, Eucheuma denticulatum and Kappaphycus striatum have been widely cultivated in Vietnam as a source of carrageenophytes for industry. In the past, biochemical properties of lectins isolated from these algae has been characterized and evaluated extensively. However, gene coding for such lectins isn’t studied yet. In this study, their full length cDNA is amfplified using cDNA ends (RACE) methods. Sequence analysis revealed that cDNA of EDA-2 from E. denticulatum consisted of 1,158 bp containing 103 bp of a 5'untranslated region, 248 bp of 3'untranslated region, and 807 bp of an open reading frame; and cDNA of KSA-2 from K. striatum consisted of 1174 bp containing 94 bp of the 5'-untranslated region, 273 bp of 3'untranslated region and 807 bp of the open reading frame. The cDNA of both EDA-2 and KSA-2 encoded for a polypeptide of 269 amino acids including an initiating methionine, but differed in sequences and molecular masses. The deduced amino acid sequences of EDA-2 and KSA-2 composed of four tandem repeated domains with about 67 amino acids each. The primary structure of EDA-2 and KSA-2 is highly similar to those of the high mannose N-glycan specific lectins including OAA from cyanobacterium, BOA, MBHA and PFA from bacteria, and ESA-2, KAA-1, KAA-2 from macro red algae, which showed strong anti-HIV and anti-influenza virus activities. These results indicate that these cultivated algae are becoming promising materials for production of anti-virus reagent or functional food that can prevent virus infection in future.

show abstract

Section: Resultssupporting

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning and characterizing cDNA sequences coding high-mannose n-glycan binding lectins from cultivated red algae Eucheuma denticulatum and Kappaphycus striatum

Hung

Hirayama

Hori

2016

Vietnam J. Biotechnol.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Such species may be potential sources for studies and application of lectins. However, only little information is known about lectins from Vietnam marine organisms, including several reports on lectins from marine invertebrates (Cao Dang Nguyen, 1998), (Cao Dang Nguyen, Nguyen Quoc Khang, 1998), (Cao Dang Nguyen et al, 2000, 2008, (Nguyen Quoc Khang et al, 2000) and from marine algae (Le Dinh Hung et al, 2009aHung et al, , 2009bHung et al, , 2011Hung et al, , 2012Hung et al, , 2015aHung et al, , 2015b. Thus, the objective of this research was to survey haemagglutinins from Vietnam marine invertebrates, which will provide more valuable information for future applications.…”

Section: Marinementioning

confidence: 99%

Haemagglutination Activity of the Extracts From Some Vietnam Marine Invertebrates

Trung¹,

Trang²,

Ngoc³

et al. 2018

Vietnam J. Biotechnol.

Self Cite

View full text Add to dashboard Cite

Aqueous extracts from 21 species of Vietnam marine invertebrates, including 11 bivalve and 10 gastropod species, were examined for haemagglutination activity using native and enzyme-treated different animal and human erythrocytes. The 8 bivalve and 10 gastropod species were found to have haemagglutinination activities toward at least one type of erythrocyte tested. A total of 86% of marine invertebrate species surveyed were active. Strong activity was detected in extracts from two bivalve species (Tridacna squamosa and Geloina coaxans) and three gastropod species (Tutufa rubeta, Pleuroploca trapezium and Tectus conus) with enzyme-treated rabbit, horse and human A, B, O erythrocytes. In a haemagglutination–inhibition test with various monosaccharides and glycoproteins, haemagglutination activities of two extracts from T. rubeta and P. trapezium had no affinity for any of the monosaccharides and glycoproteins tested, while activities of the extracts from T. squamosa and T. conus were strongly inhibited by porcine stomach mucin tested, suggesting the presence of lectins specific for O-glycans of these species. The activities of four marine invertebrate extracts were stable over a wide range ofpH and temperature. The haemagglutination activities of T. rubeta and P. trapezium extracts were independent of the presence of divalent cations, whereas the haemagglutination activity of extracts from T. squamosa and T. conus were slightly dependent on the presence of divalent cations. The results suggest that Vietnam marine invertebrates may be good sources of useful lectins for biochemical and biomedical applications.

show abstract

“…Among them, algal lectins have recently been remarked. Moreover, the recently discovered anti-HIV and antiinfluenza virus lectins from cyanobacteria (blue-green algae) and macroalgae are promised as a new antiviral agent because their inhibiting activities are extremely strong compared to those of lectins from other biological groups (Hung et al, 2015). Despite disparity in physicochemical and biochemical characteristics, lectins from different sources essentially exhibit common biological activities.…”

Section: Prospects For Algal Lectins Research In Indonesiamentioning

confidence: 99%

Algal Lectins and their Potential Uses

Praseptiangga¹

2015

Squalen Bull. Marine Fisheries Postharvest Biotech.

View full text Add to dashboard Cite

Lectins (hemagglutinins), or carbohydrate-binding proteins, are ubiquitous in nature and play important roles in many biological processes. They bind mono-and oligosaccharides reversibly with high specificity, but are devoid of catalytic activity, and in contrast to antibodies, are not products of an immune response. The erythrocyte agglutination or hemagglutination activity of lectins is a major attribute of these proteins and is used routinely for their detection and characterization. Due to their biochemical and biological properties, lectins attract a great deal of attention in the fields of medicine, molecular biology, biochemistry, and glycobiology. Lectins have been isolated and characterized from marine algae. Many of algal lectins generally have common characteristics of low molecular weight, no divalent cations requirements for their activity, and have an affinity for glycoproteins but not for monosaccharides. These properties imply that they may possess molecular structures and carbohydrate-binding specificities distinct from known lectins from other sources. Recent investigations revealed that algal lectins have the strict binding specificity to some definite oligosaccharide structures and are grouped into several types on the basis of oligosaccharide-binding specificity. Thus, marine algae are promising sources of novel lectin molecules for basic research and application. In spite of the progress made in biochemical characterization of algal lectins, additional information are still needed for a more comprehensive understanding of their molecular structures and possible biological functions for the future applications.

show abstract

Biological activity, cDNA cloning and primary structure of lectin KSA-2 from the cultivated red alga Kappaphycus striatum (Schmitz) Doty ex Silva

Cited by 26 publications

References 28 publications

Cloning and characterizing cDNA sequences coding high-mannose n-glycan binding lectins from cultivated red algae Eucheuma denticulatum and Kappaphycus striatum

Cloning and characterizing cDNA sequences coding high-mannose n-glycan binding lectins from cultivated red algae Eucheuma denticulatum and Kappaphycus striatum

Haemagglutination Activity of the Extracts From Some Vietnam Marine Invertebrates

Algal Lectins and their Potential Uses

Contact Info

Product

Resources

About