Purification and structural characterization of lectins from the cnidarian Bunodeopsis antillienis

Fenton-Navarro, B; Arreguı́n-L, Barbarı́n; García‐Hernández, Enrique; Heimer, Edgar P.; Aguilar, Manuel B.; Rodrı́guez-A, C; Arreguı́n-Espinosa, Roberto

doi:10.1016/s0041-0101(03)00231-9

Cited by 8 publications

(3 citation statements)

References 20 publications

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“…the sperm agglutination factor from E. coli) [26]. Lectins have also been reported in sea anemone venoms [27]; however, lectins possess higher molecular weights than those detected in our MALDI-TOF analysis. The nature of the molecule and process causing the sperm agglutination remains to be elucidated until a complete chemical characterization of the fraction has been conducted.…”

Section: Sperm Motilitysupporting

confidence: 47%

A Sea Anemone Lebrunia neglecta Venom Fraction Decreases Boar Sperm Cells Capacitation: Possible Involvement of HVA Calcium Channels

Lazcano-Pérez

Bermeo

Castro

et al. 2022

Toxins

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Sea anemones produce venoms characterized by a complex mixture of low molecular weight compounds, proteins and peptides acting on voltage-gated ion channels. Mammal sperm cells, like neurons, are characterized by their ion channels. Calcium channels seem to be implicated in pivotal roles such as motility and capacitation. In this study, we evaluated the effect of a low molecular weight fraction from the venom of the sea anemone Lebrunia neglecta on boar sperm cells and in HVA calcium channels from rat chromaffin cells. Spermatozoa viability seemed unaffected by the fraction whereas motility and sperm capacitation were notoriously impaired. The sea anemone fraction inhibited the HVA calcium current with partial recovery and no changes in chromaffin cells’ current kinetics and current–voltage relationship. These findings might be relevant to the pharmacological characterization of cnidarian venoms and toxins on voltage-gated calcium channels.

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Section: Sperm Motilitysupporting

confidence: 47%

A Sea Anemone Lebrunia neglecta Venom Fraction Decreases Boar Sperm Cells Capacitation: Possible Involvement of HVA Calcium Channels

Lazcano-Pérez

Bermeo

Castro

et al. 2022

Toxins

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“…To date, coral lectins have been reported from three hexacoral species, including Gerardia savaglia (zoanthid) [26], Acropora millepora [27], Cerianthus membranaceus [28] and Bunodeopsis antilliensis [29], as well as four octocoral species Sinularia lochmodes [19], Lobophytum variatum [30], Sinularia sp. [31], and Eunicella cavolinii [32].…”

Section: Discussionmentioning

confidence: 99%

Effects of lectin in the scleractinian coral Ctenactis echinata on symbiotic zooxanthellae

et al. 2010

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We report herein the presence of a lectin in the scleractinian coral Ctenactis (Fungia) echinata. The lectin bound preferentially to lactose, melibiose, and D-galactose. The purified lectin CecL was composed of several isolectins, and it was found to have a molecular mass of 67.4 kDa via gel filtration. Glycopeptidase F-treated CecL showed a single band at 32.5 kDa. The mass/charge ratios of the reduced CecL peaks were equivalent to half those of the native peaks. These results suggest that CecL is composed of two glycosylated polypeptides linked by interchain disulfide bonds. In a biological activity test using a zooxanthellal culture (Dinoflagellate Symbiodinium) clonally isolated from Fungia cf. fungites, CecL transformed the flagellated motile form of Symbiodinium into the nonmotile coccoid form, a form equivalent to the symbiotic stage. The activity of CecL on Symbiodinium cells was concentration dependent, and 100 lg/ml CecL arrested Symbiodinium cells in the coccoid form for 5 days. CecL also suppressed the growth of Symbiodinium cells, unlike the octocoral lectin derived from Sinularia lochmodes, which arrests Symbiodinium cells in the coccoid form but does not affect the growth of the coccoid. This result provides further evidence that coral lectins play a role in symbiont engagement and maintenance in zooxanthellaecoral symbiosis.

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“…Repopulation of bleached adult anemones by Symbiodinium can be inhibited in the presence of the α‐mannose/α‐glucose‐binding lectin Concanavalin A (ConA) or when symbionts have been treated with enzymes that alter the algal cell surface (Reisser et al ., 1982; Lin et al ., 2000). In addition, there is biochemical and molecular evidence for the presence of glycoproteins on the cell surface of Symbiodinium (Markell et al ., 1992; Jimbo et al ., 2000) as well as for lectins in several soft coral species (Fenton‐Navarro et al ., 2003; Koike et al ., 2004; Jimbo et al ., 2005), and both components are hypothesized to act in inter‐partner signalling.…”

Section: Introductionmentioning

confidence: 99%

Lectin/glycan interactions play a role in recognition in a coral/dinoflagellate symbiosis

et al. 2006

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SummaryRecognition is an important stage in the establishment of highly specific mutualistic associations. Yet, for the majority of symbioses, very few of the mechanisms involved in recognition and specificity are known. In this study, we provide evidence for a recognition mechanism at the onset of symbiosis between larvae of the coral Fungia scutaria and their endosymbiotic dinoflagellate algae. This recognition step occurs during initial cellular contact between the symbiotic partners through a lectin/glycan interaction. We determined that an intact algal cell surface was required for successful infection of F. scutaria larvae. Modification of the algal cell surface by enzymatic digestion with trypsin or N-glycosidase significantly reduced infection success, and implicated algal cell surface glycans in recognition. Using flow cytometry, a-mannose/aglucose and a-galactose residues were identified as potential recognition ligands on the algal cell surface. Finally, inhibition of these cell surface glycans significantly reduced infection of F. scutaria larvae by the algae. These data provide evidence that the algal cell surface contains glycan ligands, such as a-mannose/ a-glucose and a-galactose, which play a role in recognition during initial contact at the onset of symbiosis with F. scutaria larvae.

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Purification and structural characterization of lectins from the cnidarian Bunodeopsis antillienis

Cited by 8 publications

References 20 publications

A Sea Anemone Lebrunia neglecta Venom Fraction Decreases Boar Sperm Cells Capacitation: Possible Involvement of HVA Calcium Channels

A Sea Anemone Lebrunia neglecta Venom Fraction Decreases Boar Sperm Cells Capacitation: Possible Involvement of HVA Calcium Channels

Effects of lectin in the scleractinian coral Ctenactis echinata on symbiotic zooxanthellae

Lectin/glycan interactions play a role in recognition in a coral/dinoflagellate symbiosis

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