Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family

Chaves, Renata Pinheiro; Silva, Suzete Roberta da; Silva, João Pedro Freire Alves da; Carneiro, Rômulo Farias; Sousa, Bruno; Abreu, Jade Oliveira; Carvalho, Fátima; Rocha, Cecília; Farias, Wladimir Ronald Lobo; Sousa, Oscarina Viana de; Silva, André Luiz Coelho; Sampaio, Alexandre Holanda; Nagano, Celso Shiniti

doi:10.1007/s10811-018-1473-7

Cited by 15 publications

(6 citation statements)

References 36 publications

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“…A-M correspond to lectins used as structural scaffolds (( A ): Griffithsin, ( B ): ASL-1, ( C ): BU14, ( D ): HfL, ( E ): BCA, ( F ): OtL, ( G ): BPL-2, ( H ): NgL, ( I ): Actinohivin, ( J ): CVN, ( K ): MVN, ( L ): OAA, ( M ): Scytovirin. References [ 28 , 29 , 30 , 112 , 113 , 114 , 115 , 116 , 117 , 118 , 119 , 120 , 121 , 122 , 123 , 124 , 125 , 126 , 127 , 128 , 129 ] correspond to the lectins presented in the figure.…”

Section: Figurementioning

confidence: 99%

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Barre

Damme

Simplicien

et al. 2021

Cells

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Betacoronaviruses, responsible for the “Severe Acute Respiratory Syndrome” (SARS) and the “Middle East Respiratory Syndrome” (MERS), use the spikes protruding from the virion envelope to attach and subsequently infect the host cells. The coronavirus spike (S) proteins contain receptor binding domains (RBD), allowing the specific recognition of either the dipeptidyl peptidase CD23 (MERS-CoV) or the angiotensin-converting enzyme ACE2 (SARS-Cov, SARS-CoV-2) host cell receptors. The heavily glycosylated S protein includes both complex and high-mannose type N-glycans that are well exposed at the surface of the spikes. A detailed analysis of the carbohydrate-binding specificity of mannose-binding lectins from plants, algae, fungi, and bacteria, revealed that, depending on their origin, they preferentially recognize either complex type N-glycans, or high-mannose type N-glycans. Since both complex and high-mannose glycans substantially decorate the S proteins, mannose-specific lectins are potentially useful glycan probes for targeting the SARS-CoV, MERS-CoV, and SARS-CoV-2 virions. Mannose-binding legume lectins, like pea lectin, and monocot mannose-binding lectins, like snowdrop lectin or the algal lectin griffithsin, which specifically recognize complex N-glycans and high-mannose glycans, respectively, are particularly adapted for targeting coronaviruses. The biomedical prospects of targeting coronaviruses with mannose-specific lectins are wide-ranging including detection, immobilization, prevention, and control of coronavirus infection.

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Section: Figurementioning

confidence: 99%

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Barre

Damme

Simplicien

et al. 2021

Cells

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“…Many red algal lectins (e.g., Solieria filiformis lectin [29]) have four to eight tandem repeats of short domains or motifs. The function of these repeated sequences is unclear; prediction algorithms have been developed to clarify their role in protein function and their evolutionary significance [30].…”

Section: Discussionmentioning

confidence: 99%

Induction of Recombinant Lectin Expression by an Artificially Constructed Tandem Repeat Structure: A Case Study Using Bryopsis plumosa Mannose-Binding Lectin

et al. 2018

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Lectin is an important protein in medical and pharmacological applications. Impurities in lectin derived from natural sources and the generation of inactive proteins by recombinant technology are major obstacles for the use of lectins. Expressing recombinant lectin with a tandem repeat structure can potentially overcome these problems, but few studies have systematically examined this possibility. This was investigated in the present study using three distinct forms of recombinant mannose-binding lectin from Bryopsis plumosa (BPL2)—i.e., the monomer (rD1BPL2), as well as the dimer (rD2BPL2), and tetramer (rD4BPL2) arranged as tandem repeats. The concentration of the inducer molecule isopropyl β-D-1-thiogalactopyranoside and the induction time had no effect on the efficiency of the expression of each construct. Of the tested constructs, only rD4BPL2 showed hemagglutination activity towards horse erythrocytes; the activity of towards the former was 64 times higher than that of native BPL2. Recombinant and native BPL2 showed differences in carbohydrate specificity; the activity of rD4BPL2 was inhibited by the glycoprotein fetuin, whereas that of native BPL2 was also inhibited by d-mannose. Our results indicate that expression as tandem repeat sequences can increase the efficiency of lectin production on a large scale using a bacterial expression system.

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“…Результати свідчать про те, що S. aureus та V. alginolyticus мають O-гліканову структуру (структури) типу NeuAc/GalNAc на клітинній поверхні, яка може відповідати як рецептор(и) для GCL. Повідомлялося про видоспецифічну антибактеріальну активність для лектинів червоних водоростей Eucheuma serra, Galaxaura marginata (Liao et al, 2003), Eucheuma denticulatum (Hung et al, 2015), Gracilaria fisheri (Boonsri et al, 2017) та Meristiella echinocarpa (Chaves et al, 2018b). Інформація щодо водоростевих лектинів допоможе з'ясувати механізм зараження морських патогенів і захистити риб та молюсків від зараження.…”

Section: результати та обговоренняunclassified

N-acetylneuraminic acid specific lectin and antibacterial activity from the red alga Gracilaria canaliculata Sonder

Hung¹,

Trang²

2021

Algologia

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A new lectin from the marine red alga Gracilaria canaliculata (GCL) was isolated by a combination of aqueous ethanol extraction, ethanol precipitation, ion exchange and filtration chromatography. Lectin gave a single band with molecular mass of 22,000 Da in both non-reducing and reducing SDS-PAGE conditions, indicating that GCL is a monomeric protein. The hemagglutination activities of GCL were stable over a wide range of pH from 3 to 10, temperature up 60 oC and not affected by either the presence of EDTA or addition of divalent cations. Lectin GCL had high affinity for N-acetylneuraminic acid through interacting with the acetamido group at equatorial C2 position of these sugar residues, suggesting that GCL is specific for N-acetylneuraminic acid. Furthermore, GCL inhibited the growth of human and shrimp pathogenic bacteria, Staphylococcus aureus and Vibrio alginolyticus, although it did not affect the growth of Escherichia coli, Enterobacter cloace, Vibrio parahaemolyticus and V. harveyi. The red alga G. canaliculata may promise to be a source of valuable lectins for application as antibacterial agents.

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Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family

Cited by 15 publications

References 36 publications

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives

Induction of Recombinant Lectin Expression by an Artificially Constructed Tandem Repeat Structure: A Case Study Using Bryopsis plumosa Mannose-Binding Lectin

N-acetylneuraminic acid specific lectin and antibacterial activity from the red alga Gracilaria canaliculata Sonder

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