Amino acid sequence of the d-galactose binding lectin II from the sponge Axinella polypoides (Schmidt) and identification of the carbohydrate binding site in lectin II and related lectin I

Buck, Fritz; Schulze, Christian; Breloer, Minka; Strupat, Kerstin; Bretting, Hagen

doi:10.1016/s0305-0491(98)10083-4

Cited by 10 publications

(5 citation statements)

References 13 publications

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“…To our knowledge, the previous investigations that have been reported on the chemistry of this sponge relate to sterols and lectin families only. [1][2][3] Herein we describe the isolation of two new modified amino acids, axiphenylalaninium (1) and axityrosinium (2), along with the known metabolites C 2 -R-Dmannosylpyranosyl-L-tryptophan (3), N 3 ,5′-cycloxanthosine (4), palythine (5), and taurine.…”

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confidence: 99%

Axiphenylalaninium and Axityrosinium, Modified Amino Acids from the Mediterranean Marine Sponge Axinella polypoides

et al. 2009

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Two new modified amino acids, axiphenylalaninium (1) and axityrosinium (2), along with four known metabolites, C2-alpha-D-mannosylpyranosyl-L-tryptophan (3), N3,5'-cycloxanthosine (4), palythine (5), and taurine, were isolated from the marine sponge Axinella polypoides collected in the Mediterranean Sea. The structures were determined by spectroscopic studies and confirmed by X-ray analysis and chemical modifications.

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confidence: 99%

Axiphenylalaninium and Axityrosinium, Modified Amino Acids from the Mediterranean Marine Sponge Axinella polypoides

et al. 2009

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“…Recently, it has become apparent that the galectin family of lectins can also participate in the innate immune defense against pathogens (12). Galectins are present in all multicellular organisms, including worms, sponges, multicellular fungi, and insects (13)(14)(15)(16)(17)(18)(19). Galectins are PRRs in several types of organisms, and many mammalian pathogens express saccharide structures that are recognized by galectins.…”

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confidence: 99%

Galectin-3 Induces Death of Candida Species Expressing Specific β-1,2-Linked Mannans

Kohatsu

Hsu

Jegalian

et al. 2006

The Journal of Immunology

202

157

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Lectins play a critical role in host protection against infection. The galectin family of lectins recognizes saccharide ligands on a variety of microbial pathogens, including viruses, bacteria, and parasites. Galectin-3, a galectin expressed by macrophages, dendritic cells, and epithelial cells, binds bacterial and parasitic pathogens including Leishmania major, Trypanosoma cruzi, and Neisseria gonorrhoeae. However, there have been no reports of galectins having direct effects on microbial viability. We found that galectin-3 bound only to Candida albicans species that bear β-1,2-linked oligomannans on the cell surface, but did not bind Saccharomyces cerevisiae that lacks β-1,2-linked oligomannans. Surprisingly, binding directly induced death of Candida species containing specific β-1,2-linked oligomannosides. Thus, galectin-3 can act as a pattern recognition receptor that recognizes a unique pathogen-specific oligosaccharide sequence. This is the first description of antimicrobial activity for a member of the galectin family of mammalian lectins; unlike other lectins of the innate immune system that promote opsonization and phagocytosis, galectin-3 has direct fungicidal activity against opportunistic fungal pathogens.

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“…The partial structural elucidation of lectins was usually performed using mass spectrometry [ 49 , 62 , 64 ] or Edman degradation [ 61 , 65 ].…”

Section: Sponge Lectin Purification Sequencing and Expressionmentioning

confidence: 99%

“…Later, this classification was modified with the identification of the A. polypoides lectin II, which exhibited the same structural characteristics. Both lectins have only one QxW motif and their intrachain disulfide loop showed to play a crucial role in the binding activity onto carbohydrates [ 64 ].…”

Section: Biochemical Properties Of Sponge Lectinsmentioning

confidence: 99%

Porifera Lectins: Diversity, Physiological Roles and Biotechnological Potential

et al. 2015

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An overview on the diversity of 39 lectins from the phylum Porifera is presented, including 38 lectins, which were identified from the class of demosponges, and one lectin from the class of hexactinellida. Their purification from crude extracts was mainly performed by using affinity chromatography and gel filtration techniques. Other protocols were also developed in order to collect and study sponge lectins, including screening of sponge genomes and expression in heterologous bacterial systems. The characterization of the lectins was performed by Edman degradation or mass spectrometry. Regarding their physiological roles, sponge lectins showed to be involved in morphogenesis and cell interaction, biomineralization and spiculogenesis, as well as host defense mechanisms and potentially in the association between the sponge and its microorganisms. In addition, these lectins exhibited a broad range of bioactivities, including modulation of inflammatory response, antimicrobial and cytotoxic activities, as well as anticancer and neuromodulatory activity. In view of their potential pharmacological applications, sponge lectins constitute promising molecules of biotechnological interest.

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Amino acid sequence of the d-galactose binding lectin II from the sponge Axinella polypoides (Schmidt) and identification of the carbohydrate binding site in lectin II and related lectin I

Cited by 10 publications

References 13 publications

Axiphenylalaninium and Axityrosinium, Modified Amino Acids from the Mediterranean Marine Sponge Axinella polypoides

Axiphenylalaninium and Axityrosinium, Modified Amino Acids from the Mediterranean Marine Sponge Axinella polypoides

Galectin-3 Induces Death of Candida Species Expressing Specific β-1,2-Linked Mannans

Porifera Lectins: Diversity, Physiological Roles and Biotechnological Potential

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