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At least 19 recordsLinked to original sources
PubMed1996

Characterization and molecular cloning of Sambucus nigra agglutinin V (nigrin b), a GalNAc-specific type-2 ribosome-inactivating protein from the bark of elderberry (Sambucus nigra).

The molecular structure of the Sambucus nigra agglutinin V (SNAV), which has been described previously as a type-2 ribosome-inactivating protein called nigrin b, has been studied in detail by analysis of the purified protein combined with cDNA cloning and molecular modelling. Native SNAV is a dimer of two [A-s-s-B] pairs. Hapten inhibition assays indicated that GalNAc is a 20-fold more potent inhibitor of SNAV than Gal. A cDNA clone encoding SNAV was isolated from a cDNA library constructed with mRNA from the bark. Sequence analysis of this cDNA revealed a striking similarity to the recently cloned NeuAc alpha-2,6-gal/GalNAc-specific S. nigra bark agglutinin I (SNAI) and to the previously sequenced type-2 ribosome-inactivating proteins from Ricinus communis and Abrus precatorius. In addition, molecular modelling of SNAV further suggested that its structure closely resembles that of ricin. The N-terminal sequence of the B chain of SNAV also shows a marked similarity with the polypeptide of the previously described GalNAc-specific s. nigra bark agglutinin II (SNAII), which unlike SNAV and SNAI has no ribosome-inactivating activity. It appears, therefore, that elderberry bark contains at least two different type-2 ribosome-inactivating proteins and a lectin built up of subunits which are closely related to the B chain of SNAV.

Amino Acid Sequence↗
PubMed2001

Hydraulic vulnerability, vessel refilling, and seasonal courses of stem water potential of Sorbus aucuparia L. and Sambucus nigra L.

Differences in the seasonal variation in stem water potential between the two shrub species Sorbus aucuparia and Sambucus nigra were related with their vulnerability to xylem cavitation. It was also demonstrated indirectly that the two species differ in the extent to which they reverse cavitation. Seasonal variation in stem water potential was investigated during three growing seasons with in situ stem psychrometers. Sorbus experienced wide water potential variations and reached a minimum of -4.2 MPa during drought. Under the same microclimatic conditions, Sambucus experienced consistent stem water potentials with a minimum of -1.7 MPa. The relationship between percentage loss in hydraulic conductivity (PLC) and water potential (hydraulic vulnerability curve) of the two species differed in shape: a flat curve with nearly total loss of conductivity at -6 MPa was found for SORBUS: Sambucus showed a steep vulnerability curve with 90% loss conductivity at -2.2 MPa. Thus, Sambucus is extremely vulnerable to cavitation, but Sorbus is an almost invulnerable species. This different cavitation resistance adjusted the ranges of field stem water potential that the species experienced. Finally, seasonal courses of naturally occurring (native) embolism were compared with calculated PLC courses. This comparison indicates that Sorbus did not refill embolized xylem vessels whereas Sambucus reversed embolism. It was concluded that species which are highly vulnerable to cavitation and drought-induced embolism need refilling of embolized vessels as well as isohydric water potential patterns as two strategies of survival.

Biological Transport↗
PubMed2003

Non-toxic type 2 ribosome-inactivating proteins (RIPs) from Sambucus: occurrence, cellular and molecular activities and potential uses.

Ribosome-inactivating proteins (RIPs) are a family of enzymes that trigger the catalytic inactivation of ribosomes. The most known member of the family is the highly poisonous two-chain ricin isolated from Ricinus communis L. Sambucus species contain a number of two-chain RIPs structurally and enzymatically related to ricin which have the noteworthy feature that, having an enzymatic activity on ribosomes, leading to the inhibition of protein synthesis, higher than ricin, they are lacking of the tremendous unspecific toxicity of ricin. Therefore, they have been called non-toxic type 2 RIPs. The most representative and studied members are nigrin b present in the bark of the common (black) elder Sambucus nigra L. and ebulin 1 present in the leaves of the dwarf elder Sambucus ebulus L. The molecular basis for the low unspecific activities of nigrin b and ebulin 1 as compared with ricin seems to be related with single changes of amino acids in the high affinity sugar binding sites of the B chains. These changes determine the intracellular traffic of these proteins and thus the cellular toxicity. Conjugation ofnigrin b or ebulin 1 to either transferrin or monoclonal antibodies provided highly active conjugates targeting cancer. Thus these non-toxic type 2 RIPs are promising tools for cancer therapy.

Amino Acid Sequence↗
PubMed2005

[Protective effects of the granule of Sambucus chinensis lindl on acute hepatic injury].

OBJECTIVE: To investigate the protective effects of the granule of Sambucus chinensis Lindl on acute hepatic injury. METHODS: The acute liver-injury model induced by CCl4 or D-GalN or ConA was established in mice or rats. RESULTS: The granule of Sambucus chinensis Lindl showed significantly protective effects on mice acute hepatic injury induced by CCl4 ,and the effects were concern of antagonizing lipoperoxidation and improving energy of Ca2+ -ATPase of theca mitochondria and microsome. It showed significantly protective effects on mice or rats acute hepatic injury induced by D-GalN or Con A, too. CONCLUSION: The granule of Sambucus chinensis Lindl showed significantly protective effects against many kinds of chemical and immunological liver injuries.

Animals↗
PubMed2003

Isolation and characterization of a new d-galactose-binding lectin from Sambucus racemosa L.

A new acidic lectin from red elder (Sambucus racemosa L.) bark has been isolated by affinity chromatography and gel filtration. Noteworthy, and in contrast to other Sambucus species, red elder bark lacks acidic non-toxic type 2 ribosome-inactivating proteins but has basic ribosome-inactivating protein activities. The new lectin (SRLbm) shows specificity for N-Ac-Galactosamine/D-Galactose and has an apparent Mr of 30,000. The N-terminal amino acid sequence displays a close homology with other lectins and B chains of non-toxic type 2 ribosome-inactivating proteins nigrins and ebulins present in other Sambucus species. SRLbm triggers red blood cell agglutination in the range 4-12 micro g/ml.

Acetylgalactosamine↗
PubMed1991

Expression of alpha 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins.

Increased sialylation of cell surface glycoconjugates has been demonstrated in malignant tumors and shown to be correlated with the invasive and metastatic growth of colon carcinoma cells. The authors have applied the Maackia amurensis lectin, which interacts with alpha 2,3-linked sialic acid, and the Sambucus nigra I lectin specific for alpha 2,6-linked sialic acid. In human colon, alpha 2,3-linked sialic acid was detectable in normal and transitional mucosa as well as in adenomas with different degrees of dysplasia and in carcinoma. In contrast, alpha 2,6-linked sialic acid as visualized with Sambucus nigra I lectin was found only in severe dysplasia and carcinoma. Thus expression of binding sites for Sambucus nigra I lectin was associated with the occurrence of histologic features of malignancy. It is concluded that malignant transformation in human colonic epithelium is accompanied by the de novo expression of an alpha 2,6 sialyl-transferase. These findings provide the basis for more detailed studies of the possible role of cell surface glycoconjugates bearing alpha 2,6-linked sialic acid in growth behavior of human colonic epithelial cells.

Adenocarcinoma↗
PubMed2005

Antiviral activity in vitro of Urtica dioica L., Parietaria diffusa M. et K. and Sambucus nigra L.

Parietaria diffusa M. et K., Urtica dioica L. (Urticaceae) and Sambucus nigra L. (Caprifoliaceae) are plants usually used in popular medicine of central Italy for treating numerous diseases, first of all Herpes zoster. Several plant products have been described as potential antiviral agents, with special attention being devoted to those having retroviruses as etiological agents, including acquired immunodeficiency syndrome (AIDS), in which a retrovirus, the designated human immunodeficiency virus HIV, has been clearly identified as the primary cause of this disease. The present study proposes a preliminary screening of the antiviral activity of Parietaria diffusa, Sambucus nigra and Urtica dioica preparation against the feline immunodeficiency virus (FIV) infection. The feline immunodeficiency virus is a widespread lentivirus of domestic cats sharing numerous biological and pathogenic features with the human immunodeficiency virus (HIV). FIV infection in cats has therefore been proposed as an animal model for AIDS studies with respect to pathogenesis, chemotherapy, and vaccine development [Pedersen, N.C., 1993. Feline immunodeficiency virus infection. In: Levy, J.A. (Ed.), The Retroviridae. Plenum Press, New York; Bendinelli, M., Pistello, M., Lombardi, S., Poli, A., Garzelli, C., Matteucci, D., Ceccherini-Nelli, L., Malvaldi, G., Tozzini, F., 1995. Feline immunodeficiency virus: an interesting model for AIDS studies and an important cat pathogen. Clinical Microbiology Revue 8, 87-112; North, T.W., LaCasse, R.A., 1995. Testing anti-HIV drugs in the FIV model. Nature Medicine 1, 410-411; Matteucci, D., Pistello, M., Mazzetti, P., Giannechini, S., Isola, P., Merico, A., Zaccaro, L., Rizzati, A., Bendinelli, M., 2000. AIDS vaccination studies using feline immunodeficiency virus as a model: immunisation with inactivated whole virus suppresses viraemia levels following intravaginal challenge with infected cells but non-following intravenous challenge with cell-free virus. Vaccine 18, 119-130]. Early studies showed that some of them presented antiviral activity against infection of FIV as assayed by syncytia formation using feline kidney Crandell cells (CrFK).

Animals↗
PubMed2002

A complex fruit-specific type-2 ribosome-inactivating protein from elderberry (Sambucus nigra) is correctly processed and assembled in transgenic tobacco plants.

Fruits of elderberry (Sambucus nigra) express small quantities of a type-2 ribosome-inactivating protein with an exclusive specificity towards the NeuAc(alpha2,6)Gal/GalNAc disaccharide and a unique molecular structure typified by the occurrence of a disulfide bridge between the B-chains of two adjacent protomers. A cDNA clone encoding this so-called Sambucus nigra fruit specific agglutinin I (SNA-If) was isolated and expressed in tobacco (Samsun NN) under the control of the 35S cauliflower mosaic virus promoter. Characterization of the purified protein indicated that the recombinant SNA-If from tobacco leaves has the same molecular structure and biological activities as native SNA-If from elderberry fruits, demonstrating that transgenic tobacco plants are fully capable of expressing and correctly processing and assembling a type-2 ribosome-inactivating protein with a complex molecular structure. None of the transformants showed a phenotypic effect, indicating that the ectopically expressed SNA-If does not affect the viability of the tobacco cells. Bioassays further demonstrated that none of the transgenic lines exhibited a decreased sensitivity to infection with tobacco mosaic virus suggesting that the elderberry type-2 RIP SNA-If does not act as an antiviral agent in planta.

Amino Acid Sequence↗
PubMed1991

Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit.

A previously unknown haemagglutinin, named Sambucus nigra agglutinin-III (SNA-III), has been purified from the fruit of the elder (Sambucus nigra). Whereas elder bark agglutinin I (SNA-I) is highly specific for terminal alpha 2,6-linked sialic acid residues, SNA-III displays a high affinity for oligosaccharides containing exposed N-acetylgalactosamine and galactose residues. Different N-terminal sequences and the amino acid composition distinguish the fruit lectin from elder bark agglutinin II (SNA-II), which shows a similar carbohydrate specificity. The 40-fold higher affinity of SNA-III for asialofetuin than for human asialo-alpha 1-acid glycoprotein and human asialotransferrin respectively suggests a preference for O-linked glycans. SNA-III occurs mainly as a monomeric glycoprotein, but tends to form di- and oligo-meric aggregates. This aggregation seems to mediate the multivalent interaction, leading to agglutination. SDS/PAGE revealed two major polypeptides with apparent molecular masses of 32 and 33 kDa respectively. This heterogeneity is probably a result of proteolysis in the C-terminal region. Binding to concanavalin A and susceptibility to peptide: N-glycosidase F indicated the presence of N-glycosidically linked oligosaccharides.

Amino Acid Sequence↗
PubMed1997

The major elderberry (Sambucus nigra) fruit protein is a lectin derived from a truncated type 2 ribosome-inactivating protein.

The major protein of elderberry (Sambucus nigra L.) fruits is a lectin, called Sambucus nigra agglutinin IVf or SNAIVf. This lectin is composed of subunits that strongly resemble the B chain of the type 2 ribosome-inactivating protein (RIP), called SNAVf, present in the same tissue. To corroborate the possible relationship between both proteins their corresponding cDNAs were cloned and compared. Alignment of the deduced amino acid sequences revealed that the cDNA encoding SNAIVf is almost identical to that of SNAVf except that its A chain is truncated. Northern blot analysis confirmed that the mRNA encoding SNAIVf is about 500 nucleotides shorter than the SNAVf mRNA. In addition, the occurrence of a truncated type 2 RIP gene was unambiguously demonstrated by the analysis of PCR amplified genomic sequences. These results not only demonstrate for the first time that a plant lectin is encoded by a truncated type 2 RIP gene but also address important questions with respect to the molecular evolution of RIP and lectins.

Amino Acid Sequence↗
PubMed1996

Sialylated oligosaccharide-specific plant lectin from Japanese elderberry (Sambucus sieboldiana) bark tissue has a homologous structure to type II ribosome-inactivating proteins, ricin and abrin. cDNA cloning and molecular modeling study.

Bark lectins from the elderberry species belonging to the genus Sambucus have a unique carbohydrate binding specificity for sialylated glycoconjugates containing NeuAc(alpha 2-6)Gal/GalNAc sequence. To elucidate the structure of the elderberry lectin, a cDNA library was constructed from the mRNA isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) with lambda gt11 phage and screened with anti-S. sieboldiana agglutinin (SSA) antibody. The nucleotide sequence of a cDNA clone encoding full-length SSA (LecSSA1) showed the presence of an open reading frame with 1902 base pairs, which corresponded to 570 amino acid residues. This open reading frame encoded a signal peptide and a linker region (19 amino acid residues) between the two subunits of SSA, the hydrophobic (A-chain) and hydrophilic (B-chain) subunits. This indicates that SSA is synthesized as a preproprotein and post-translationally cleaved into two mature subunits. Homology searching as well as molecular modeling studies unexpectedly revealed that each subunit of SSA has a highly homologous structure to the galactose-specific lectin subunit and ribosome-inactivating subunit of plant toxic proteins such as ricin and abrin, indicating a close evolutionary relationship between these carbohydrate-binding proteins.

Abrin↗
PubMed2000

The traditional plant treatment, Sambucus nigra (elder), exhibits insulin-like and insulin-releasing actions in vitro.

Sambucus nigra (elder) has been documented as a traditional treatment of diabetes. In the present study, an aqueous extract of elder (AEE, 1 g/L) significantly increased 2-deoxy-glucose transport, glucose oxidation and glycogenesis of mouse abdominal muscle in the absence of added insulin (2 x 2 factorial design). in acute 20-min tests, 0.25-1 g/L AEE evoked a stepwise stimulation of insulin secretion from clonal pancreatic beta-cells. The insulin releasing effect of AEE (0.5 g/L) was significantly potentiated by 16.7 mmol/L of glucose and significantly reduced by 0.5 mmol/L of diazoxide. AEE did not further enhance insulin secretion in cells stimulated by 10 mmol/L of L-alanine, 1 mmol/L of 3-isobutyl-1-methylxanthine or a depolarizing concentration of KCl (25 mmol/L). Prior exposure of clonal pancreatic beta-cells to AEE did not alter subsequent stimulation of insulin secretion induced by 10 mmol/L of L-alanine, thereby precluding a detrimental effect on cell viability. The insulinotropic action of AEE was partially dependent upon use of heat during extract preparation. Activity of AEE was heat-stable, acetone-insoluble and unaltered by prolonged exposure to acid/alkali (0.1 mol/L of HCl and NaOH). However, activity was significantly decreased 41% by dialysis to remove components with molecular mass <2000 Da. Sequential extraction with solvents revealed activity in both methanol and water fractions, indicating a cumulative effect of more than one extract constituent. Known constituents of elder, including lectin, rutin and the lipophilic triterpenoid (lupeol) and sterol (beta-sitosterol), did not stimulate insulin secretion. The results demonstrate the presence of insulin-releasing and insulin-like activity in the traditional antidiabetic plant, Sambucus nigra.

1-Methyl-3-isobutylxanthine↗
PubMed1977

Isolation and properties of a ferredoxin from leaves of Sambucus racemosa L.

Ferredoxin was isolated in good yield from leaves of Sambucus racemosa L. by the following procedure: (1) homogenization in buffered acetone-water (1:1v/v); (2) ion-exchange chromatography on several columns of DEAE-cellulose; and (3) purification by gel filtration with Sephadex G-75. The ultraviolet and visible spectrum showed maxima at 277, 331, 423, and 466 nm. The electron paramagnetic resonance spectrum was centered around g = 1.957. The protein sustained an initial photoreduction rate of 86 mumol NADP per milligram chlorophyll per hour. The amino acid composition was found to be Lys 5, His 2, Arg1, Asx11, Thr5, Ser7, Glx17, Pro6, Gly7, Ala6-7, Cys4, Val8, Ile5, Leu7, Tyr3, Phe2, and Trp1. The molecule had a molecular weight of 10 700 and contained two atoms of iron. The amino-terminal residue was alanine. These properties are highly similar to those of other angiosperm ferredoxins. Sambucus ferredoxin was found to be most closely related to that of Leucaena.

Amino Acids↗
PubMed2000

Morphophysiological dormancy in seeds of two North American and one Eurasian species of Sambucus (Caprifoliaceae) with underdeveloped spatulate embryos.

In contrast to previous reports, the endocarps ("seed coats") of Sambucus species are not impermeable to water; thus, the seeds do not have physical dormancy. Seeds of the North American species Sambucus canadensis and S. pubens and of the European species S. racemosa have spatulate shaped embryos that are ∼60% fully developed (elongated) at seed maturity. The embryo has to extend to the full length of the seed to germinate. Embryos in freshly matured seeds of S. canadensis and in those of S. pubens grew better at 25°/15°C than at 5°C, whereas the rate of embryo growth in S. racemosa was higher at 5°C than at 25°/15°C. Seeds of all three species germinated to significantly higher percentages in light (14-h photoperiod) than in darkness. Fresh seeds of neither species germinated during 2 wk of incubation over a range of thermoperiods. Warm followed by cold stratification broke dormancy in seeds of S. canadensis and in those of S. pubens. Thus, seeds of these two North American species have deep simple morphophysiological dormancy (MPD). In comparison, seeds of the European species S. racemosa required a cold stratification period only for dormancy break, and thus they have intermediate complex MPD. GA(3) was much more effective in breaking dormancy in seeds of S. racemosa than it was in those of S. canadensis or S. pubens.

Journal Article↗
PubMed1997

Characterization of a new non-toxic two-chain ribosome-inactivating protein and a structurally-related lectin from rhizomes of dwarf elder (Sambucus ebulus L.).

A new N-glycosidase ribosome-inactivating protein (RIP) belonging to the novel family of the nontoxic type 2 RIPs from Sambucaceae has been isolated from rhizomes of dwarf elder (Sambucus ebulus L.) and named ebulin r. Dwarf elder rhizomes also contain a novel monomeric N-Ac-galactosamine-binding lectin that we named SEAII. Ebulin r and SEAII have two isoforms each one, which were readily resolved by ion exchange. Both isoforms of ebulin (ebulins r1 and r2) strongly inhibited protein synthesis in mammalian but not in plant ribosomes by promoting depurination of sensitive ribosomes. Ebulin r and SEAII have apparent molecular masses of 56 and 33.5 kDa, respectively. Ebulins r1 and r2 are composed of two dissimilar subunits (types A-B) of apparent molecular masses of 26 and 30 kDa by disulphide bridges. The rhizome SEAII and the lectins SNA II and SNA III from elder (Sambucus nigra L.) share good amino acid sequence homology. This rhizome ebulin-A chain is more sequence-related to RIP members of cucurbitaceae than to any other plant family. The rhizome ebulin B chain shares a large homology in amino acid sequence with ebulin 1-B chain and SEAII. Anti-ebulin 1 polyclonal antibodies raised in rabbits reacted better with ebulin r1 than with ebulin r2, thus suggesting that both RIP isoforms could have some differences.

Amino Acid Sequence↗