An unusual lectin from stinging nettle (<i>Urtica dioica</i>) rhizomes

Peumans, Willy J.; Ley, Marc De; Broekaert, Willem F.

doi:10.1016/0014-5793(84)80989-8

Cited by 132 publications

(77 citation statements)

References 14 publications

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“…The CBAs HHA, UDA, and PRM-A were isolated and purified (23,25,33) and kindly provided by E. Van Damme and W. Peumans (University of Ghent, Ghent, Belgium) and T. Oki and Y. Igarashi (Toyama University, Toyama, Japan).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Cell-to-Cell Transmission of Human T-Cell Lymphotropic Virus Type 1 In Vitro by Carbohydrate-Binding Agents

Balestrieri¹,

Ascolani

Igarashi

et al. 2008

Antimicrob Agents Chemother

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Peripheral blood mononuclear cells (PBMCs) from healthy individuals can be infected by human Tlymphotropic virus type 1 (HTLV-1) upon cocultivation of the PBMCs with irradiated HTLV-1-transformed human MT-2 cells. This model system closely mimics HTLV-1 transmission through cell-to-cell contact.Carbohydrate-binding agents (CBAs) such as the ␣(1,3)/␣(1,6)mannose-specific Hippeastrum hybrid agglutinin and the GlcNAc-specific Urtica dioica agglutinin, and also the small, nonpeptidic ␣(1,2)-mannose-specific antibiotic pradimicin A, were able to efficiently prevent cell-to-cell HTLV-1 transmission at nontoxic concentrations, as evidenced by the lack of appearance of virus-specific mRNA and of the viral protein Tax Human T-lymphotropic virus type 1 (HTLV-1) is a member of the genus Deltaretrovirus of the family Retroviridae and is associated with various pathologies (35). The most common characterized pathologies are oncological transformation (i.e., adult T-cell leukemia [ATL] and cutaneous T-cell lymphoma) and neurological abnormalities (i.e., tropic spastic paraparesis). The virus is spread in areas of endemicity in Japan, Central America, and South America. Its worldwide spread encompasses around 20 million infected individuals (12,13,26). The main routes of HTLV-1 infection in vivo consist of mother-to-infant transmission (mainly through breast-feeding), parenteral infection, and viral transmission through sexual intercourse (20,26,27). HTLV-1 infection occurs predominantly by infection of CD4 ϩ T lymphocytes, followed by random integration of the provirus into the cellular genome (11). HTLV-1 infection in vivo results in a lifelong infection that is characterized by low, if any, viremia. Therefore, in the absence of a sustained extracellular phase during the replication cycle of HTLV-1, survival and propagation of the virus within the host seem to be mainly ensured by two modalities: (i) the reverse transcriptase (RT)-independent mitotic pathway and (ii) cell-to-cell contacts allowing the virus to migrate from infected to uninfected cells through an RT-dependent route. However, the mechanisms involved in the entry of HTLV-1 into the cell have not been fully elucidated. HTLV-1 transmission benefits from the formation of cellular conjugates through the generation of biological synapses and involvement of the cytoskeleton (17). Although the glucose transporter GLUT-1 has been identified as a cellular receptor for HTLV-1 (22), other studies indicate that the interaction with this receptor is not sufficient by itself for viral entry into the cell (18,29). The structural component of HTLV-1 presumably required for receptor recognition is composed of the envelope glycoprotein (gp46) and a noncovalently associated transmembrane anchor protein (gp21), derived from a common gp63 precursor (21). gp46 is among the smallest retroviral envelope proteins known, and it exhibits little sequence variability (19). Studies have revealed that all four potential N-glycosylation sites (28) in gp46 are used and that the glycans are m...

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Section: Methodsmentioning

confidence: 99%

Inhibition of Cell-to-Cell Transmission of Human T-Cell Lymphotropic Virus Type 1 In Vitro by Carbohydrate-Binding Agents

Balestrieri¹,

Ascolani

Igarashi

et al. 2008

Antimicrob Agents Chemother

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“…Urtica dioica agglutinin (UDA) is a chitin-binding lectin isoated from the stinging nettle rhizome [1] with insecticidal [2], mtifungal [3], and selective antiviral [4] activities. UDA is capable of inhibiting HIV infectivity [4], a property usually associlted with mannose-binding lectins [4].…”

Section: T Introductionmentioning

confidence: 99%

Ligand‐induced perturbations in Urtica dioica agglutinin

et al. 1995

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The binding of the trisaccharide, N,N',N'-triacet ylchitotriose, to Urtica dioica agglutinin (UDA) was investigated using ~H NMR spectroscopy. UDA is a small antiviral plant lectin containing two homologous 43-amino acid domains. Carbohydrate-induced perturbations occur in one domain of UDA at l risaccharide concentrations below equimolar. Residues in the • .econd domain are shifted at higher carbohydrate concentrations. Fhis data confirms the presence of two binding sites of nonidentical affinities per UDA monomer. Qualitative analysis of the 2D NOESY spectra indicates that UDA contains two short ~tretches of antiparallel/3-sheet. The ~H resonance assignments 10r both antiparallel/3-sheet sequences have been completed and there is one /]-stretch per domain. A number of these t-sheet residues are perturbed in the presence of carbohydrate. [4]. This antiviral effect is inked to its ability to recognize and bind a specific type of :arbohydrate. The present study was designed to characterize he UDA carbohydrate binding sites.Nuclear magnetic resonance (NMR) techniques were used to :xamine the complex between UDA and N,N',N"-triacetylchiotriose. Previous studies concluded that this trisaccharide is :omplementary to the binding site [5]. Because of the small size 89 amino acids) and monomeric nature of UDA, NMR has )rovided an excellent method for studying carbohydrate-intuced perturbations of specific lectin residues. Trisaccharidenduced shifts occur selectively for one set of UDA resonances a concentrations below equimolar and for a second group of • esonances at higher concentrations. These results are consisent with the presence of two binding sites of non-identical lffinities per monomer of UDA. The titration data were used o estimate the binding affinities at each site. A number of the ,'esonances perturbed in the presence of trisaccharide have been ;equentially assigned. We find that most of these perturbed "Corresponding author. Fax: (1) (415) 929 6654. 4bbreviations. UDA, Urtica dioica agglutinin; GlcNAc, N-acetylglu-,:osamine. residues reside in one of the two short stretches of antiparallel t-sheet located in UDA. Materials and methodsUDA was isolated and purified as described previously [6]. A single isolectin of UDA was obtained from reverse phase HPLC using a Vydac C-18 column (Hesperia, CA) and a 45 min linear gradient of 3.(~36% acetonitrile in 0.1% trifluoroacetic acid.The NMR samples were prepared by dissolving lyophilized lectin in either 90% H20/10% D20 or 99.996% D20. The samples prepared in D20 were lyophilized several times from 99.96% D20 prior to the final preparation. In order to maximize solubility, the pH was adjusted to 3.3 3.5 by adding small amounts of DC1. Initial studies monitoring the T~ relaxation of UDA at 35°C as a function of concentration indicated some aggregation of the protein at concentrations above 3 mM. Therefore, protein samples containing 3 mM UDA were used for the twodimensional studies.The NMR experiments were carried out either on the GN-500 or Omega 500 MHz...

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“…SDS-PAGE was done on 12.5 to 25% polyacrylamide gradient gels using a discontinuous system as described by Laemmli (6). Amino acid compositions of individual UDA isolectins were determined as described previously (1 1 (12). Although in the original large-scale purification of UDA the lectin eluted in a more or less symmetrical peak from an SPSephadex column (and in addition yielded a single polypeptide band upon SDS-PAGE) (12), a closer examination under conditions allowing higher resolution revealed the presence of at least three distinct peaks in the elution pattern of UDA from an SP-Sephadex column (Fig.…”

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confidence: 99%

The Urtica dioica Agglutinin Is a Complex Mixture of Isolectins

Damme

Broekaert²,

Peumans³

1988

Plant Physiol.

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Rhizomes of stinging nettle (Urtica dioica) contain a complex mixture of isolectins. Ion exchange chromatography with a high resolution fast protein liquid chromatography system revealed six isoforms which exhibit identical agglutination properties and carbohydrate-binding specificity and in addition have the same molecular structure and virtually identical biochemical properties. However, since the U. dioica agglutinin isolectins differ definitely with respect to their amino acid composition, it is likely that at least some of them are different polypeptides coded for by different genes.

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An unusual lectin from stinging nettle (Urtica dioica) rhizomes

Cited by 132 publications

References 14 publications

Inhibition of Cell-to-Cell Transmission of Human T-Cell Lymphotropic Virus Type 1 In Vitro by Carbohydrate-Binding Agents

Inhibition of Cell-to-Cell Transmission of Human T-Cell Lymphotropic Virus Type 1 In Vitro by Carbohydrate-Binding Agents

Ligand‐induced perturbations in Urtica dioica agglutinin

The Urtica dioica Agglutinin Is a Complex Mixture of Isolectins

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