The <i>Urtica dioica</i> Agglutinin Is a Complex Mixture of Isolectins

Damme, Els J. M. Van; Broekaert, Willem F.; Peumans, Willy J.

doi:10.1104/pp.86.2.598

Cited by 42 publications

(24 citation statements)

References 13 publications

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“…Test Compounds-The mannose-specific plant lectins from Hippeastrum hybrid (HHA) and from G. nivalis (GNA) and the N-acetylglucosamine-specific plant lectin from U. dioica (UDA) were derived and purified from these plants as described previously (15,16) and kindly provided by Prof. E. J. M. Van Damme and Dr. W. Peumans (Ghent, Belgium). Pradimicin A (PRM-A) was obtained from Prof. T. Oki and Prof. Y. Igarashi (Toyama, Japan).…”

Section: Methodsmentioning

confidence: 99%

The Highly Conserved Glycan at Asparagine 260 of HIV-1 gp120 Is Indispensable for Viral Entry

François

Balzarini

2011

Journal of Biological Chemistry

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Carbohydrate-binding agents bind to the N-glycans of HIV-1 envelope gp120 and prevent viral entry. Carbohydrate-binding agents can select for mutant viruses with deleted envelope glycans. Not all glycosylation motifs are mutated to the same extent. Site-directed mutagenesis revealed that deletions destroying the highly conserved 260 NGS 262 glycosylation motif resulted in non-infectious virus particles. We observed a significant lower CD4 binding in the case of the N260Q mutant gp120 virus strains, caused by a strikingly lower expression of gp120 and gp41 in the virus particle. In addition, the mutant N260Q HIV-1 envelope expressed in 293T cells was unable to form syncytia in co-cultures with U87.CD4.CXCR4.CCR5 cells, due to the lower expression of envelope protein on the surface of the transfected 293T cells. The detrimental consequence of this N-glycan deletion on virus infectivity could not be compensated for by the creation of novel glycosylation sites near this amino acid, leaving this uncovered envelope epitope susceptible to neutralizing antibody binding. Thus, the Asn-260 glycan in the gp120 envelope of HIV-1 represents a hot spot for targeting suicidal drugs or antibodies in a therapeutic effort to efficiently neutralize a broad array of virus strains.

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Section: Methodsmentioning

confidence: 99%

The Highly Conserved Glycan at Asparagine 260 of HIV-1 gp120 Is Indispensable for Viral Entry

François

Balzarini

2011

Journal of Biological Chemistry

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“…The chitin-binding domain consists of one Ser and two aromatic amino acid residues located at the intercysteine loop 3 and one aromatic residue at loop 4 ( Figure 1 ). This conserved chitin-binding domain can also be found in class I chitinases, such as Cht-2 from rice Oryza sativa (Takakura et al, 2000) and urtica dioica agglutinin (UDA) from the stinging nettle Urtica dioica (Van Damme et al, 1988). …”

Section: Introductionmentioning

confidence: 99%

Ginkgotides: Proline-Rich Hevein-Like Peptides from Gymnosperm Ginkgo biloba

et al. 2016

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Hevein and hevein-like peptides belong to the family of chitin-binding cysteine-rich peptides. They are classified into three subfamilies, the prototypic 8C- and the 6C- and 10C-hevein-like peptides. Thus far, only five 8C-hevein-like peptides have been characterized from three angiosperms and none from gymnosperm. To determine their occurrence and distribution in the gymnosperm, Ginkgo biloba leaves were examined. Here, we report the discovery and characterization of 11 novel 8C-hevein-like peptides, namely ginkgotides gB1–gB11. Proteomic analysis showed that the ginkgotides contain 41–44 amino acids (aa), a chitin-binding domain and are Pro-rich, a distinguishing feature that differs from other hevein-like peptides. Solution NMR structure determination revealed that gB5 contains a three β-stranded structure shaped by a cystine knot with an additional disulfide bond at the C-terminus. Transcriptomic analysis showed that the ginkgotide precursors contain a three-domain architecture, comprised of a C-terminal tail (20 aa) that is significantly shorter than those of other 8C- and 10C-hevein-like peptides, which generally contain a protein cargo such as a Barwin-like protein (126 aa) or class I chitinase (254 aa). Transcriptomic data mining found an additional 48 ginkgotide homologs in 39 different gymnosperms. Phylogenetic analysis revealed that ginkgotides and their homologs belong to a new class of 8C-hevein-like peptides. Stability studies showed that ginkgotides are highly resistant to thermal, acidic and endopeptidase degradation. Ginkgotides flanked at both the N- and C-terminal ends by Pro were resistant to exopeptidase degradation by carboxypeptidase A and aminopeptidase. Antifungal assays showed that ginkgotides inhibit the hyphal growth of phyto-pathogenic fungi. Taken together, ginkgotides represent the first suite of hevein-like peptides isolated and characterized from gymnosperms. As a group, they represent a novel class of 8C-hevein-like peptides that are Pro-rich and protein-cargo free. Our findings also suggest that the ginkgotide scaffold could be useful for engineering metabolic-stable peptide therapeutics.

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“…PRM-A (molecular weight, 838) was isolated and purified from the fermentation broth of the Actinomyces species Actinomadura hibisca TP-A0016 (12,26). The mannose-specific plant lectins GNA, HHA, and UDA were derived and purified from these plants as previously described (33,34). Polyvinyl alcohol sulfate (PVAS) was kindly provided by S. Görög (Budapest, Hungary).…”

Section: Methodsmentioning

confidence: 99%