The type-1 and type-2 ribosome-inactivating proteins from Iris confer transgenic tobacco plants local but not systemic protection against viruses

Vandenbussche, Frank; Peumans, Willy J.; Desmyter, Stijn; Proost, Paul; Ciani, Marialibera; Damme, Els J.M. Van

doi:10.1007/s00425-004-1334-2

Cited by 29 publications

(29 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several lines of evidence support the idea that ricin-B related lectins play a role in plant defense against pathogens (Chen et al, 2002b; Vandenbussche et al, 2004a,b) and insects (Wei et al, 2004; Shahidi-Noghabi et al, 2009). Over-expressing SNA-I′ or SNA-V from S. nigra in transgenic tobacco (Samsun NN) plants enhances the tobacco plant’s resistance against infection with tobacco mosaic virus.…”

Section: Pathogen Recognition Based On Protein–carbohydrate Interactionsmentioning

confidence: 77%

“…Over-expressing SNA-I′ or SNA-V from S. nigra in transgenic tobacco (Samsun NN) plants enhances the tobacco plant’s resistance against infection with tobacco mosaic virus. Though the antiviral effect is clearly related to the amount of protein expressed it cannot be related to an increased expression of pathogenesis-related proteins (Chen et al, 2002b; Vandenbussche et al, 2004a,b). Furthermore, no clear correlation was observed between in planta antiviral activity of the transgenic tobacco lines and the in vitro N -glycosidase activity of the proteins toward genomic RNA of the tobacco mosaic virus, suggesting that the in planta antiviral activity of these RIPs may rely on a direct interaction with the virus (Vandenbussche et al, 2004a).…”

Section: Pathogen Recognition Based On Protein–carbohydrate Interactionsmentioning

confidence: 99%

See 1 more Smart Citation

Lectin domains at the frontiers of plant defense

2014

View full text Add to dashboard Cite

Plants are under constant attack from pathogens and herbivorous insects. To protect and defend themselves, plants evolved a multi-layered surveillance system, known as the innate immune system. Plants sense their encounters upon perception of conserved microbial structures and damage-associated patterns using cell-surface and intracellular immune receptors. Plant lectins and proteins with one or more lectin domains represent a major part of these receptors. The whole group of plant lectins comprises an elaborate collection of proteins capable of recognizing and interacting with specific carbohydrate structures, either originating from the invading organisms or from damaged plant cell wall structures. Due to the vast diversity in protein structures, carbohydrate recognition domains and glycan binding specificities, plant lectins constitute a very diverse protein superfamily. In the last decade, new types of nucleocytoplasmic plant lectins have been identified and characterized, in particular lectins expressed inside the nucleus and the cytoplasm of plant cells often as part of a specific plant response upon exposure to different stress factors or changing environmental conditions. In this review, we provide an overview on plant lectin motifs used in the constant battle against pathogens and predators during plant defenses.

show abstract

Section: Pathogen Recognition Based On Protein–carbohydrate Interactionsmentioning

confidence: 77%

Section: Pathogen Recognition Based On Protein–carbohydrate Interactionsmentioning

confidence: 99%

Lectin domains at the frontiers of plant defense

2014

View full text Add to dashboard Cite

show abstract

“…The toxicity of some ricin homologs from Abrus precatorius , Sambucus nigra and Viscum album has been confirmed but it should be mentioned that not all proteins are as toxic as ricin [68]. Expression analysis and overexpression of type-2 RIPs provide evidence that these proteins play a role in plant defense of the plant against pathogens (tobacco mosaic virus) and pest insects (caterpillars, aphids) [69,70,71,72,73]. …”

Section: Resultsmentioning

confidence: 99%

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

Holle

Schutter

Eggermont

et al. 2017

IJMS

View full text Add to dashboard Cite

Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsis thaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.

show abstract

“…These antiviral activities possibly rely on the direct depurination of the viral genomic RNA, since the expression of SNA-V did not induce the synthesis of pathogenesis-related proteins. Similarly, the type 2 RIP from Iris showed antiviral activity to tobacco mosaic virus and tobacco etch virus, without alteration of gene expression for pathogenesis-related proteins (Vandenbussche et al 2004b;Desmyter et al 2003). …”

Section: Antiviral Activity Of Type 2 Ripsmentioning

confidence: 95%

Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

View full text Add to dashboard Cite

As part of their defense system different plant species each express a diverse set of defense proteins, among them proteins with lectin domains. The whole group of plant lectins assembles all proteins that have the ability to recognize and bind specific carbohydrate structures. Based on the sequence and the conformation of the carbohydrate recognition domains several lectin families are distinguished. Although many lectins are composed only of carbohydrate binding domains, several lectins are chimeric proteins composed of a lectin domain and another unrelated domain. In some cases this second domain can be considered as a toxin domain. This chapter focuses on different types of plant AB toxins and their physiological importance in the battle against pathogens and predators. Most information is available on type 2 ribosome-inactivating proteins in which an N-glycosidase domain is linked through a disulfide bridge to a lectin domain. More recently chimeric proteins consisting of one or more lectin domains and a dirigent domain or aerolysin domain have also been discovered. Although these AB toxins all consist of a lectin domain and a toxin domain, the nature of the toxin and the lectin domain are different resulting in proteins with different carbohydrate binding properties as well as a different mode of action for toxicity.

show abstract

The type-1 and type-2 ribosome-inactivating proteins from Iris confer transgenic tobacco plants local but not systemic protection against viruses

Cited by 29 publications

References 42 publications

Lectin domains at the frontiers of plant defense

Lectin domains at the frontiers of plant defense

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

Plant AB Toxins with Lectin Domains

Contact Info

Product

Resources

About