Discovery of digestive enzymes in carnivorous plants with focus on proteases

Ravee, Rishiesvari; Salleh, Faris ‘Imadi Mohd; Goh, Hoe-Han

doi:10.7717/peerj.4914

Cited by 42 publications

(32 citation statements)

References 102 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…pteronyssinus has the potential to reveal biochemical pathways that could be exploited in future biocontrol strategies. These “Omic” approaches have accelerated digestive enzyme discovery [15], enabling in silico prediction of biochemical activities coupled with measurement of gene or protein expression. Potent enzymes are excreted by HDM into their surroundings as a by-product of their digestive processes, therefore the presence of putative enzymes in faeces is a strong indicator of a digestive function [16].…”

Section: Introductionmentioning

confidence: 99%

Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus

et al. 2019

View full text Add to dashboard Cite

The European house dust mite Dermatophagoides pteronyssinus is of significant medical importance as it is a major elicitor of allergic illnesses. In this analysis we have undertaken comprehensive bioinformatic and proteomic examination of Dermatophagoides pteronyssinus airmid, identified 12,530 predicted proteins and validated the expression of 4,002 proteins. Examination of homology between predicted proteins and allergens from other species revealed as much as 2.6% of the D . pteronyssinus airmid proteins may cause an allergenic response. Many of the potential allergens have evidence for expression ( n = 259) and excretion ( n = 161) making them interesting targets for future allergen studies. Comparative proteomic analysis of mite body and spent growth medium facilitated qualitative assessment of mite group allergen localisation. Protein extracts from house dust contain a substantial number of uncharacterised D . pteronyssinus proteins in addition to known and putative allergens. Novel D . pteronyssinus proteins were identified to be highly abundant both in house dust and laboratory cultures and included numerous carbohydrate active enzymes that may be involved in cuticle remodelling, bacteriophagy or mycophagy. These data may have clinical applications in the development of allergen-specific immunotherapy that mimic natural exposure. Using a phylogenomic approach utilising a supermatrix and supertree methodologies we also show that D . pteronyssinus is more closely related to Euroglyphus maynei than Dermatophagoides farinae .

show abstract

Section: Introductionmentioning

confidence: 99%

Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Previous studies, including literature review and comparative annotation approaches, accurately identified GO terms and KEGG enzymes strictly related to the carnivory-associated functions among the sequenced carnivorous plants available in public databases [31,32]. Based on this data, we investigated our functional annotation results and observed that U. reniformis had an extensive gene repertoire of carnivory-associated and ROS-related functions (Table 4).…”

Section: Utricularia Reniformis Displays Unique Patterns Of Carnivorymentioning

confidence: 98%

The Terrestrial Carnivorous Plant Utricularia reniformis Sheds Light on Environmental and Life-Form Genome Plasticity

Silva

Moraes

Penha

et al. 2019

IJMS

View full text Add to dashboard Cite

Utricularia belongs to Lentibulariaceae, a widespread family of carnivorous plants that possess ultra-small and highly dynamic nuclear genomes. It has been shown that the Lentibulariaceae genomes have been shaped by transposable elements expansion and loss, and multiple rounds of whole-genome duplications (WGD), making the family a platform for evolutionary and comparative genomics studies. To explore the evolution of Utricularia, we estimated the chromosome number and genome size, as well as sequenced the terrestrial bladderwort Utricularia reniformis (2n = 40, 1C = 317.1-Mpb). Here, we report a high quality 304 Mb draft genome, with a scaffold NG50 of 466-Kb, a BUSCO completeness of 87.8%, and 42,582 predicted genes. Compared to the smaller and aquatic U. gibba genome (101 Mb) that has a 32% repetitive sequence, the U. reniformis genome is highly repetitive (56%). The structural differences between the two genomes are the result of distinct fractionation and rearrangements after WGD, and massive proliferation of LTR-retrotransposons. Moreover, GO enrichment analyses suggest an ongoing gene birth–death–innovation process occurring among the tandem duplicated genes, shaping the evolution of carnivory-associated functions. We also identified unique patterns of developmentally related genes that support the terrestrial life-form and body plan of U. reniformis. Collectively, our results provided additional insights into the evolution of the plastic and specialized Lentibulariaceae genomes.

show abstract

“…Cysteine cathepsins are not only lysosomal peptidases, as there is clear evidence of their localization in other cellular compartments, such as the nucleus, cytoplasm and plasma membranes (Wex et al, 2003;Hsing and Rudensky, 2005;Salminen-Mankonen et al, 2007). Of particular interest are the cysteine cathepsins found in the multi-enzyme digestive complex of some insects (Vinokurov et al, 2005(Vinokurov et al, , 2006a(Vinokurov et al, ,b, 2009Semashko et al, 2014), as well as carnivorous plants (Ravee et al, 2018). Being digestive, these cathepsins not only have a higher degradomic potential than ordinary lysosomal cathepsins because of expanded substrates, but due to the structure of their natural substrates, they also exhibit specificity that is not characteristic of most known lysosomal cathepsins.…”

Section: Introductionmentioning

confidence: 99%

New Glutamine-Containing Substrates for the Assay of Cysteine Peptidases From the C1 Papain Family

Filippova

Dvoryakova

Sokolenko

et al. 2020

Front. Mol. Biosci.

View full text Add to dashboard Cite

New substrates with glutamine in the P1-position are introduced for the assay of peptidases from the C1 papain family, with a general formula of Glp-Phe-Gln-X, where Glp is pyroglutamyl and X is pNA (p-nitroanilide) or AMC (4-amino-7-methylcoumaride). The substrates have a simple structure, and C1 cysteine peptidases of various origins cleave them with high efficiency. The main advantage of the substrates is their selectivity for cysteine peptidases of the C1 family. Peptidases of other clans, including serine trypsin-like peptidases, do not cleave glutamine-containing substrates. We demonstrate that using Glp-Phe-Gln-pNA in combination with a commercially available substrate, Z-Arg-Arg-pNA, provided differential determination of cathepsins L and B. In terms of specific activity and kinetic parameters, the proposed substrates offer improvement over the previously described alanine-containing prototypes. The efficiency and selectivity of the substrates was demonstrated by the example of chromatographic and electrophoretic analysis of a multi-enzyme digestive complex of stored product pests from the Tenebrionidae family.

show abstract

Discovery of digestive enzymes in carnivorous plants with focus on proteases

Cited by 42 publications

References 102 publications

Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus

Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus

The Terrestrial Carnivorous Plant Utricularia reniformis Sheds Light on Environmental and Life-Form Genome Plasticity

New Glutamine-Containing Substrates for the Assay of Cysteine Peptidases From the C1 Papain Family

Contact Info

Product

Resources

About