Gene Sequences of Potential Targets of Insecticidal PF2 Lectin Identified from the Larval De Novo Transcriptome of the Mexican Bean Weevil (Zabrotes Subfasciatus; Boheman 1833)

Abstract

The available genomic and proteomic information of non-model organisms is often underrepresented in public databases hindering their study at molecular, cellular, and physiological levels. Information on Zabrotes subfasciatus (Mexican bean weevil) is poorly represented in databases, yet it is a major pest of common beans. We report the transcriptome of Z. subfasciatus larvae; transcripts were sequenced using an Illumina RNA-Seq technology and assembled de novo identifying 29,029 unigenes with an average size of 1168 bp and an N50 value of 2196 bp. About 15,124 unigenes (52%) were functionally annotated and categorized. Further analysis revealed 30 unigene sequences encoding putative targets of the insecticidal PF2 lectin. The complete deduced amino acid sequences of eight selected proteins potentially related to insecticidal mechanism of Palo Fierro 2 (PF2) were used for predicting probable N-glycosylation sites and analyzing phylogenetic relationships with insect sequences. This work provides a dramatic increase in the genetic resources available for Coleopterans and set the basis for developing future studies on biological aspects and potential control strategies for Z. subfasciatus.

Antiproliferative Potential of Olneya tesota PF2 Lectin in Human Acute Monocytic Leukemia Cells

“…Additionally, PF2 lectin was able to recognize a number of soluble and membrane proteins in the Z. subfasciatus middle intestine during larval development. The PF2 lectin targets identified in Z. subfasciatus included α‐amylase, the V‐type proton ATPase, arginine kinase, prohibitin, polyubiquitin, actin, ATP‐dependent RNA helicase, ATP synthase subunit alpha, mitochondrial‐processing peptidase, α‐tubulin, the odorant receptor, and cytochrome c oxidase [15,16,20,21] . This suggests that these proteins could potentially mediate lectin toxicity.…”

“…The PF2 lectin targets identified in Z. subfasciatus included α-amylase, the V-type proton ATPase, arginine kinase, prohibitin, polyubiquitin, actin, ATP-dependent RNA helicase, ATP synthase subunit alpha, mitochondrial-processing peptidase, α-tubulin, the odorant receptor, and cytochrome c oxidase. [15,16,20,21] This suggests that these proteins could potentially mediate lectin toxicity. Thus, PF2 could interact with the orthologous receptors on human THP-1 cells.…”

“…The PF2 lectin, isolated from the seeds of the desert wild legume Olneya tesota (desert ironwood), is toxic to the Zabrotes subfasciatus beetle and displays recognition specificity for triantennary tetrasialylated glycans. [16] Furthermore, the expression of proteins recognized by PF2 varies according to the life cycle stage of the insect. [17] Interestingly, the sialylation levels and profiles of siaoglycoconjugates on the surface of and within THP-1 monocytes vary during differentiation into macrophages and subsequent polarization.…”

“…The PF2 lectin, isolated from the seeds of the desert wild legume Olneya tesota (desert ironwood), is toxic to the Zabrotes subfasciatus beetle and displays recognition specificity for triantennary tetrasialylated glycans [16] . Furthermore, the expression of proteins recognized by PF2 varies according to the life cycle stage of the insect [17] .…”

Transcriptome analysis of the endangered dung beetle Copris tripartitus (Coleoptera: Scarabaeidae) and characterization of genes associated to immunity, growth, and reproduction

“…The IPS-based conserved domain search identified C2H2-like zinc-finger, protein kinase, immunoglobulin-like fold, carboxylesterase type B, zinc finger (RING-type), and reverse transcriptase as being among the most abundant domains in the unigenes. Such domains were also widely distributed in transcriptome-derived unigenes of H. hampei [ 32 ], Asian giant hornet V. mandarinia [ 18 ], Nymphalid butterfly Fabriciana nerippe [ 2 ], and Mexican bean weevil Zabrotes subfasciatus [ 33 ]. C2H2-like zinc-finger domains are among the most abundant protein domains belonging to the family of transcription factors that regulate gene expression in complex eukaryotes.…”