Xianchun Li

Xianchun Li

Professor, Entomology
Professor, Entomology / Insect Science - GIDP
Professor, BIO5 Institute
Primary Department
Department Affiliations
Contact
(520) 626-1749

Work Summary

Xianchun Li's research aims to use genetics to shed light on the defense signaling of plants and the counterdefense of herbivorous insects, which may result in the design of new insecticides for crops like corn, in defense against the corn earworm. Additionally, Dr. Li's research is to define, globally, the regulatory triangle between nuclear receptors (NRs), their ligands, and cytochrome P450s (P450s) in Drosophila melanogaster, and to investigate the molecular mechanisms of Bt and conventional insecticide resistance.

Research Interest

Xianchun Li, PhD, is interested in understanding the physiological, biochemical, molecular and evolutionary bases of fundamental processes in the life history of insects such as embryonic polarity, metamorphosis, developmental commitment, host usage and environmental adaptation. One focus of his research is to elucidate the reciprocal signaling interactions between plants and insects, and the resulted on-going defense (in the case of plants) / counterdefense (in the case of herbivorous insects) phenotypic arm race over ecological time scale, with emphasis on the genetic machinery that percepts and transduces the reciprocal cues into genome and regulate defense / counterdefense phenotypes. Working systems include Helicoverpa zea, the corn earworm, a polyphagous noctuide of economic importance, and Drosophila melanogaster, the fruit fly, a model organism. State of arts and traditional techniques are combining to identify the cues and to uncover the signaling transduction cascade that links environmental cues, gene expression and the resulted defense/counterdefense phenotypes. This research may lead to characterization of genes for designing new insecticides and/or genetically modifying crops. The second focus of Dr. Li’s research is to define, globally, the regulatory triangle between nuclear receptors (NRs), their ligands, and cytochrome P450s (P450s) in Drosophila melanogaster. Nuclear receptors (NRs) constitute a transcription factor superfamily that has evolved to sense and bind endogenous (e.g., hormones) and/or exogenous (e.g., naturally-occurring or synthetic xenobiotics) signal compounds, resulting in differential expression of particular target genes, which underlies a range of fundamental biological processes, including growth, development, reproduction, behavior, host usage, and environmental adaptation. Many of those cue chemicals, namely NR ligands, are synthesized and/or metabolized by members of the P450s gene superfamily, whose expression may be regulated by certain NRs. Bioinformatics analyses as well as systematic functional genomic techniques such as microarray, X-ChIP, mutation and ectopic expression will be combined to define the genome-wide regulatory interaction loops between NRs and P450s as well as to assign, at least partially, functions of individual NRs and P450s in the life history of fruit fly. Given the evolutionary conservations of homologous NRs and P450s between vertebrates and invertebrates, the results obtained in this project are expected to provide insights into the reciprocal regulatory interactions between NRs and P450s in other animals including humans as well as to provide great insights into new avenue for human NR ligand identification and NR-related drug design. The third focus of his research is to investigate the molecular mechanisms of Bt and conventional insecticide resistance, which is a major threat in current IPM system. In collaboration with Dr. Bruce Tabashnik, Timothy Dennehy, and Yves Carriere in our Department, Dr. Li is going to compare Bt toxin binding affinity and other defects of natural (s, r1, r2, r3) and artificial mutant PBW (Pink Bollworm) cadherin proteins and thus define the key functional domains of PBW cadherin.

Publications

Chen, S., & Xianchun, L. i. (2008). Molecular characterization of the first intact Transib transposon from Helicoverpa zea. Gene, 408(1-2), 51-63.

PMID: 18031956;Abstract:

Transib is a superfamily of DNA transposons recently reconstructed in silico from degenerate elements in the genomes of Drosophila melanogaster and Anopheles gambiae. Here we report characterization of the first intact Transib transposon designated Hztransib from Helicoverpa zea. At least two Hztransib copies (one full-length, one internally-deleted) exist in the genomes of a midgut cell line and a laboratory strain of H. zea. The full-length Hztransib has 3518 bp including a 5′ terminal inverted repeat (TIR) of 552 bp, a promoter sequence of 381 bp, an intact open reading frame encoding 507 amino acids, and a 3′ TIR of 502 bp, and is flanked by 5-bp (CGTCG) target site duplications. The full-length Hztransib is transcriptionally active, producing an 3′-truncated mRNA lacking a termination codon (known as nonstop mRNA) due to alternative polyadenylation in two somatic tissues (midgut and fat body) and one germline tissue (ovary). A BLAST search with the deduced Hztransib transposase identified 51 novel Transib elements from 11 insect genomes. While the full-length Hztransib inserts into the 5′-flanking region of a xenobiotic-metabolizing P450 gene CYP6B8 in the midgut cell line, it does not insert into the 5′-flanking region of CYP6B8 in the laboratory strain. Such an insertion dimorphism, together with its complete structural features and mRNA transcripts, demonstrates that the full-length Hztransib not only represents the first known intact Transib element in any organism, but has been recently transposed in H. zea. The fact that the intact Hztransib is transcribed into a 3′-truncated nonstop mRNA which may encode a non-functional transposase or be blocked from further translation via nonstop mRNA decay suggests that it is silenced at the translational or transpositional level. © 2007 Elsevier B.V. All rights reserved.

Wei, J., Liang, G., Wu, K., Gu, S., Guo, Y., Ni, X., & Li, X. (2017). Cytotoxicity and binding profiles of activated Cry1Ac and Cry2Ab to three insect cell lines. Insect science.

While Cry1Ac has been known to bind with larval midgut proteins cadherin, APN (amino peptidase N), ALP (alkaline phosphatase) and ABCC2 (adenosine triphosphate-binding cassette transporter subfamily C2), little is known about the receptors of Cry2Ab. To provide a clue to the receptors of Cry2Ab, we tested the baseline cytotoxicity of activated Cry1Ac and Cry2Ab against the midgut and fat body cell lines of Helicoverpa zea and the ovary cell line of Spodoptera frugiperda (SF9). As expected, the descending order of cytotoxicity of Cry1Ac against the three cell lines in terms of 50% lethal concetration (LC50 ) was midgut (31.0 μg/mL) > fat body (59.0 μg/mL) and SF9 cell (99.6 μg/mL). By contrast, the fat body cell line (LC50 = 7.55 μg/mL) was about twice more susceptible to Cry2Ab than the midgut cell line (16.0 μg/mL), the susceptibility of which was not significantly greater than that of SF9 cells (27.0 μg/mL). Further, ligand blot showed the binding differences between Cry1Ac and Cry2Ab in the three cell lines. These results indicated that the receptors of Cry2Ab were enriched in fat body cells and thus largely different from the receptors of Cry1Ac, which were enriched in midgut cells.

Chen, W., Liu, C., Xiao, Y., Zhang, D., Zhang, Y., Li, X., Tabashnik, B. E., & Wu, K. (2015). A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera. PloS one, 10(4), e0126288.

Evolution of resistance by insects threatens the continued success of pest control using insecticidal crystal (Cry) proteins from the bacterium Bacillus thuringiensis (Bt) in sprays and transgenic plants. In this study, laboratory selection with Cry1Ac yielded five strains of cotton bollworm, Helicoverpa armigera, with resistance ratios at the median lethal concentration (LC50) of activated Cry1Ac ranging from 22 to 1700. Reduced activity and reduced transcription of an alkaline phosphatase protein that binds Cry1Ac was associated with resistance to Cry1Ac in the four most resistant strains. A Cry1Ac-binding fragment of alkaline phosphatase from H. armigera (HaALP1f) was not toxic by itself, but it increased mortality caused by Cry1Ac in a susceptible strain and in all five resistant strains. Although synergism of Bt toxins against susceptible insects by toxin-binding fragments of cadherin and aminopeptidase N has been reported previously, the results here provide the first evidence of synergism of a Bt toxin by a toxin-binding fragment of alkaline phosphatase. The results here also provide the first evidence of synergism of a Bt toxin by any toxin-binding peptide against resistant insects.

Dennehy, T. J., Degain, B. A., Harpold, V. S., Zaborac, M., Morin, S., Fabrick, J. A., Nichols, R. L., Brown, J. K., Byrne, F. J., & Xianchun, L. i. (2010). Extraordinary resistance to insecticides reveals exotic Q biotype of Bemisia tabaci in the New World. Journal of Economic Entomology, 103(6), 2174-2186.

PMID: 21309242;Abstract:

A strain of the whitefly Bemisia tabaci (Gennadius) possessing unusually high levels of resistance to a wide range of insecticides was discovered in 2004 in the course of routine resistance monitoring in Arizona. The multiply resistant insects, collected from poinsettia (Euphorbia pulcherrima Willd. ex Klotzsch) plants purchased at a retail store in Tucson, were subjected to biotype analysis in three laboratories. Polyacrylamide gel electrophoresis of naphthyl esterases and sequencing of the mitochondrial cytochrome oxidase I gene (780 bp) confirmed the first detection of the Q biotype of B. tabaci in the New World. This U.S. Q biotype strain, referred to as Poinsettia'04, was highly resistant to two selective insect growth regulators, pyriproxyfen and buprofezin, and to mixtures of fenpropathrin and acephate. It was also unusually low in susceptibility to the neonicotinoid insecticides imidacloprid, acetamiprid, and thiamethoxam, relative to B biotype whiteflies. In 100 collections of whiteflies made in Arizona cotton (Gossypium spp.), vegetable, and melon (Cucumis melo L.) fields from 2001 to 2005, no Q biotypes were detected. Regions of the United States that were severely impacted by the introduction of the B biotype of B. tabaci in the 1980s would be well advised to promote measures that limit movement of the Q biotype from controlled environments into field systems and to formulate alternatives for managing this multiply-resistant biotype, in the event that it becomes more widely distributed.

Xianchun, L. i., Berenbaum, M. R., & Schuler, M. A. (2000). Molecular cloning and expression of CYP6B8: A xanthotoxin-inducible cytochrome P450 cDNA from Helicoverpa zea. Insect Biochemistry and Molecular Biology, 30(1), 75-84.

PMID: 10646973;Abstract:

Xanthotoxin, a plant allelochemical, induces α-cypermethrin insecticide tolerance in Helicoverpa zea (corn earworm); inhibition of tolerance by piperonyl butoxide implicates cytochrome P450 monooxygenases (P4950s) in the detoxification of this insecticide. To characterize the xanthotoxin-inducible P450 that might mediate α-cypemethrin tolerance in this species, a cDNA library prepared from xanthotoxin-induced H. zea fifth instar larvae was screened with cDNAs encoding furanocoumarin-metabolizing P450s from Papilio polyxenes (CYP6B1v2) and P. glaucus (CYP6B4v2) as well as a sequence-related P450 from Helicoverpa armigera (CYP6B2). One full-length cDNA isolated in this screening shares 51-99% amino acid identity with the CYP6B subfamily of P450S isolated from Papilio and Helicoverpa species and, thus, has been designated CYP6B8. All of these CYP6B subfamily members share a number of highly conserved domains, including substrate recognition site 1 (SRS 1) that is critical for xanthotoxin metabolism by CYP6B 1 v2 from Papilio polyxenes and coumarin metabolism by CYP2a5 from Mus musculus. Northern and RT-PCR analyses indicate that CYP6B8 expression is strongly induced by xanthotoxin and phenobarbital and negligibly induced by α-cypermethrin.