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Brenda S Oppert

Research Molecular Biologist
Dr. Brenda Oppert                

Dr. Brenda Oppert
Research Molecular Biologist

ATTN: Brenda Oppert
1515 College Avenue
Manhattan, KS  66502
Telephone: 785.776.2780


B.S., Biology, Kansas State University

M.S., Biology, Kansas State University

Ph.D., Protein Biochemistry, Kansas State University

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Dr. Oppert’s research historically has focused on how stored product insects digest food, looking for enzymes/proteins that are critical for survival as potential targets for new control products. Additionally, she has studied mode of action and resistance mechanisms to Bt toxins in stored product moths and beetles. Since 2007, she has applied high throughput sequencing to functional genomics of stored product insects. Using transcriptome sequencing and bioinformatics, Dr. Oppert applies gene expression analysis (RNASeq) to the evaluation of toxin mode of action and insecticide resistance in Tribolium castaneum and Tenebrio molitor. She also uses RNASeq in developmental stages and tissues to identify potential targets for RNAi and CRISPR in stored product pests. She leads projects sequencing the genomes of Rhyzopertha dominica, T. molitor, and Sitophilus oryzae.
   Recently, Dr. Oppert began working on genomic resources for the development of insects as food to meet the global protein sustainability crisis. Working with All Things Bugs LLC, she collaborated on a Department of Defense DARPA SBIR project to develop genetic resources for T. molitor, Gryllodes sigillatus, and Acheta domesticus. The research will improve the protein and vitamin content in insects for animal feed, and solve problems associated with disease in crickets and other species.

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Dunaevsky, Y. E., V. F. Tereshchenkova, B. Oppert, M. A. Belozersky, I. Y. Filippova, and E. N. Elpidina. 2020. Human proline specific peptidases: a systemic analysis. Biochim. Biophys. Acta 1864: 129636.
Filippova, I. Y., E. A. Dvoryakova, N. I. Sokolenko, T. R. Simonyan, V. F. Tereshchenkova, N. I. Zhiganov, Y. E. Dunaevsky, M. A. Belozersky, B. Oppert, and E. N. Elpidina. 2020. New glutamine-containing substrates for the assay of cysteine peptidases from the C1 papain family. Front. Mol. Biosci. 7: 578758.
Oeyen, J. P. et al. (Oppert, B. #50). 2020. Sawfly genomes reveal evolutionary acquisitions that fostered the mega-radiation of parasitoid and eusocial Hymenoptera. Genome Biol. Evol. 12: 1099-1188.
Oppert, B. S., L. C. Perkin, M. Lorenzen, and A. T. Dossey. 2020. Transcriptome analysis of life stages of the house cricket, Acheta domesticus, to improve insect crop production. Sci. Rep. 10: 3471.
Sparks, M., D. E. Gundersen, R. Bansal, B. S. Oppert, M. F. Poelchau, C. Childers, J. H. Rhoades, A. S. Velamuri, J. B. Benoit, H. Chao, M. B. Blackburn, and J. Johnston. 2020. Brown marmorated stink bug, Halyomorpha halys (Stål), genome: Underpinngs of polyphagy, insecticide resistance potential and biology of a top worldwide pest. BMC Genomics 21: 227.
Athanassiou, C. G., N. G. Kavallieratos, D. L. Brabec, B. S. Oppert, R. N. C. Guedes, and J. F. Campbell. 2019. From immobilization to recovery: Towards the development of a rapid diagnostic indicator for phosphine resistance. J. Stored Prod. Res. 80: 28-33.
Elpidina, E. N., T. A. Semashko, Y. A. Smirnova, E. A. Dvoryakova, Y. E. Dunaevsky, M. A. Belozersky, M. V. Serebryakova, E. V. Klyachko, A. O Abd El-latif, B. Oppert, and I. Y. Filippova. 2019. Direct detection of cysteine peptidases for MALDI-TOF MS analysis using fluorogenic substrates. Anal. Biochem. 567: 45-50.
Hubhachen, Z., H. Jiang, D. Schlipalius, Y. Park, R. N. C. Guedes, B. Oppert, G. Opit, and T. W. Phillips. 2019. A CAPS marker for determination of strong phosphine resistance in Tribolium castaneum from Brazil. J. Pest Sci. p. 1-8.
Oppert, B., and L. Perkin. 2019. RNAiSeq: How to see the big picture. Front. Microbiol. 10: 2570.
Oppert, B., F.-C. Chu, S. Reyna, S. Pinzi, S. Adrianos, L. Perkin, and M. Lorenzen. 2019. Effects of targeting eye color in Tenebrio molitor through RNA interference of tryptophan 2,3-dioxygenase (vermilion): Implications for insect farming. Arch. Insect Biochem. Physiol. 10: e21546.