Molecular, Cell and Systems Biology

Sarjeet Gill

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Phone: (951) 827-4621
Fax: (951) 827-3087
Office Location: 3117 Biological Sciences
Office Hours:
Email: sarjeet.gill@ucr.edu

Sarjeet S. Gill, Ph.D.

Distinguished Professor Cell Biology and Toxicologist


Mechanisms of toxicity and membrane transport

The lab has three principal research areas all utilizing a cellular and molecular approach to elucidate the mechanisms of toxicity and cell membrane transport. The focus of the first area is to elucidate the mode of action of toxins derived from Bacillus thuringiensis and Clostridium bifermantans. The research aims to gain a molecular understanding of the characteristics of these toxins and how they interact with cellular targets, which result in a disruption of ion regulation and lethality. Current research projects include the elucidation of structure and function relationships of these bacterial toxins; toxin receptor isolation and an attempt to define how these receptors modulate in vivo toxicity.

A second research focus is on insect cell membrane transport, and how toxins affect this function. Currently, the laboratory is characterizing ion and amino acid transporters. The lab is focusing on the Na+/H+ exchangers that play a key role in transport of high salt load on mosquitoes following a blood meal. Studies include functional analysis and regulation of these exchangers in the mosquito Malpighian tubules. In conjunction with this effort the lab is also characterizing transport processes involved in nutrient uptake following a blood meal, and the regulation of such transport.

Finally, the lab has a long ongoing interest in xenobiotic metabolism and characterization of the effects of environmental toxicants on mammalian systems. This molecular toxicology emphasis defines how toxicants regulate the expression of the soluble epoxide hydrolase and fatty acid metabolism.


  • Patrick, M. L., K. Aimanova, H. R. Sanders and S. S. Gill. 2006. Na+/K+ ATPase and V-type H+ ATPase expression patterns in the osmoregulatory organs of larval and adult mosquito Aedes aegypti. J. Exp. Biol. In Press
  • Pullikuth, A. K., K. Aimanova, W. Kang'ethe, H. R. Sanders and S. S. Gill. 2006. Molecular characterization of sodium/proton exchanger 3 (NHE3) from the yellow fever vector, Aedes aegypti. J. Exp. Biol. 209:3529-3544.
  • Aimanova, K.G., M. Zhuang and S. S. Gill. 2006. Expression of Cry1Ac cadherin receptors in insect midgut and cell lines. J Invertebr Pathol. 92:178-187.
  • Fernandez L.E., K. G. Aimaniova, S. S. Gill, A. Bravo, and M. Soberón. 2006. A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem. J. 394:77-84.
  • Perez C, L.E. Fernandez, J. Sun, J.L. Folch, S. S. Gill, M. Soberon, and A. Bravo A. 2005. Bacillus thuringiensis subsp. israelensis Cyt1Aa synergizes Cry11Aa toxin by functioning as a membrane-bound receptor. Proc Natl Acad Sci U S A. 102:18303-18308.
  • Liu Y, Y. Zhang, K. Schmelzer, T.S. Lee, X. Fang, Y. Zhu, A. A. Spector, S. S. Gill, C. Morisseau, B. D. Hammock, and J. Y. Shyy. 2005. The antiinflammatory effect of laminar flow: The role of PPAR{gamma}, epoxyeicosatrienoic acids, and soluble epoxide hydrolase. Proc. Natl. Acad. Sci. USA 102: 16747-16752.
  • Xie, R., M. Zhuang, L. S. Ross, I. Gomez, D. I. Oltean, A. Bravo, M. Soberon, and S. S. Gill. 2005. Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins. J. Biol. Chem. 280:8416-8425.
  • Fernandez L.E., C. Perez, L. Segovia, M. H. Rodriguez, S. S. Gill, A. Bravo, and M. Soberón. 2005. Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae through loop alpha-8 of domain II.. FEBS Lett. 579:3508-14.
  • Sanders, H. R., B. D. Foy, A. M. Evans, L. S. Ross, B. J. Beaty, K. E. Olson and S. S. Gill. 2005. Sindbis virus induces transport processes and alters expression of innate immunity pathway genes in the midgut of the disease vector, Aedes aegypti. Insect Biochem. Mol. Biol. 35:1293-307.
  • Bravo, A., S. S. Gill, A. Bravo, and M. Soberón. 2005. Bacillus thuringiensis, with Resistance mechanisms, In Comprehensive Molecular Insect Science (Ed. L.I. Gilbert, I. Kostas and S.S.Gill), Elsevier, Vol 6, 175-205.
  • Gilbert, L. I., I. Kostas and S. S. Gill. 2005. Comprehensive Molecular Insect Science. Vols 1-7. Elsevier Pergammon, Amsterdam.
  • Corton, J.C., U. Apte, S. P. Anderson, P. Limaye, L. Yoon, J. Latendresse, C. Dunn, J. I. Everitt, K. A. Voss, C. Swanson, C. Kimbrough, J. S. Wong, S. S. Gill, R. A. Chandraratna, M. K. Kwak, T. W. Kensler, T. M. Stulnig, K. R. Steffensen, J. A. Gustafsson, H. M. Mehendale. 2004. Mimetics of caloric restriction include agonists of lipid-activated nuclear receptors. J. Biol. Chem. 279:46204-46212
  • Bravo, A., Gómez, I., R. Miranda-CasoLuengo, J. Conde, C. Munoz-Garay, J. Sánchez, M. Zhuang, S. S. Gill, and M. Soberón. 2004. Manduca sexta aminopeptidase N drives the oligomeric form of Bacillus thuringiensis Cry1Ab toxin and the cadherin receptor to plasma membrane microdomains. Biochim. Biophys. Acta. 1667:38-46.
  • Umesh, A. B. N. Cohen, L. S. Ross, and S. S. Gill. 2003. Functional characterization of a glutamate/aspartate transporter from the mosquito, Aedes aegypti. J. Exp. Biol. 206:241-2255.
  • Filippov, V., K. Aimanova and S. S. Gill. 2003. Expression of an Aedes aegypti cation-chloride cotransporter and its Drosophila homologues. Insect Mol. Biol. 12:319-331.
  • Jin, X., K. Aimanova, L. S. Ross and S. S. Gill. 2003. Identification, functional characterization and expression of a LAT type amino acid transporter from the mosquito Aedes aegypti. Insect Biochem. Mol. Biol. 33: 815-827.
  • Pullikuth, A. K., V. Filippov and S. S. Gill. 2003. Phylogeny and cloning of ion transporters in mosquitoes. J. Exp. Biol. 206:3857-3868.
  • Sanders, H. R., A. M. Evans, L. S. Ross, and S. S. Gill. 2003. Blood meal induces global changes in midgut gene expression in the disease vector, Aedes aegypti. Insect Biochem. Mol. Biol. 33:1105-1122.

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Molecular, Cell and Systems Biology
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