Edward Eisenstein

Associate Professor

Eisenstein Group


Email: eisenste@umd.edu

Call: (240) 314-6244


  • Postdoctoral Research, Molecular Biology, University of California Berkeley, 1985-1989
  • Ph.D., Biochemistry, Georgetown University, 1985
  • B.S., Biology and Chemistry, Saint Joseph’s College, 1979


The Eisenstein laboratory is building next-generation bioenergy plants with enhanced capacity to manage biotic and abiotic challenges. Their strategy is to derive mechanistic information from multidisciplinary tools, ranging from molecular and structural biology, to plant, systems and synthetic biology, as well as protein design and engineering, to develop superior traits. These improvements are being introduced into plants via genome engineering in order to extend our diminishing supply of fossil fuels. In addition, Dr. Eisenstein is applying systems engineering principles to improve the development of protein biopharmaceuticals. 


Poplar Trees as New Biofuels 

A challenge to improving the quality and availability of biofuel feedstocks is that transgenic plants with enhanced biotechnology traits (such as higher ethanol yields) often display reduced fitness, lower biomass, and an increased susceptibility to disease. The Eisenstein lab focuses on poplar trees as a feedstock because they grow rapidly, produce significant biomass in short times, and yield substantial energy. Through several profitable collaborations, the group is addressing the following three challenges to improving poplar as a bioenergy feedstock:

Increase plant resistance to pathogens

Plant pathogens use a variety of mechanisms to infect and spread disease, but the plant immune system limits infection by recognizing pathogen effectors and activating local cell death. Leaf rust – one of the most important diseases in poplar - is caused by the pathogenic fungus Melampsora larici-populina. The lab is elucidating the components of the poplar defense response that are targeted by rust effectors, as well as the components of poplar nutrient homeostasis that are hijacked by the pathogen to spread disease. Additionally, the lab is determining the structures of receptor-effector complexes to unravel the elementary steps of host-pathogen interactions. These outcomes will afford new approaches for genetically engineering useful biotechnology traits into poplar to enhance resistance to pathogens and expand its potential for use as a critical bioenergy feedstock.

Remobilize nutrients to increase biomass

Seasonal nitrogen cycling plays a key role in the overall nitrogen budget of poplar and has a significant impact on new growth and biomass yield. The lab is using protein, metabolic, and system engineering to enhance the synthesis and storage of nitrogen-rich metabolites and to rewire the signaling between nitrogen utilization and storage to improve Nitrogen Use Efficiency (NUE). The outcomes will increase biomass yields and enhance efficient downstream processing to advance the long-term sustainability of poplar as a bioenergy crop.

Improve plant response to abiotic stress

A barrier to the broad adoption of plant feedstocks for bioenergy is lignin – a phenolic-based polymer that provides rigidity and strength to plant tissues, but which must be removed from pulp to make cellulose for biofuel. Low lignin plants display enhanced ethanol yields, but are prone to metabolic stress since they cannot as readily cope with abiotic challenges, such as constant exposure to UV radiation. Ecophysiologic and metabolomic investigations of genetically engineered poplar will help to decipher the mechanisms whereby low-lignin plants respond to UV stress. The results will inform engineering approaches to boost acclimation and fitness of new biofuel feedstocks.

Enhance Soluble Protein Production

The lab also has a long-standing interest in improving the production of therapeutic proteins in bacterial and mammalian cell cultures. They are using modern genome-engineering approaches to rewire cell circuits to improve the production of therapeutic proteins. Their goal is to establish cell lines that enhance soluble protein production for a range of therapeutic protein targets.

Highly efficient C-to-T and A-to-G base editing in a Populus hybrid.
Structural Insights into the Inhibitory Mechanism of an Antibody against B7-H6, a Stress-Induced Cellular Ligand for the Natural Killer Cell Receptor NKp30.
Development of a Model Protein Interaction Pair as a Benchmarking Tool for the Quantitative Analysis of 2-Site Protein-Protein Interactions.
A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.
Structural basis for the binding specificity of human Recepteur d'Origine Nantais (RON) receptor tyrosine kinase to macrophage-stimulating protein.
Systems approaches to unraveling plant metabolism: identifying biosynthetic genes of secondary metabolic pathways.
Calcium antagonists: a ready prescription for treating infectious diseases?
ABRF-MIRG benchmark study: molecular interactions in a three-component system.
Some new speculative ideas about the "behavioral homeostasis theory" as to how the simple learned behaviors of habituation and sensitization improve organism survival throughout phylogeny.
Structural reorganization of the interleukin-7 signaling complex.
Gene identification in black cohosh (Actaea racemosa L.): expressed sequence tag profiling and genetic screening yields candidate genes for production of bioactive secondary metabolites.
Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate.
Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA.
NMR structure of HI0004, a putative essential gene product from Haemophilus influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog.
Structure of the phenazine biosynthesis enzyme PhzG.
Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79.
Local and global control mechanisms in allosteric threonine deaminase.
NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae--a putative essential gene product.
NMR assignment of HI1723 from Haemophilus influenzae--a sequence homologue from the iron sulfur cluster assembly (IscA) family.
Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.