photo of Che-Yen Wang

Che-Yen (Joe) Wang, Ph.D.
Assistant Scientist

Simon Hall 047D
812.855.4963
wangjoe@indiana.edu

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I have been trained on using cryo-TEM to solve macromolecule structures since 2003. My main areas of expertise are using single-particle reconstruction (SPR) approach to study virus assembly, symmetrical and asymmetrical macromolecular structures. I also have experience in applying electron tomography technique on both macromolecule and tissue section.

I obtained a bachelor’s degree in the Department of Biology at Catholic Fu-Jen University in Taiwan and turned to medical image processing for my master's degree in the Department of Anatomy and Cellular Biology at National Yang-Ming University (NYMU), Taiwan. For my master thesis, I developed a cross platform medical imaging processing software for virtual anatomy classroom using Java language. As I love both biology and computation, I continued to pursue a doctoral degree in a group of Biomedical Informatics under the Institute of Public Health at NYMU. At my second semester, I was introduced by Prof. Yen-Jen Sung to structural biology using cryo-TEM. With supports from my PhD advisor Prof. Der-Ming Liou and NYMU, I went to Prof. R Holland Cheng's lab at Karolinska Institutet in Sweden and later at the University of California at Davis to learn imaging processing and cryo-TEM operation. The central theme of my PhD study was to understand macromolecular assembly, structure, and function using cryo-TEM.

My initial effort was to elucidate the assembly mechanism of hepatitis E virus (HEV) virus-like particles (VLP's) at a three-dimensional level as HEV-VLP is one of the vaccine candidates in the current clinical trials. My achievements in this project include mapping the essential regions of the capsid protein for VLP formation ( J Virol 79:12999, 2005), characterizations of the immuno-dominant epitopes of the vaccine candidate (J Virol. 85:1117, 2011), stability studies of the VLP's, crystallization and preliminary high resolution structural analysis of the VLP's (Acta Crystallogr Sect F Struct Biol Cryst Commun 64:318, 2008), and determining the role of RNA incorporation in the formation of virion-sized VLP's (J Biol Chem. 285:33175, 2010).

image, transform and reconstruction of 2d crystal of Phi 29 motorsIn a second group of projects, my focus was extended to characterize the controlled assembly of bacteriophage phi29 DNA-packaging motors for nanotechnology applications. The project was in collaboration with the lab of Prof. Peixuan Guo and my role was to characterize structurally the macromolecules assembled from re-engineered phi29 connectors. I performed image analysis of a single layered 2-D array of phi29 motors. Hypothetically, such arrays can be engineered to serve as components in chips for numerous applications (ACS Nano 3:100, 2009). I also participated in structural analysis of self-assembled heptameric nanoparticles derived from the re-engineered phi29 motors (ACS Nano 3:2163, 2009; ACS Nano 4:7651, 2010).

asymmetric reconstruction of HBV showing the distribution of RNASince joining Dr. Adam Zlotnick’s lab in 2010, my research has focused on exploring capsid assembly driven by protein-protein and protein-nucleic acid interactions using hepatitis B virus (HBV) core protein as the primary model. I have worked closely with members of the Zlotnick lab and used different biophysical methods to characterize the structure and the functional role of the C-terminal domain (CTD) in HBV capsid assembly. We have found that the HBV capsid is a multi-function protein and the exposure of the CTD modulates its biological functions (PLoS Pathog 7:e1002388, 2011; PLoS Pathog 8:e1002919, 2012; J Biol Chem 290:28584, 2015). We have also developed an unique strategy to determine the asymmetric structure of the authentic HBV RNA-filled capsid during the reverse transcription process. This is the first view of the HBV reverse transcriptase and reverse transcription complex in its native environment (PNAS 111:11329, 2014). With Prof. Adam Zlotnick's full supports, in 2013 I was promoted as a Research Assistant Professor (equivalent to Assistant Scientist rank).

In the fall of 2015, I joined the electron microscopy center (EMC) at Indiana University as a staff scientist. My primary responsibility as a staff scientist is in a service role to major users of the microscope, providing fee-for-service work, and training of graduate students, post-doctoral research scientists, and faculty. A secondary responsibility is assisting Dr. David Morgan with upkeep of the JEOL JEM 3200FS.  I am encouraged to perform a mix of collaborative and independent research, to the extent dictated by the external grant support as PI, co-PI or collaborating investigator. Therefore, I may spend up to 25% of time working on my own research projects, ~50% of time will be spent performing fee for service work, the majority of which will be for IU-affiliated researchers. The remaining 25% of time will be devoted to training new users and miscellaneous tasks associated with EMC.