Jeanmarie Verchot,
Professor
Dr Jeanmarie Verchot completed undergraduate degree at Rutgers University in 1987. She received PhD from Texas A&M University in 1995 under Dr James C Carrington and Post doctoral research on the topic of virus movement carried out at the Sainsbury Laboratory under the guidance of Dr David C Baulcombe. Thereafter, She joined Oklahoma State University in 1998 and current rank of Professor. The Current research in her laboratory can be categorized into two topics: 1) Plant Virology of Canna lily and germplasm screening program; 2) Cell death and ER stress factors relating to virus infection. T
The Verchot laboratory has written more than 60 manuscripts in highly regarded journals. The Verchot laboratory, among others, have for more than a decade reported on viral induced modifications of membranous networks in eukaryotic cells. Viral protein interactions with the endoplasmic reticulum (ER) are often vital contributions to persistent infection. For many positive strand RNA viruses, the ER provides architectural support for genome synthesis and translation. The Verchot laboratory has used potato virus X as a model for studying virus interactions with the ER and has reported on the role for small membrane binding proteins in promoting virus egress from the cell. ER stress resulting from disease or extreme abiotic conditions can chronically impact cell survival and is linked to the transcriptional activation of the unfolded protein response (UPR) and components of the ER associated degradation (ERAD) machineries. Virus infection, heat/cold, and tunicamycin are seemingly dissimilar triggers of ER stress that similarly coordinate the action of a common set of molecular chaperones to cope with the demand for increasing protein folding capacity and to mitigate the toxic accumulation of malformed proteins. RNA viruses create a huge biosynthetic burden on the ER and transiently enhance UPR to manipulate the production of protein chaperones and foldases to meet their needs. Abiotic stressors such as heat/cold/tunicamycin cause accumulation of malformed proteins in the ER and triggers the same machinery to ensure efficient maturation and secretion of proteins. The Verchot/ laboratory has reported on the prototypical ER stress responsive proteins bZIP60, BIP, and BI1 to both virus infection and abiotic stressors. Current research examines the impact of overexpressing or knocking-out/down critical ER stress factors in virus susceptibility and cold tolerance with the goal of uncovering critical new information that can be exploited in a next generation of crops with engineered abiotic stress tolerance and virus resistance. Until now the research has provided new insights into how viruses activate the UPR. With recent funding in the next years, this work will provide a global view of the similar and different outcomes that result when unrelated triggers converge to activate the UPR to overcome a condition that is singly termed ER stress.
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