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Lindsay Carpp

Lindsay Carpp works at Seattle BioMed and is also a visiting scientist at the Institute For Systems Biology in Seattle, Washington.

Lindsay completed her undergraduate education at Iowa State University, where she obtained Bachelor's Degrees in both biochemistry and philosophy. She then went on to complete her graduate work in biochemistry at the University of Glasgow in Dr. Nia Bryant's lab, where she studied how the Sec1/Munc18 family of proteins regulate SNARE-mediated membrane trafficking. This work was supported by a four-year studentship from the Wellcome Trust ("Molecular Functions in Disease").  After this time, she went to work in the laboratory of Dr. Kate Bowers, at University College London, where she studied the requirements for vacuole-vacuole fusion.

Lindsay next decided to apply her experience in biochemistry and protein trafficking towards the field of infectious disease research, and went to Rio de Janeiro, Brazil to study host proteins that contribute to the release of yellow fever virus. This work was done at the Instituto Oswaldo Cruz/FIOCRUZ in Dr. Myrna Bonaldo's laboratory, the Laboratório de Biologia Molecular de Flavivírus. Lindsay obtained a postdoctoral fellowship from Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) which supported this work.

Following her time in Brazil, Lindsay wanted to keep working with flaviviruses and in particular, to continue to try to understand their interactions with host cells on the molecular level. Lindsay joined the Aitchison lab in 2010 and started a project aimed at identifying host interactors of dengue virus nonstructural proteins. Dengue virus is a pathogen of global importance, against which no specific vaccines or antivirals exist, and understanding virus-host interactions will make an important contribution to our understanding of dengue infection. Lindsay is obtaining protein complexes from infected cells and identifying host proteins bound to dengue proteins through an immunoprecipitation/mass spectrometry approach. This work is supported by the National Center for Dynamic Interactome Research.

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