Melanie Ohi Lab

We use single particle cryo-electron microscopy — in combination with biophysical, biochemical, and genetic approaches — to structurally and functionally characterize molecular machines that affect human health.

Our Research

The Ohi lab's research interest focuses on dissecting the structural organization of large macromolecular machines. Our goal is to use structure as a springboard to understand function within the context of cells.

Our laboratory uses single particle cryo-electron microscopy (cryo-EM) in combination with biophysical, biochemical, and genetic approaches to structurally and functionally characterize biologically important but structurally challenging molecular machines. We have exciting projects studying the machinery involved in gene regulation, bacterial pathogenesis, and membrane remodeling proteins.

Image

Melanie Ohi, Ph.D.

Rowena G. Matthews Collegiate Professor in the Life Sciences
Research Professor and Cryo-EM Facility Faculty Director, U-M Life Sciences Institute
Professor of Cell and Developmental Biology, U-M Medical School
LSI Grads and LSI Postdocs Faculty Advisor, U-M Life Sciences Institute

Publication Highlights

Molecular architecture of the human caveolin-1 complex

Porta JC, Han B, Gulsevin A, Chung JM, Peskova Y, Connolly S, Mchaourab HS, Meiler J, Karakas E, Kenworthy AK, Ohi MD, Sci Adv (2022)

Functional properties of oligomeric and monomeric forms of Helicobacter pylori VacA toxins

Caso GC, McClain MS, Erwin AL, Truelock MD, Campbell AM, Leasure CS, Nagel M, Schey KL, Lacy DB, Ohi MD, Cover TL, Infect Immun (2021)

Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS

Sheedlo MJ, Durie CL, Chung JM, Chang L, Roberts J, Swanson M, Lacy DB, Ohi MD, Elife (2021)

Ion mobility-mass spectrometry reveals the role of peripheral myelin protein dimers in peripheral neuropathy

Fantin SM, Parson KF, Yadav P, Juliano B, Li GC, Sanders CR, Ohi MD, Ruotolo BT, Proc Natl Acad Sci U S A (2021) 

N-terminal transmembrane-helix epitope tag for x-ray crystallography and electron microscopy of small membrane protein

McIlwain BC, Erwin AL, Davis AR, Ben Koff B, Chang L, Bylund T, Chuang GY, Kwong PD, Ohi MD, Lai YT, Stockbridge RB, J Mol Biol (2021)

Human antibody recognition of antigenic site IV on Pneumovirus fusion proteins

Mousa JJ, Binshtein E, Human S, Fong RH, Alvarado G, Doranz BJ, Moore ML, Ohi MD, Crowe JE Jr, PLoS Pathog (2018)

Peripheral myelin protein 22 alters membrane architecture

Mittendorf KF#, Marinko JT#, Hampton CM, Ke Z, Hadziselimovic A, Schlebach JP, Law CL, Li J, Wright ER, Sanders CR*, Ohi MD*, Sci Adv (2017)

#co-first authors, *Co-corresponding authors

Structural organization of membrane-inserted hexamers formed by Helicobacter pylori VacA toxin

Pyburn TM, Foegeding NJ, González-Rivera C, McDonald NA, Gould KL, Cover TL, Ohi MD, Mol Microbiol (2016)

Molecular and Structural Analysis of the Helicobacter pylori cag Type IV Secretion System Core Complex

Frick-Cheng AE, Pyburn TM, Voss BJ, McDonald WH, Ohi MD, Cover TL, MBio (2016)

Room 6183
Life Sciences Institute
Mary Sue Coleman Hall
210 Washtenaw Avenue
Ann Arbor, MI 48109-2216