Chi-Min Ho, PhD
- Assistant Professor of Microbiology and Immunology
Overview
Dr. Chi-Min Ho earned her BA in Molecular and Cell Biology at the University of California, Berkeley in 2004, after which she worked on membrane protein structure in the lab of Robert Stroud at the University of California, San Francisco for six years and small molecule drug discovery in the Infectious Diseases Division at the Novartis Institutes for Biomedical Research for three years before returning to academia to pursue a doctoral degree in 2014. She completed her PhD in Biochemistry, Biophysics and Structural Biology at the University of California, Los Angeles under the mentorship of Dr. Hong Zhou in 2019 and joined the Faculty at Columbia University in January 2020. Dr. Ho is a 2024 Pew Scholar and a recipient of the NIH Director’s Early Independence Award.
As a graduate student, Dr. Ho pioneered the use of single-particle cryoEM to elucidate the structures and mechanisms of endogenous malarial protein complexes purified directly from malaria parasites. She elucidated the structure and mechanism of an essential malarial membrane protein complex known as the Plasmodium Translocon of Exported Proteins (PTEX), which she purified directly from malaria parasites via an epitope tag inserted into the endogenous locus of a PTEX subunit using CRISPR-Cas9. Following this work, she developed an endogenous structural proteomics approach for identification and structure determination of novel protein complexes enriched untagged from challenging endogenous sources, using mass spectrometry and near-atomic resolution cryoEM density maps reconstructed ab initio, and cryoID, a program she designed to semi-autonomously identify proteins in cryoEM maps of unknown protein complexes.
Academic Appointments
- Assistant Professor of Microbiology and Immunology
Gender
- Female
Credentials & Experience
Education & Training
- BA, 2004 Molecular and Cell Biology, University of California, Berkeley
- PhD, 2019 Biochemistry, Biophysics and Structural Biology, University of California, Los Angeles
Honors & Awards
- 2020: NIH Director’s Early Independence Award
- 2024: Pew Biomedical Scholar
Research
Research in the Dr. Ho’s Lab is focused on understanding the molecular basis of host-pathogen interactions of malarial parasites, using a combination of molecular genetics, biochemistry, and cutting-edge imaging tools such as cryo-electron microscopy and cryo-electron tomography.
The complexity and breadth of its host-cell remodeling machinery make P. falciparum a rich and exciting system for the study of host-pathogen interfaces. However, many of the molecular mechanisms underlying this parasite’s ability to hijack human red blood cells remain enigmatic, as much of the P. falciparum proteome has proven recalcitrant to structural and biochemical characterization using traditional approaches. The Ho Lab (link to www.cmholab.org) uses single-particle cryo electron microscopy (cryoEM) to determine near-atomic resolution structures of previously intractable protein complexes enriched directly from endogenous P. falciparum parasites, and in situ cryo electron tomography (cryoET) of cryoFIB-milled parasites to directly visualize proteins at the host-pathogen interface in parasite-infected red blood cells at sub-nanometer resolutions.
Research in the Dr. Ho’s Lab is focused on understanding the molecular basis of host-pathogen interactions of malarial parasites, using a combination of molecular genetics, biochemistry, and cutting-edge imaging tools such as cryo-electron microscopy and cryo-electron tomography.
The complexity and breadth of its host-cell remodeling machinery make P. falciparum a rich and exciting system for the study of host-pathogen interfaces. However, many of the molecular mechanisms underlying this parasite’s ability to hijack human red blood cells remain enigmatic, as much of the P. falciparum proteome has proven recalcitrant to structural and biochemical characterization using traditional approaches. The Ho Lab (link to www.cmholab.org(link is external and opens in a new window)) uses single-particle cryo electron microscopy (cryoEM) to determine near-atomic resolution structures of previously intractable protein complexes enriched directly from endogenous P. falciparum parasites, and in situ cryo electron tomography (cryoET) of cryoFIB-milled parasites to directly visualize proteins at the host-pathogen interface in parasite-infected red blood cells at sub-nanometer resolutions.
Selected Publications
- Anton L*, Cheng W*, Haile M*, Cobb DW, Zhu X, Han L, Li E, Nair A, Ke H, Zhang G, Doud EH, Ho CM**. Multiscale effects of perturbed translation dynamics inform antimalarial design. bioRxiv. (2023). doi.org/10.1101/2023.09.03.556115
- Ho CM*, Jih J, Lai M, Li X, Goldberg DE, Beck JR, Zhou ZH*. Native structure of the RhopH complex, a key determinant of malaria parasite nutrient acquisition. Proceedings of the National Academy of Sciences 118 (35), e2100514118 (2021).
- Ho CM*, Li X*, Lai M, Terwilliger TC, Beck JR, Wohlschegel JA, Goldberg DE, Fitzpatrick AWP, Zhou ZH. Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu. Nature Methods 17, 79-85 (2020). doi:10.1038/s41592-019-0637-y.
- Ho CM, Beck JR, Lai M, Cui Y, Goldberg DE, Egea PF, Zhou ZH. Malaria parasite translocon structure and mechanism of effector export. Nature 561, 70-75 (2018).
For a complete list of publications, please visit PubMed.gov(link is external and opens in a new window)