Hyeryun Choe

Hyeryun Choe, Ph.D.


Department: SR-IM-CHOE LAB
Business Phone: (561) 228-2440
Business Email: hchoe@ufl.edu

About Hyeryun Choe

Hyeryun Choe has done her graduate studies at Pennsylvania State University and received her Ph.D. degree from the Department of Biochemistry, Molelcular Biology, and Cell Biology in erythrocyte membrane lipid bilayer asymmetry in diseases such as sickle cell anemia. During her postdoctoral training at Beth Israel Hospital and Dana Farber Cancer Institute at Harvard Medical School, her research interests broadened to viruses and the mechanisms with which viruses enter cells and cause diseases. In the decade of 2000, as Assistant and Associate Professor at the Department of Pediatrics, Boston Children’s Hospital, Harvard Medical School, Dr. Choe discovered or co-discovered the HIV-1 coreceptors CCR3 and CCR5, the SARS-CoV receptor ACE2 when it emerged in the winter of 2002, and TFR1 as the receptor for all five South American hemorrhagic fever viruses. Of these, the identification of ACE2 as the receptor for SARS-CoV likely accelerated SARS-CoV-2 research because SARS-CoV-2 also uses ACE2 as its entry receptor. In the following decade after her relocation to the Scripps Research, Dr. Choe, as Associate Professor and Professor, studied the entry mechanisms of newly emerging viruses such as West Nile virus, Zika virus, and SARS-CoV-2. Her passion is to develop or contribute to developing effective vaccines or vaccine alternatives against dengue virus that infects hundreds of millions people and causes diseases in tens of millions a year.

Research Profile

Viruses enter cells through common mechanisms. Parallel studies of the entry processes of various viruses can therefore highlight differences among them, as well as their similarities. The Choe laboratory studies a wide range of viruses to better understand their entry pathways and the mechanisms of pathogenesis of viral diseases. In doing so, we identified a number of viral receptor and host factors critical for viral infection and pathogenesis. These include: the HIV-1 coreceptor CCR5, and its post-translational modification tyrosine sulfation critical HIV-1 infection; the SARS-CoV receptor angiotensin-converting enzyme 2 (ACE2) and the lysosomal enzyme cathepsin L as an essential target-cell factors for SARS-CoV infection; transferrin receptor 1 (TFR1) as the receptor for New World hemorrhagic fever arenaviruses, and the intimate association between virus’ ability to use human TFR1 and its tendency to cause hemorrhagic fever. We also study other entry factors such as the TIM family members of phosphatidylserine receptors. By binding the lipids on the virion membrane, they promote the infections of a wide range of enveloped viruses including filoviruses and flaviviruses such as West Nile, dengue and Zika viruses.

In addition to our focus on basic virology, we use our knowledge to discover entry inhibitors and to develop strategies to improve known inhibitors. We have previously identified potent antibodies that inhibited the infection of all five NW hemorrhagic fever arenaviruses. We also employ a novel strategy to improve the potency and breadth of protein inhibitors.

Recently, we extended our studies to adeno-associated virus (AAV), a commonly used gene therapy vector, with the goal of improving its transduction efficiency in specific target cells. We successfully developed AAV vectors that transduce skeletal muscle or CD4+ T cells with markedly improved efficiency and specificity.

Open Researcher and Contributor ID (ORCID)



Mechanisms of SARS-CoV-2 entry into cells
Nature Reviews Molecular Cell Biology. 23(1):3-20 [DOI] 10.1038/s41580-021-00418-x. [PMID] 34611326.
An Engineered Receptor-Binding Domain Improves the Immunogenicity of Multivalent SARS-CoV-2 Vaccines.
mBio. 12(3) [DOI] 10.1128/mBio.00930-21. [PMID] 33975938.
Clinical Antiviral Drug Arbidol Inhibits Infection by SARS-CoV-2 and Variants through Direct Binding to the Spike Protein.
ACS chemical biology. 16(12):2845-2851 [DOI] 10.1021/acschembio.1c00756. [PMID] 34792325.
Functional importance of the D614G mutation in the SARS-CoV-2 spike protein
Biochemical and Biophysical Research Communications. 538:108-115 [DOI] 10.1016/j.bbrc.2020.11.026. [PMID] 33220921.
How SARS-CoV-2 first adapted in humans.
Science (New York, N.Y.). 372(6541):466-467 [DOI] 10.1126/science.abi4711. [PMID] 33926942.
Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2.
PLoS pathogens. 17(1) [DOI] 10.1371/journal.ppat.1009212. [PMID] 33465165.
Mutations derived from horseshoe bat ACE2 orthologs enhance ACE2-Fc neutralization of SARS-CoV-2.
PLoS pathogens. 17(4) [DOI] 10.1371/journal.ppat.1009501. [PMID] 33836016.
A Single Immunization with Nucleoside-Modified mRNA Vaccines Elicits Strong Cellular and Humoral Immune Responses against SARS-CoV-2 in Mice.
Immunity. 53(4):724-732.e7 [DOI] 10.1016/j.immuni.2020.07.019. [PMID] 32783919.
AAV vectors engineered to target insulin receptor greatly enhance intramuscular gene delivery.
Molecular therapy. Methods & clinical development. 19:496-506 [DOI] 10.1016/j.omtm.2020.11.004. [PMID] 33313337.
An engineered receptor-binding domain improves the immunogenicity of multivalent SARS-CoV-2 vaccines.
bioRxiv : the preprint server for biology. [DOI] 10.1101/2020.11.18.388934. [PMID] 33236008.
Mutations from bat ACE2 orthologs markedly enhance ACE2-Fc neutralization of SARS-CoV-2.
bioRxiv : the preprint server for biology. [DOI] 10.1101/2020.06.29.178459. [PMID] 32637954.
Phosphatidylethanolamine and Phosphatidylserine Synergize To Enhance GAS6/AXL-Mediated Virus Infection and Efferocytosis.
Journal of virology. 95(2) [DOI] 10.1128/JVI.02079-20. [PMID] 33115868.
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Nature Communications. 11(1) [DOI] 10.1038/s41467-020-19808-4. [PMID] 33243994.
The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity.
bioRxiv : the preprint server for biology. [DOI] 10.1101/2020.06.12.148726. [PMID] 32587973.
Transferrin receptor 1 is a cellular receptor for human heme-albumin
Communications Biology. 3(1) [DOI] 10.1038/s42003-020-01294-5. [PMID] 33110194.
Reply to Marques and Drexler, “Complex Scenario of Homotypic and Heterotypic Zika Virus Immune Enhancement”.
mBio. 10(5) [DOI] 10.1128/mBio.02073-19. [PMID] 31481388.
Zika Virus-Immune Plasmas from Symptomatic and Asymptomatic Individuals Enhance Zika Pathogenesis in Adult and Pregnant Mice.
mBio. 10(4) [DOI] 10.1128/mBio.00758-19. [PMID] 31266863.
Diverse pathways of escape from all well-characterized VRC01-class broadly neutralizing HIV-1 antibodies
PLOS Pathogens. 14(8) [DOI] 10.1371/journal.ppat.1007238. [PMID] 30125330.
AXL-dependent infection of human fetal endothelial cells distinguishes Zika virus from other pathogenic flaviviruses.
Proceedings of the National Academy of Sciences of the United States of America. 114(8):2024-2029 [DOI] 10.1073/pnas.1620558114. [PMID] 28167751.
Ebselen, a Small-Molecule Capsid Inhibitor of HIV-1 Replication.
Antimicrobial agents and chemotherapy. 60(4):2195-208 [DOI] 10.1128/AAC.02574-15. [PMID] 26810656.
Zika virus infection during the period of maximal brain growth causes microcephaly and corticospinal neuron apoptosis in wild type mice.
Scientific reports. 6 [DOI] 10.1038/srep34793. [PMID] 27713505.
Virion-associated phosphatidylethanolamine promotes TIM1-mediated infection by Ebola, dengue, and West Nile viruses.
Proceedings of the National Academy of Sciences of the United States of America. 112(47):14682-7 [DOI] 10.1073/pnas.1508095112. [PMID] 26575624.
Human and host species transferrin receptor 1 use by North American arenaviruses.
Journal of virology. 88(16):9418-28 [DOI] 10.1128/JVI.01112-14. [PMID] 24920811.
Dual host-virus arms races shape an essential housekeeping protein.
PLoS biology. 11(5) [DOI] 10.1371/journal.pbio.1001571. [PMID] 23723737.
TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.
PLoS pathogens. 9(3) [DOI] 10.1371/journal.ppat.1003232. [PMID] 23555248.
An antibody recognizing the apical domain of human transferrin receptor 1 efficiently inhibits the entry of all new world hemorrhagic Fever arenaviruses.
Journal of virology. 86(7):4024-8 [DOI] 10.1128/JVI.06397-11. [PMID] 22278244.
Enhanced recognition and neutralization of HIV-1 by antibody-derived CCR5-mimetic peptide variants.
Journal of virology. 86(22):12417-21 [DOI] 10.1128/JVI.00967-12. [PMID] 22933279.
A tyrosine-sulfated CCR5-mimetic peptide promotes conformational transitions in the HIV-1 envelope glycoprotein.
Journal of virology. 85(15):7563-71 [DOI] 10.1128/JVI.00630-11. [PMID] 21613393.
Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus.
PLoS pathogens. 7(1) [DOI] 10.1371/journal.ppat.1001258. [PMID] 21253575.
Transferrin receptor 1 in the zoonosis and pathogenesis of New World hemorrhagic fever arenaviruses.
Current opinion in microbiology. 14(4):476-82 [DOI] 10.1016/j.mib.2011.07.014. [PMID] 21807555.
Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses.
Nature structural & molecular biology. 17(4):438-44 [DOI] 10.1038/nsmb.1772. [PMID] 20208545.
A New World primate deficient in tetherin-mediated restriction of human immunodeficiency virus type 1.
Journal of virology. 83(17):8771-80 [DOI] 10.1128/JVI.00112-09. [PMID] 19553332.
Chapter 7. Tyrosine sulfation of HIV-1 coreceptors and other chemokine receptors.
Methods in enzymology. 461:147-70 [DOI] 10.1016/S0076-6879(09)05407-X. [PMID] 19480918.
Host-species transferrin receptor 1 orthologs are cellular receptors for nonpathogenic new world clade B arenaviruses.
PLoS pathogens. 5(4) [DOI] 10.1371/journal.ppat.1000358. [PMID] 19343214.
Mutagenesis and evolution of sulfated antibodies using an expanded genetic code.
Biochemistry. 48(37):8891-8 [DOI] 10.1021/bi9011429. [PMID] 19715291.
Influenza A virus neuraminidase limits viral superinfection.
Journal of virology. 82(10):4834-43 [DOI] 10.1128/JVI.00079-08. [PMID] 18321971.
Protein evolution with an expanded genetic code.
Proceedings of the National Academy of Sciences of the United States of America. 105(46):17688-93 [DOI] 10.1073/pnas.0809543105. [PMID] 19004806.
Receptor determinants of zoonotic transmission of New World hemorrhagic fever arenaviruses.
Proceedings of the National Academy of Sciences of the United States of America. 105(7):2664-9 [DOI] 10.1073/pnas.0709254105. [PMID] 18268337.
Severe acute respiratory syndrome coronavirus entry as a target of antiviral therapies.
Antiviral therapy. 12(4 Pt B):639-50 [PMID] 17944271.
The S proteins of human coronavirus NL63 and severe acute respiratory syndrome coronavirus bind overlapping regions of ACE2.
Virology. 367(2):367-74 [PMID] 17631932.
Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses.
Nature. 446(7131):92-6 [PMID] 17287727.
A tyrosine-sulfated peptide derived from the heavy-chain CDR3 region of an HIV-1-neutralizing antibody binds gp120 and inhibits HIV-1 infection.
The Journal of biological chemistry. 281(39):28529-35 [PMID] 16849323.
Animal origins of the severe acute respiratory syndrome coronavirus: insight from ACE2-S-protein interactions.
Journal of virology. 80(9):4211-9 [PMID] 16611880.
Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor.
The Journal of biological chemistry. 281(23):15951-8 [PMID] 16595665.
Insights from the association of SARS-CoV S-protein with its receptor, ACE2.
Advances in experimental medicine and biology. 581:209-18 [PMID] 17037532.
SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells.
The Journal of biological chemistry. 281(6):3198-203 [PMID] 16339146.
SARS-CoV, but not HCoV-NL63, utilizes cathepsins to infect cells: viral entry.
Advances in experimental medicine and biology. 581:335-8 [PMID] 17037556.
Tyrosine sulfate trapped by amber.
Nature biotechnology. 24(11):1361-2 [PMID] 17093482.
Mapping binding residues in the Plasmodium vivax domain that binds Duffy antigen during red cell invasion.
Molecular microbiology. 55(5):1423-34 [PMID] 15720551.
Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.
The EMBO journal. 24(8):1634-43 [PMID] 15791205.
Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC).
Molecular microbiology. 55(5):1413-22 [PMID] 15720550.
A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2.
The Journal of biological chemistry. 279(5):3197-201 [PMID] 14670965.
Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2.
Journal of virology. 78(20):11429-33 [PMID] 15452268.
N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
Virology. 324(1):140-50 [PMID] 15183061.
Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association.
Proceedings of the National Academy of Sciences of the United States of America. 101(8):2536-41 [PMID] 14983044.
Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2.
Journal of virology. 78(19):10628-35 [PMID] 15367630.
Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120.
Proceedings of the National Academy of Sciences of the United States of America. 101(9):2706-11 [PMID] 14981267.
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.
Nature. 426(6965):450-4 [PMID] 14647384.
Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120.
Cell. 114(2):161-70 [PMID] 12887918.
The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry.
The Journal of biological chemistry. 277(33):29484-9 [PMID] 12034737.
Tyrosine-sulfated peptides functionally reconstitute a CCR5 variant lacking a critical amino-terminal region.
The Journal of biological chemistry. 277(43):40397-402 [PMID] 12183462.
The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement
. [DOI] 10.1101/2020.04.10.036418.


Ph.D. in Microbiology, Biochemistry and Molecular Biology
1984 · Pennsylvania State University
Masters of Science in Microbiology
1980 · Seoul National University
Bachelor's of Science
1977 · Seoul National University

Contact Details

(561) 228-2440
Business Mailing:
Location B207B