Mei Hong (chemist)

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Mei Hong

Mei Hong (born 1970) is a Chinese-American biophysical chemist and professor of chemistry at the Massachusetts Institute of Technology. [1] She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, [2] the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.

Contents

Education and career

Hong grew up in China and completed her B.A. degree in chemistry from Mount Holyoke College ( summa cum laude ) in 1992 and a Ph.D. degree from the University of California, Berkeley in 1996. There she worked in the laboratory of Alexander Pines to investigate phospholipid structure and dynamics using variable-angle-spinning NMR. After a one-year postdoctoral stint in the laboratory of Robert G. Griffin at the Massachusetts Institute of Technology, she went to University of Massachusetts Amherst and developed biosynthetic isotopic labeling approaches to advance protein structure determination by ssNMR. She started an assistant professorship at Iowa State University in 1999, became an associate professor in 2002 and full professor in 2004, and held the first John D. Corbett Professorship from 2007 to 2010. In 2014, she returned to the Massachusetts Institute of Technology as a professor of chemistry. [1]

Research

Hong's research focuses on elucidating the structure, dynamics and mechanism of membrane proteins using ssNMR. She is particularly known for her in-depth study of the Matrix-2 (M2) proteins of influenza A viruses, which are responsible for all flu pandemics in history. M2 is an acid-activated proton channel and a membrane scission protein of the influenza virus. [3] Hong's ssNMR studies have provided insights into the proton-conduction mechanism of this channel, by quantifying the proton transfer rates and equilibria between water and the proton-selective histidine residue. [4] [5] She showed that the antiviral drug amantadine inhibits proton conduction by direct occlusion of the channel pore. [6] She determined the cholesterol-binding structure of the M2 protein, which sheds light on how cholesterol mediates M2's membrane scission function. [7] In 2020 she determined both the influenza B M2 protein structure [8] and the SARS-CoV-2 envelope protein structure, [9] the latter in rapid response to COVID-19. The 1.5 Å BM2 structures in the closed and open states revealed different activation mechanisms of BM2 compared to influenza AM2. The 2.1 Å SARS-CoV-2 envelope protein structure forms the basis for antiviral drug design.

Other membrane proteins that Hong's group has studied include β-hairpin antimicrobial peptides, [10] channel-forming colicins, [11] and viral fusion proteins. [12] She determined the structure of the membrane toroidal pores formed by the antimicrobial peptide protegrin-1, [10] which explained the membrane-disruptive mechanism of this peptide. She showed that the transmembrane domain of viral fusion proteins can be conformationally plastic, and the β-sheet conformation can correlate with the generation of membrane curvature and membrane dehydration, which are necessary for virus-cell fusion. [12]

Hong has also investigated the structure and dynamics of amyloid proteins, including full-length tau [13] and Aβ peptides involved in neurodegenerative diseases [14] as well as amyloid fibrils formed by designed peptides. [15] She showed that the peptide hormone glucagon fibrillizes into an antiparallel hydrogen-bonded β-sheet with two coexisting molecular conformations. [16] These studies shed light on the origin of structural polymorphism, water interaction, [17] and metal ion binding.

Hong pioneered the study of plant cell walls using multidimensional ssNMR. [18] These studies revealed the molecular interactions of the polysaccharides in plant cell walls, and helped to revise the conventional model of the primary cell wall structure by proposing a single-network model where cellulose, hemicellulose and pectins all interact with each other. [19] She determined the binding target of the protein expansin to be hemicellulose-enriched regions of cellulose microfibrils, [20] thus giving insight into the mechanism of wall loosening by expansin.  

To address these questions, Hong has developed isotopic labeling strategies, [21] multidimensional NMR correlation experiments, [22] polarization transfer techniques, [23] [24] and computational methods for resonance assignment of NMR spectra. [25]

Selected awards and honors

Related Research Articles

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References

  1. 1 2 "Professor Mei Hong – Hong Lab MIT" . Retrieved 2019-05-21.
  2. ↑ Ernst, Richard R. (April 2005). "The Günther Laukien Prize". Journal of Magnetic Resonance. 173 (2): 188–191. Bibcode:2005JMagR.173..188E. doi:10.1016/j.jmr.2005.02.006. ISSN   1090-7807. PMID   15780911.
  3. ↑ Hong, Mei; DeGrado, William F. (2012-10-09). "Structural basis for proton conduction and inhibition by the influenza M2 protein". Protein Science. 21 (11): 1620–1633. doi:10.1002/pro.2158. PMC   3527700 . PMID   23001990.
  4. ↑ Hu, F.; Luo, W.; Hong, M. (2010-10-21). "Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR". Science. 330 (6003): 505–508. Bibcode:2010Sci...330..505H. doi:10.1126/science.1191714. ISSN   0036-8075. PMC   4102303 . PMID   20966251.
  5. ↑ Hu, Fanghao; Schmidt-Rohr, Klaus; Hong, Mei (2011-10-21). "NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel". Journal of the American Chemical Society. 134 (8): 3703–3713. doi:10.1021/ja2081185. ISSN   0002-7863. PMC   3288706 . PMID   21974716.
  6. ↑ Cady, Sarah D.; Schmidt-Rohr, Klaus; Wang, Jun; Soto, Cinque S.; DeGrado, William F.; Hong, Mei (2010). "Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers". Nature. 463 (7281): 689–692. Bibcode:2010Natur.463..689C. doi:10.1038/nature08722. ISSN   0028-0836. PMC   2818718 . PMID   20130653.
  7. ↑ Elkins, Matthew R.; Williams, Jonathan K.; Gelenter, Martin D.; Dai, Peng; Kwon, Byungsu; Sergeyev, Ivan V.; Pentelute, Bradley L.; Hong, Mei (2017-11-20). "Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR". Proceedings of the National Academy of Sciences. 114 (49): 12946–12951. Bibcode:2017PNAS..11412946E. doi: 10.1073/pnas.1715127114 . ISSN   0027-8424. PMC   5724280 . PMID   29158386.
  8. ↑ Mandala, Venkata S.; Loftis, Alexander R.; Shcherbakov, Alexander A.; Pentelute, Bradley L.; Hong, Mei (2020-02-03). "Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism". Nature Structural & Molecular Biology. 27 (2): 160–167. doi:10.1038/s41594-019-0371-2. ISSN   1545-9985. PMC   7641042 . PMID   32015551. S2CID   211017938.
  9. ↑ Mandala, Venkata S.; McKay, Matthew J.; Shcherbakov, Alexander A.; Dregni, Aurelio J.; Kolocouris, Antonios; Hong, Mei (December 2020). "Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers". Nature Structural & Molecular Biology. 27 (12): 1202–1208. doi: 10.1038/s41594-020-00536-8 . ISSN   1545-9985. PMC   7718435 . PMID   33177698.
  10. 1 2 Mani, R.; Cady, S. D.; Tang, M.; Waring, A. J.; Lehrer, R. I.; Hong, M. (2006-10-23). "Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR". Proceedings of the National Academy of Sciences. 103 (44): 16242–16247. Bibcode:2006PNAS..10316242M. doi: 10.1073/pnas.0605079103 . ISSN   0027-8424. PMC   1637567 . PMID   17060626.
  11. ↑ Luo, Wenbin; Yao, Xiaolan; Hong, Mei (2005). "Large Structure Rearrangement of Colicin Ia Channel Domain after Membrane Binding from 2D13C Spin Diffusion NMR". Journal of the American Chemical Society. 127 (17): 6402–6408. doi:10.1021/ja0433121. ISSN   0002-7863. PMID   15853348.
  12. 1 2 Yao, Hongwei; Lee, Michelle W.; Waring, Alan J.; Wong, Gerard C. L.; Hong, Mei (2015-08-17). "Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus–cell fusion". Proceedings of the National Academy of Sciences. 112 (35): 10926–10931. Bibcode:2015PNAS..11210926Y. doi: 10.1073/pnas.1501430112 . ISSN   0027-8424. PMC   4568205 . PMID   26283363.
  13. ↑ Dregni, Aurelio J.; Mandala, Venkata S.; Wu, Haifan; Elkins, Matthew R.; Wang, Harrison K.; Hung, Ivan; DeGrado, William F.; Hong, Mei (2019-08-13). "In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments". Proceedings of the National Academy of Sciences. 116 (33): 16357–16366. Bibcode:2019PNAS..11616357D. doi: 10.1073/pnas.1906839116 . ISSN   0027-8424. PMC   6697781 . PMID   31358628.
  14. ↑ Elkins, Matthew R.; Wang, Tuo; Nick, Mimi; Jo, Hyunil; Lemmin, Thomas; Prusiner, Stanley B.; DeGrado, William F.; Stöhr, Jan; Hong, Mei (2016-07-28). "Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study". Journal of the American Chemical Society. 138 (31): 9840–9852. doi:10.1021/jacs.6b03715. hdl:1721.1/113318. ISSN   0002-7863. PMC   5149419 . PMID   27414264.
  15. ↑ Lee, M.; Wang, T.; Makhlynets, O.V.; Wu, Y.; Polizzi, N.; Wu, H.; Gosavi, P.M.; Korendovych, I.V.; DeGrado, W.F. (2017-05-31). "Zinc-Binding Structure of a Catalytic Amyloid from Solid-State NMR Spectroscopy". doi:10.2210/pdb5ugk/pdb.{{cite journal}}: Cite journal requires |journal= (help)
  16. ↑ Gelenter, Martin D.; Smith, Katelyn J.; Liao, Shu-Yu; Mandala, Venkata S.; Dregni, Aurelio J.; Lamm, Matthew S.; Tian, Yu; Pochan, Darrin J.; Tucker, Thomas J.; Su, Yongchao; Hong, Mei (2019-06-24). "The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations". Nature Structural & Molecular Biology. 26 (7): 592–598. doi:10.1038/s41594-019-0238-6. hdl: 1721.1/125383 . ISSN   1545-9985. PMC   6609468 . PMID   31235909.
  17. ↑ Wang, Tuo; Jo, Hyunil; DeGrado, William F.; Hong, Mei (2017-04-21). "Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR". Journal of the American Chemical Society. 139 (17): 6242–6252. doi:10.1021/jacs.7b02089. ISSN   0002-7863. PMC   5808936 . PMID   28406028.
  18. ↑ Wang, Tuo; Hong, Mei (2015-09-09). "Solid-state NMR investigations of cellulose structure and interactions with matrix polysaccharides in plant primary cell walls". Journal of Experimental Botany. 67 (2): 503–514. doi:10.1093/jxb/erv416. ISSN   0022-0957. PMC   6280985 . PMID   26355148.
  19. ↑ Pérez García, Marilú; Zhang, Yuan; Hayes, Jennifer; Salazar, Andre; Zabotina, Olga A.; Hong, Mei (2011-02-15). "Structure and Interactions of Plant Cell-Wall Polysaccharides by Two- and Three-Dimensional Magic-Angle-Spinning Solid-State NMR". Biochemistry. 50 (6): 989–1000. doi:10.1021/bi101795q. ISSN   0006-2960. PMID   21204530. S2CID   42980200.
  20. ↑ Wang, T.; Park, Y. B.; Caporini, M. A.; Rosay, M.; Zhong, L.; Cosgrove, D. J.; Hong, M. (2013-09-24). "Sensitivity-enhanced solid-state NMR detection of expansin's target in plant cell walls". Proceedings of the National Academy of Sciences. 110 (41): 16444–16449. Bibcode:2013PNAS..11016444W. doi: 10.1073/pnas.1316290110 . ISSN   0027-8424. PMC   3799313 . PMID   24065828.
  21. ↑ Hong, M.; Jakes, K. (1999-05-01). "Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations". Journal of Biomolecular NMR. 14 (1): 71–74. doi:10.1023/A:1008334930603. ISSN   1573-5001. PMID   10382307. S2CID   41194972.
  22. ↑ Hong, Mei (1999-09-01). "Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR". Journal of Biomolecular NMR. 15 (1): 1–14. doi:10.1023/A:1008334204412. ISSN   1573-5001. PMID   10549131. S2CID   1474913.
  23. ↑ Hong, Mei; Schmidt-Rohr, Klaus (2013-02-07). "Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules". Accounts of Chemical Research. 46 (9): 2154–2163. doi:10.1021/ar300294x. ISSN   0001-4842. PMC   3714308 . PMID   23387532.
  24. ↑ Roos, Matthias; Mandala, Venkata S.; Hong, Mei (2018-09-13). "Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-Driven 19F–19F Dipolar Recoupling NMR". The Journal of Physical Chemistry B. 122 (40): 9302–9313. doi:10.1021/acs.jpcb.8b06878. ISSN   1520-6106. PMC   6314681 . PMID   30211552.
  25. ↑ Fritzsching, K. J.; Yang, Y.; Schmidt-Rohr, K.; Hong, Mei (2013-04-28). "Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information". Journal of Biomolecular NMR. 56 (2): 155–167. doi:10.1007/s10858-013-9732-z. ISSN   0925-2738. PMC   4048757 . PMID   23625364.
  26. ↑ "The ISMAR Organization | ISMAR". www.weizmann.ac.il. Retrieved 2019-05-21.
  27. ↑ "Monday at ENC: Laukien Prize Winners 2014". The Resonance. 2014-03-25. Retrieved 2019-05-21.
  28. ↑ "ICMRBS Founders Medal". www.icmrbs.org. Retrieved 2019-05-21.
  29. ↑ "Elected Fellows". American Association for the Advancement of Science. Retrieved 2019-05-21.
  30. ↑ "ACS Award in Pure Chemistry". American Chemical Society. Retrieved 2019-05-21.
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