Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity

Interferon-induced transmembrane proteins (IFITMs) are -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. -palmitoylated IFITM3 in particular engages incoming virus particles, prevents their cytoplasmic entry, and accelerates their lysosomal clearance by host cells. How...

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Published in:ACS chemical biology Vol. 16; no. 5; pp. 844 - 856
Main Authors: Garst, Emma H, Lee, Hwayoung, Das, Tandrila, Bhattacharya, Shibani, Percher, Avital, Wiewiora, Rafal, Witte, Isaac P, Li, Yumeng, Peng, Tao, Im, Wonpil, Hang, Howard C
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Language:English
Published: United States 21-05-2021
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Abstract Interferon-induced transmembrane proteins (IFITMs) are -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. -palmitoylated IFITM3 in particular engages incoming virus particles, prevents their cytoplasmic entry, and accelerates their lysosomal clearance by host cells. However, how -palmitoylation modulates the structure and biophysical characteristics of IFITM3 to promote its antiviral activity remains unclear. To investigate how site-specific -palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes. Collectively, our results demonstrate that site-specific -palmitoylation of IFITM3 directly alters its biophysical properties and activity in cells to prevent virus infection.
AbstractList Interferon-induced transmembrane proteins (IFITMs) are S -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. S -palmitoylated IFITM3 in particular engages incoming virus particles, prevents their cytoplasmic entry, and accelerates their lysosomal clearance by host cells. However, how S -palmitoylation modulates the structure and biophysical characteristics of IFITM3 to promote its antiviral activity remains unclear. To investigate how site-specific S -palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes. Collectively, our results demonstrate that site-specific S -palmitoylation of IFITM3 directly alters its biophysical properties and activity in cells to prevent virus infection.
Interferon-induced transmembrane proteins (IFITMs) are -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. -palmitoylated IFITM3 in particular engages incoming virus particles, prevents their cytoplasmic entry, and accelerates their lysosomal clearance by host cells. However, how -palmitoylation modulates the structure and biophysical characteristics of IFITM3 to promote its antiviral activity remains unclear. To investigate how site-specific -palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes. Collectively, our results demonstrate that site-specific -palmitoylation of IFITM3 directly alters its biophysical properties and activity in cells to prevent virus infection.
Author Im, Wonpil
Percher, Avital
Li, Yumeng
Bhattacharya, Shibani
Peng, Tao
Lee, Hwayoung
Das, Tandrila
Wiewiora, Rafal
Witte, Isaac P
Garst, Emma H
Hang, Howard C
AuthorAffiliation 1 Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York 10065, United States
2 Tri-Institutional Ph.D. Program in Chemical Biology, New York, NY 10065, United States
5 Memorial Sloan Kettering Cancer Center, New York, NY 10065, United States
7 Departments of Immunology and Microbiology and Chemistry, Scripps Research, La Jolla, CA 92037, United States
6 State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen 518055, China
3 Department of Biological Sciences, Chemistry, and Bioengineering, Lehigh University, Bethlehem, PA 18015, United States
4 New York Structural Biology Center, New York, NY 10027, United States
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Cites_doi 10.15252/embj.2020106267
10.1074/jbc.M113.514356
10.1038/s41586-020-2884-6
10.1080/22221751.2020.1787797
10.1371/journal.ppat.1007532
10.1093/infdis/jix512
10.15252/embj.2020106501
10.1016/j.cell.2017.11.018
10.1074/jbc.M114.557694
10.1021/cr2001977
10.1074/jbc.AC119.010611
10.1093/nar/gky995
10.1146/annurev-virology-031413-085537
10.1093/infdis/jix242
10.1016/j.celrep.2016.05.074
10.1038/nchembio.405
10.1002/eji.201847692
10.1073/pnas.0710389105
10.1038/nchembio.388
10.1021/ja054842f
10.1038/nrm2084
10.1146/annurev.biochem.052308.105824
10.1074/jbc.M112.362095
10.1146/annurev-biochem-060713-035737
10.1016/j.chembiol.2020.03.004
10.1021/acsnano.0c10567
10.1371/journal.ppat.1004048
10.1021/acs.jproteome.8b00002
10.1038/nature10921
10.1083/jcb.200404100
10.1016/j.cell.2009.12.017
10.1128/JVI.00481-13
10.1016/j.jmb.2013.09.024
10.1038/nchembio834
10.1128/JVI.01254-16
10.1039/D0CC06073A
10.2217/fmb.14.65
10.1371/journal.ppat.1001258
10.1021/jacs.6b08733
10.1074/jbc.M117.800482
10.1073/pnas.1900784116
10.1073/pnas.1602244113
10.1016/j.cbpa.2013.07.031
10.15252/embr.201642771
10.1371/journal.pone.0104341
10.1093/infdis/jiaa224
10.1038/nature09907
10.1007/s10858-009-9333-z
10.1083/jcb.200507067
10.1038/srep24029
10.1016/j.cell.2010.04.007
10.1074/jbc.M110.173583
10.1002/anie.201707554
10.1038/s41589-018-0213-2
10.1038/s41586-020-2355-0
10.1038/nm.4370
10.1126/science.1105654
10.1371/journal.pone.0143539
10.1073/pnas.1016184107
10.1021/cr400355w
10.4049/jimmunol.1201305
10.1016/j.cbpa.2013.08.004
10.15252/embr.201744100
10.1002/anie.201914836
10.1016/j.chom.2013.03.006
10.26508/lsa.201900542
10.1038/nchembio0605-13
10.1038/ni.2525
10.1038/emboj.2012.15
10.1016/0092-8674(84)90270-8
10.1126/science.aaw7733
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References ref9/cit9
ref45/cit45
ref3/cit3
ref27/cit27
ref63/cit63
Prelli Bozzo C. (ref74/cit74) 2020
ref56/cit56
ref16/cit16
ref52/cit52
ref23/cit23
ref8/cit8
ref31/cit31
ref59/cit59
ref2/cit2
ref34/cit34
ref71/cit71
ref37/cit37
ref20/cit20
ref48/cit48
ref60/cit60
ref17/cit17
Buchrieser J. (ref19/cit19) 2019; 365
ref10/cit10
ref35/cit35
ref53/cit53
ref21/cit21
ref42/cit42
ref46/cit46
ref49/cit49
ref13/cit13
ref61/cit61
ref67/cit67
ref24/cit24
ref38/cit38
ref50/cit50
ref64/cit64
ref54/cit54
ref6/cit6
ref36/cit36
ref18/cit18
ref65/cit65
ref11/cit11
ref25/cit25
ref72/cit72
ref32/cit32
ref39/cit39
ref14/cit14
ref57/cit57
ref5/cit5
ref51/cit51
ref43/cit43
ref28/cit28
ref40/cit40
ref68/cit68
ref26/cit26
Zang R. (ref29/cit29) 2020; 30
ref55/cit55
ref73/cit73
ref69/cit69
ref12/cit12
ref15/cit15
ref62/cit62
ref66/cit66
ref41/cit41
ref58/cit58
ref22/cit22
ref33/cit33
ref4/cit4
ref30/cit30
ref47/cit47
ref1/cit1
ref44/cit44
ref70/cit70
ref7/cit7
References_xml – ident: ref27/cit27
  doi: 10.15252/embj.2020106267
– ident: ref38/cit38
  doi: 10.1074/jbc.M113.514356
– ident: ref17/cit17
  doi: 10.1038/s41586-020-2884-6
– ident: ref28/cit28
  doi: 10.1080/22221751.2020.1787797
– ident: ref34/cit34
  doi: 10.1371/journal.ppat.1007532
– ident: ref23/cit23
  doi: 10.1093/infdis/jix512
– ident: ref73/cit73
  doi: 10.15252/embj.2020106501
– ident: ref13/cit13
  doi: 10.1016/j.cell.2017.11.018
– ident: ref44/cit44
  doi: 10.1074/jbc.M114.557694
– ident: ref70/cit70
  doi: 10.1021/cr2001977
– ident: ref18/cit18
  doi: 10.1074/jbc.AC119.010611
– ident: ref41/cit41
  doi: 10.1093/nar/gky995
– ident: ref8/cit8
  doi: 10.1146/annurev-virology-031413-085537
– ident: ref22/cit22
  doi: 10.1093/infdis/jix242
– ident: ref7/cit7
  doi: 10.1016/j.celrep.2016.05.074
– ident: ref46/cit46
  doi: 10.1038/nchembio.405
– ident: ref16/cit16
  doi: 10.1002/eji.201847692
– ident: ref56/cit56
  doi: 10.1073/pnas.0710389105
– ident: ref57/cit57
  doi: 10.1038/nchembio.388
– start-page: 1
  year: 2020
  ident: ref74/cit74
  publication-title: bioRxiv
  contributor:
    fullname: Prelli Bozzo C.
– ident: ref67/cit67
  doi: 10.1021/ja054842f
– ident: ref69/cit69
  doi: 10.1038/nrm2084
– ident: ref58/cit58
  doi: 10.1146/annurev.biochem.052308.105824
– ident: ref37/cit37
  doi: 10.1074/jbc.M112.362095
– ident: ref59/cit59
  doi: 10.1146/annurev-biochem-060713-035737
– ident: ref45/cit45
  doi: 10.1016/j.chembiol.2020.03.004
– volume: 30
  start-page: 555
  year: 2020
  ident: ref29/cit29
  publication-title: BioRxiv
  contributor:
    fullname: Zang R.
– ident: ref43/cit43
  doi: 10.1021/acsnano.0c10567
– ident: ref32/cit32
  doi: 10.1371/journal.ppat.1004048
– ident: ref65/cit65
  doi: 10.1021/acs.jproteome.8b00002
– ident: ref4/cit4
  doi: 10.1038/nature10921
– ident: ref51/cit51
  doi: 10.1083/jcb.200404100
– ident: ref2/cit2
  doi: 10.1016/j.cell.2009.12.017
– ident: ref5/cit5
  doi: 10.1128/JVI.00481-13
– ident: ref9/cit9
  doi: 10.1016/j.jmb.2013.09.024
– ident: ref68/cit68
  doi: 10.1038/nchembio834
– ident: ref12/cit12
  doi: 10.1128/JVI.01254-16
– ident: ref62/cit62
  doi: 10.1039/D0CC06073A
– ident: ref30/cit30
  doi: 10.2217/fmb.14.65
– ident: ref6/cit6
  doi: 10.1371/journal.ppat.1001258
– ident: ref31/cit31
  doi: 10.1021/jacs.6b08733
– ident: ref48/cit48
  doi: 10.1074/jbc.M117.800482
– ident: ref10/cit10
  doi: 10.1073/pnas.1900784116
– ident: ref47/cit47
  doi: 10.1073/pnas.1602244113
– ident: ref63/cit63
  doi: 10.1016/j.cbpa.2013.07.031
– ident: ref21/cit21
  doi: 10.15252/embr.201642771
– ident: ref39/cit39
  doi: 10.1371/journal.pone.0104341
– ident: ref25/cit25
  doi: 10.1093/infdis/jiaa224
– ident: ref3/cit3
  doi: 10.1038/nature09907
– ident: ref66/cit66
  doi: 10.1007/s10858-009-9333-z
– ident: ref52/cit52
  doi: 10.1083/jcb.200507067
– ident: ref40/cit40
  doi: 10.1038/srep24029
– ident: ref49/cit49
  doi: 10.1016/j.cell.2010.04.007
– ident: ref54/cit54
  doi: 10.1074/jbc.M110.173583
– ident: ref72/cit72
  doi: 10.1002/anie.201707554
– ident: ref33/cit33
  doi: 10.1038/s41589-018-0213-2
– ident: ref26/cit26
  doi: 10.1038/s41586-020-2355-0
– ident: ref35/cit35
  doi: 10.1021/acsnano.0c10567
– ident: ref24/cit24
  doi: 10.1038/nm.4370
– ident: ref50/cit50
  doi: 10.1126/science.1105654
– ident: ref11/cit11
  doi: 10.1371/journal.pone.0143539
– ident: ref53/cit53
  doi: 10.1073/pnas.1016184107
– ident: ref61/cit61
  doi: 10.1021/cr400355w
– ident: ref15/cit15
  doi: 10.4049/jimmunol.1201305
– ident: ref64/cit64
  doi: 10.1016/j.cbpa.2013.08.004
– ident: ref42/cit42
  doi: 10.15252/embr.201744100
– ident: ref71/cit71
  doi: 10.1002/anie.201914836
– ident: ref36/cit36
  doi: 10.1016/j.chom.2013.03.006
– ident: ref20/cit20
  doi: 10.26508/lsa.201900542
– ident: ref60/cit60
  doi: 10.1038/nchembio0605-13
– ident: ref14/cit14
  doi: 10.1038/ni.2525
– ident: ref55/cit55
  doi: 10.1038/emboj.2012.15
– ident: ref1/cit1
  doi: 10.1016/0092-8674(84)90270-8
– volume: 365
  start-page: 176
  year: 2019
  ident: ref19/cit19
  publication-title: Science
  doi: 10.1126/science.aaw7733
  contributor:
    fullname: Buchrieser J.
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Snippet Interferon-induced transmembrane proteins (IFITMs) are -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. -palmitoylated IFITM3...
Interferon-induced transmembrane proteins (IFITMs) are S -palmitoylated proteins in vertebrates that restrict a diverse range of viruses. S -palmitoylated...
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SourceType Open Access Repository
Aggregation Database
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SubjectTerms Amino Acid Sequence
Antiviral Agents - chemistry
Antiviral Agents - pharmacology
Binding Sites
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Computational Biology
Drug Design
Humans
Interferons - chemistry
Interferons - pharmacology
Lipids - chemistry
Lipoylation
Lysosomes - metabolism
Membrane Proteins - metabolism
Molecular Dynamics Simulation
Protein Binding
Protein Conformation
RNA-Binding Proteins - metabolism
Signal Transduction
Title Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity
URI https://www.ncbi.nlm.nih.gov/pubmed/33887136
https://pubmed.ncbi.nlm.nih.gov/PMC9112659
Volume 16
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