دورية أكاديمية
Reversible structural changes in the influenza hemagglutinin precursor at membrane fusion pH.
العنوان: | Reversible structural changes in the influenza hemagglutinin precursor at membrane fusion pH. |
---|---|
المؤلفون: | Garcia-Moro E; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Zhang J; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Calder LJ; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Brown NR; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Gamblin SJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Skehel JJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom., Rosenthal PB; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 AT London, United Kingdom. |
المصدر: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Aug 16; Vol. 119 (33), pp. e2208011119. Date of Electronic Publication: 2022 Aug 08. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Washington, DC : National Academy of Sciences |
مواضيع طبية MeSH: | Hemagglutinin Glycoproteins, Influenza Virus*/chemistry , Membrane Fusion* , Orthomyxoviridae*/physiology , Virus Internalization*, Humans ; Hydrogen-Ion Concentration ; Protein Conformation |
مستخلص: | The subunits of the influenza hemagglutinin (HA) trimer are synthesized as single-chain precursors (HA0s) that are proteolytically cleaved into the disulfide-linked polypeptides HA1 and HA2. Cleavage is required for activation of membrane fusion at low pH, which occurs at the beginning of infection following transfer of cell-surface-bound viruses into endosomes. Activation results in extensive changes in the conformation of cleaved HA. To establish the overall contribution of cleavage to the mechanism of HA-mediated membrane fusion, we used cryogenic electron microscopy (cryo-EM) to directly image HA0 at neutral and low pH. We found extensive pH-induced structural changes, some of which were similar to those described for intermediates in the refolding of cleaved HA at low pH. They involve a partial extension of the long central coiled coil formed by melting of the preexisting secondary structure, threading it between the membrane-distal domains, and subsequent refolding as extended helices. The fusion peptide, covalently linked at its N terminus, adopts an amphipathic helical conformation over part of its length and is repositioned and packed against a complementary surface groove of conserved residues. Furthermore, and in contrast to cleaved HA, the changes in HA0 structure at low pH are reversible on reincubation at neutral pH. We discuss the implications of covalently restricted HA0 refolding for the cleaved HA conformational changes that mediate membrane fusion and for the action of antiviral drug candidates and cross-reactive anti-HA antibodies that can block influenza infectivity. |
References: | Virology. 1992 Sep;190(1):11-8. (PMID: 1529523) Nat Struct Mol Biol. 2015 Nov;22(11):833-4. (PMID: 26581513) Cell. 1998 Oct 30;95(3):409-17. (PMID: 9814710) Elife. 2013 Feb 19;2:e00333. (PMID: 23550179) Virology. 1986 Dec;155(2):484-97. (PMID: 3788061) Biochemistry. 2004 May 18;43(19):5902-11. (PMID: 15134464) Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8967-72. (PMID: 10430879) Proc Natl Acad Sci U S A. 2017 Jan 10;114(2):206-214. (PMID: 28003465) Cell. 1985 Feb;40(2):431-9. (PMID: 3967299) Biophys J. 1994 Dec;67(6):2355-60. (PMID: 7696474) J Struct Biol. 2012 Dec;180(3):519-30. (PMID: 23000701) J Virol. 2011 May;85(10):5172-82. (PMID: 21367895) Protein Sci. 2018 Jan;27(1):293-315. (PMID: 29067766) Antiviral Res. 2009 Feb;81(2):132-40. (PMID: 19028526) PLoS Pathog. 2020 Nov 30;16(11):e1009062. (PMID: 33253316) Virology. 1992 May;188(1):14-24. (PMID: 1566569) J Mol Graph. 1996 Dec;14(6):354-60, 376. (PMID: 9195488) Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12205-9. (PMID: 8618870) Biochim Biophys Acta. 2007 Dec;1768(12):3052-60. (PMID: 17963720) Virology. 1971 Jul;45(1):275-88. (PMID: 5165251) Proc Natl Acad Sci U S A. 2014 Jul 29;111(30):11175-80. (PMID: 25024224) Nature. 2022 Feb;602(7896):314-320. (PMID: 34942633) Nature. 1981 Jan 29;289(5796):366-73. (PMID: 7464906) Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67. (PMID: 21460454) Sci Adv. 2020 Apr 29;6(18):eaaz8822. (PMID: 32494683) Virology. 1985 Aug;145(1):72-83. (PMID: 2409671) Nature. 1982 Dec 16;300(5893):658-9. (PMID: 6815542) J Virol. 2019 Oct 15;93(21):. (PMID: 31391268) J Struct Biol. 2015 Nov;192(2):216-21. (PMID: 26278980) J Virol. 1991 Sep;65(9):4853-9. (PMID: 1870204) J Struct Biol. 2019 Jan 1;205(1):30-40. (PMID: 30502495) Nat Methods. 2017 Mar;14(3):290-296. (PMID: 28165473) Elife. 2015 Nov 27;4:e11009. (PMID: 26613408) Annu Rev Biochem. 1987;56:365-94. (PMID: 3304138) Proc Natl Acad Sci U S A. 2018 Oct 2;115(40):10112-10117. (PMID: 30224494) Cell Rep. 2017 Aug 1;20(5):1201-1214. (PMID: 28768203) EMBO J. 1987 Sep;6(9):2643-50. (PMID: 3315651) Commun Biol. 2021 Jul 15;4(1):874. (PMID: 34267316) Virology. 1975 Dec;68(2):440-54. (PMID: 128196) Protein Sci. 2021 Jan;30(1):70-82. (PMID: 32881101) Cell. 2018 Aug 9;174(4):926-937.e12. (PMID: 29961575) Virology. 1975 Dec;68(2):426-39. (PMID: 173078) Proc Natl Acad Sci U S A. 2017 Jan 3;114(1):E28-E36. (PMID: 27974607) Nature. 2020 Jul;583(7814):150-153. (PMID: 32461688) Proc Natl Acad Sci U S A. 1975 Jan;72(1):93-7. (PMID: 1054518) Trends Microbiol. 1994 Feb;2(2):39-43. (PMID: 8162439) EMBO J. 1992 Jul;11(7):2407-14. (PMID: 1628614) Proc Natl Acad Sci U S A. 2012 Dec 4;109(49):19994-9. (PMID: 23169643) J Mol Biol. 1996 Jul 19;260(3):312-6. (PMID: 8757795) Nature. 1994 Sep 1;371(6492):37-43. (PMID: 8072525) Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501. (PMID: 20383002) J Gen Virol. 1983 Aug;64 (Pt 8):1657-62. (PMID: 6192202) Virology. 1999 May 25;258(1):1-20. (PMID: 10329563) J Virol. 2015 Jul;89(14):7417-20. (PMID: 25926650) Biochim Biophys Acta Gen Subj. 2020 Feb;1864(2):129313. (PMID: 30825615) Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17736-41. (PMID: 19004788) Elife. 2018 Nov 09;7:. (PMID: 30412051) Arch Virol. 1988;101(1-2):119-23. (PMID: 3415477) Virology. 1971 May;44(2):396-408. (PMID: 4998414) Acta Crystallogr D Struct Biol. 2018 Jun 1;74(Pt 6):519-530. (PMID: 29872003) EMBO J. 2002 Nov 1;21(21):5701-10. (PMID: 12411488) Annu Rev Biochem. 2000;69:531-69. (PMID: 10966468) Arch Biochem Biophys. 2015 Sep 1;581:86-97. (PMID: 25958107) EMBO J. 1986 Jan;5(1):41-9. (PMID: 3956479) Commun Biol. 2019 Jun 19;2:218. (PMID: 31240256) J Gen Virol. 1977 Jul;36(1):151-61. (PMID: 142124) Nat Methods. 2017 Apr;14(4):331-332. (PMID: 28250466) Virology. 2015 May;479-480:498-507. (PMID: 25866377) J Biol Chem. 1997 Apr 11;272(15):9764-70. (PMID: 9092509) J Biol Chem. 1988 Mar 25;263(9):4474-80. (PMID: 3346256) Curr Top Microbiol Immunol. 2014;385:3-34. (PMID: 25031010) Proc Natl Acad Sci U S A. 1982 Feb;79(4):968-72. (PMID: 6951181) Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11341-6. (PMID: 20534508) EMBO J. 2002 Mar 1;21(5):865-75. (PMID: 11867515) |
معلومات مُعتمدة: | FC001078 United Kingdom CRUK_ Cancer Research UK; FC001078 United Kingdom MRC_ Medical Research Council; FC001078 United Kingdom WT_ Wellcome Trust; FC001143 United Kingdom CRUK_ Cancer Research UK; FC001143 United Kingdom MRC_ Medical Research Council; FC001143 United Kingdom WT_ Wellcome Trust; 219946/Z/19/Z United Kingdom WT_ Wellcome Trust |
فهرسة مساهمة: | Keywords: cryo-EM; hemagglutinin; influenza; membrane fusion; protein folding |
المشرفين على المادة: | 0 (Hemagglutinin Glycoproteins, Influenza Virus) |
تواريخ الأحداث: | Date Created: 20220808 Date Completed: 20220810 Latest Revision: 20220930 |
رمز التحديث: | 20221213 |
مُعرف محوري في PubMed: | PMC9388137 |
DOI: | 10.1073/pnas.2208011119 |
PMID: | 35939703 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1091-6490 |
---|---|
DOI: | 10.1073/pnas.2208011119 |