7skt

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Nipah virus matrix protein

Structural highlights

7skt is a 2 chain structure with sequence from Nipah henipavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.048Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MATRX_NIPAV Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane (PubMed:17005661, PubMed:17204159, PubMed:19000317). Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane (PubMed:21085610). Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles (PubMed:28250132). Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6 (PubMed:27622505).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Measles virus, Nipah virus, and multiple other paramyxoviruses cause disease outbreaks in humans and animals worldwide. The paramyxovirus matrix (M) protein mediates virion assembly and budding from host cell membranes. M is thus a key target for antivirals, but few high-resolution structures of paramyxovirus M are available, and we lack the clear understanding of how viral M proteins interact with membrane lipids to mediate viral assembly and egress that is needed to guide antiviral design. Here, we reveal that M proteins associate with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] at the plasma membrane. Using x-ray crystallography, electron microscopy, and molecular dynamics, we demonstrate that PI(4,5)P2 binding induces conformational and electrostatic changes in the M protein surface that trigger membrane deformation, matrix layer polymerization, and virion assembly.

Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.,Norris MJ, Husby ML, Kiosses WB, Yin J, Saxena R, Rennick LJ, Heiner A, Harkins SS, Pokhrel R, Schendel SL, Hastie KM, Landeras-Bueno S, Salie ZL, Lee B, Chapagain PP, Maisner A, Duprex WP, Stahelin RV, Saphire EO Sci Adv. 2022 Jul 22;8(29):eabn1440. doi: 10.1126/sciadv.abn1440. Epub 2022 Jul, 20. PMID:35857835^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ciancanelli MJ, Basler CF. Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization. J Virol. 2006 Dec;80(24):12070-8. PMID:17005661 doi:10.1128/JVI.01743-06
↑ Patch JR, Crameri G, Wang LF, Eaton BT, Broder CC. Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein. Virol J. 2007 Jan 4;4:1. PMID:17204159 doi:10.1186/1743-422X-4-1
↑ Patch JR, Han Z, McCarthy SE, Yan L, Wang LF, Harty RN, Broder CC. The YPLGVG sequence of the Nipah virus matrix protein is required for budding. Virol J. 2008 Nov 10;5:137. PMID:19000317 doi:10.1186/1743-422X-5-137
↑ Wang YE, Park A, Lake M, Pentecost M, Torres B, Yun TE, Wolf MC, Holbrook MR, Freiberg AN, Lee B. Ubiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus matrix protein is important for viral budding. PLoS Pathog. 2010 Nov 11;6(11):e1001186. PMID:21085610 doi:10.1371/journal.ppat.1001186
↑ Bharaj P, Wang YE, Dawes BE, Yun TE, Park A, Yen B, Basler CF, Freiberg AN, Lee B, Rajsbaum R. The Matrix Protein of Nipah Virus Targets the E3-Ubiquitin Ligase TRIM6 to Inhibit the IKKε Kinase-Mediated Type-I IFN Antiviral Response. PLoS Pathog. 2016 Sep 13;12(9):e1005880. PMID:27622505 doi:10.1371/journal.ppat.1005880
↑ Johnston GP, Contreras EM, Dabundo J, Henderson BA, Matz KM, Ortega V, Ramirez A, Park A, Aguilar HC. Cytoplasmic Motifs in the Nipah Virus Fusion Protein Modulate Virus Particle Assembly and Egress. J Virol. 2017 Apr 28;91(10):e02150-16. PMID:28250132 doi:10.1128/JVI.02150-16
↑ Norris MJ, Husby ML, Kiosses WB, Yin J, Saxena R, Rennick LJ, Heiner A, Harkins SS, Pokhrel R, Schendel SL, Hastie KM, Landeras-Bueno S, Salie ZL, Lee B, Chapagain PP, Maisner A, Duprex WP, Stahelin RV, Saphire EO. Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization. Sci Adv. 2022 Jul 22;8(29):eabn1440. PMID:35857835 doi:10.1126/sciadv.abn1440

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7skt"

Categories: Large Structures | Nipah henipavirus | Norris MJ | Saphire EO

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7skt is ON HOLD
+==Crystal structure of Nipah virus matrix protein==
+<StructureSection load='7skt' size='340' side='right'caption='[[7skt]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7skt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nipah_henipavirus Nipah henipavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SKT FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.048&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7skt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7skt OCA], [https://pdbe.org/7skt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7skt RCSB], [https://www.ebi.ac.uk/pdbsum/7skt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7skt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MATRX_NIPAV MATRX_NIPAV] Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane (PubMed:17005661, PubMed:17204159, PubMed:19000317). Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane (PubMed:21085610). Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles (PubMed:28250132). Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6 (PubMed:27622505).<ref>PMID:17005661</ref> <ref>PMID:17204159</ref> <ref>PMID:19000317</ref> <ref>PMID:21085610</ref> <ref>PMID:27622505</ref> <ref>PMID:28250132</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Measles virus, Nipah virus, and multiple other paramyxoviruses cause disease outbreaks in humans and animals worldwide. The paramyxovirus matrix (M) protein mediates virion assembly and budding from host cell membranes. M is thus a key target for antivirals, but few high-resolution structures of paramyxovirus M are available, and we lack the clear understanding of how viral M proteins interact with membrane lipids to mediate viral assembly and egress that is needed to guide antiviral design. Here, we reveal that M proteins associate with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] at the plasma membrane. Using x-ray crystallography, electron microscopy, and molecular dynamics, we demonstrate that PI(4,5)P2 binding induces conformational and electrostatic changes in the M protein surface that trigger membrane deformation, matrix layer polymerization, and virion assembly.
-Authors:
+Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.,Norris MJ, Husby ML, Kiosses WB, Yin J, Saxena R, Rennick LJ, Heiner A, Harkins SS, Pokhrel R, Schendel SL, Hastie KM, Landeras-Bueno S, Salie ZL, Lee B, Chapagain PP, Maisner A, Duprex WP, Stahelin RV, Saphire EO Sci Adv. 2022 Jul 22;8(29):eabn1440. doi: 10.1126/sciadv.abn1440. Epub 2022 Jul, 20. PMID:35857835<ref>PMID:35857835</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7skt" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Nipah henipavirus]]
+[[Category: Norris MJ]]
+[[Category: Saphire EO]]

7skt

From Proteopedia

Current revision

Crystal structure of Nipah virus matrix protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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