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Crystal structure of measles virus matrix proteinCrystal structure of measles virus matrix protein
Structural highlights
FunctionMATRX_MEASC The M protein has a crucial role in virus assembly and interacts with the RNP complex as well as with the viral membrane. Publication Abstract from PubMedMeasles 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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