7SKS

Crystal structure of measles virus matrix protein

Summary for 7SKS

• Entry DOI: 10.2210/pdb7sks/pdb
• Descriptor: Matrix protein (2 entities in total)
• Functional Keywords: matrix, dimer, viral assembly, viral protein
• Biological source: Measles virus (MeV, Subacute sclerose panencephalitis virus)
• Total number of polymer chains: 2
• Total formula weight: 83473.70

Authors

Norris, M.J.,Saphire, E.O. (deposition date: 2021-10-21, release date: 2022-08-24, Last modification date: 2023-10-18)

Primary citation

Norris, M.J.,Husby, M.L.,Kiosses, W.B.,Yin, J.,Saxena, R.,Rennick, L.J.,Heiner, A.,Harkins, S.S.,Pokhrel, R.,Schendel, S.L.,Hastie, K.M.,Landeras-Bueno, S.,Salie, Z.L.,Lee, B.,Chapagain, P.P.,Maisner, A.,Duprex, W.P.,Stahelin, R.V.,Saphire, E.O.
Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization.
Sci Adv, 8:eabn1440-eabn1440, 2022

PubMed Abstract: 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)P] at the plasma membrane. Using x-ray crystallography, electron microscopy, and molecular dynamics, we demonstrate that PI(4,5)P binding induces conformational and electrostatic changes in the M protein surface that trigger membrane deformation, matrix layer polymerization, and virion assembly.

PubMed: 35857835
DOI: 10.1126/sciadv.abn1440

Experimental method

X-RAY DIFFRACTION (2.541 Å)