Virus

Phosphatidylinositol 4,5-bisphosphate

Phosphatidylserine

Mononegavirales

Paramyxoviridae

Viral protein

Viral membrane

Membrane

Viral matrix protein

VP40

Biology

Viral envelope

Biophysics

Viral replication

Virology

Vaccination

Chemistry

Measles

Budding

Phosphatidylinositol

Measles virus

Viral disease

Phospholipid

Lipid bilayer

Signal transduction

Cell biology

Biochemistry

Viral entry

Science Advances

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

Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization