Abstract Nipah virus is a highly pathogenic virus in the family Paramyxoviridae that utilizes two distinct surface glycoproteins to infect cells . The receptor-binding protein (RBP) binds host receptors whereas the fusion protein (F) merges viral and host membranes . Here, we use nonreplicative pseudoviruses to safely measure the effects of all F single amino acid residue mutations on its cell entry function and neutralization by monoclonal antibodies . We compare mutational tolerance in F with previous experimental measurements for RBP and show that F is much more functionally constrained than the RBP . We also identify mutationally intolerant sites on the F trimer surface and core that are critical for proper function, and describe mutations that are candidates for stabilizing F in the prefusion conformation for vaccine design . We quantify how F mutations affect neutralization by six monoclonal antibodies, and show that the magnitude of mutational effects on neutralization var...
Abstract Mpox, caused by the monkeypox virus (MPXV; Orthopoxvirus monkeypox), is on the rise in West and Central Africa . African rodents , especially squirrels , are suspected to be involved in MPXV emergence , but no evidence of a direct transmission to humans or non-human primates has been established. Here we describe an outbreak of MPXV in a group of wild sooty mangabeys (Cercocebus atys) in TaĂ¯ National Park (CĂ´te d’Ivoire). The outbreak affected one-third of the group, killing four infants . To track its origin, we analysed rodents and wildlife carcasses from the region. We identified a MPXV-infected fire-footed rope squirrel (Funisciurus pyrropus), found dead 3 km from the mangabey territory 12 weeks before the outbreak. MPXV genomes from the squirrel and the mangabey were nearly identical. A video record from 2014 showed a mangabey from this group eating the same squirrel species and diet metabarcoding of faecal samples collected from mangabeys before the outbreak identi...