title: Unity in diversity: shared mechanism of entry among paramyxoviruses.
abstract: The Paramyxoviridae family includes many viruses that are pathogenic in humans, including parainfluenza viruses, measles virus, respiratory syncytial virus, and the emerging zoonotic Henipaviruses. No effective treatments are currently available for these viruses, and there is a need for efficient antiviral therapies. Paramyxoviruses enter the target cell by binding to a cell surface receptor and then fusing the viral envelope with the target cell membrane, allowing the release of the viral genome into the cytoplasm. Blockage of these crucial steps prevents infection and disease. Binding and fusion are driven by two virus-encoded glycoproteins, the receptor-binding protein and the fusion protein, that together form the viral "fusion machinery." The development of efficient antiviral drugs requires a deeper understanding of the mechanism of action of the Paramyxoviridae fusion machinery, which is still controversial. Here, we review recent structural and functional data on these proteins and the current understanding of the mechanism of the paramyxovirus cell entry process.
authors.affiliation: Department of Pediatrics, Weill Cornell Medical College, Cornell University, New York, USA; Department of Biology, Ecole Normale Supérieure, Lyon, France.
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Palgen
authors.affiliation: Department of Pediatrics, Weill Cornell Medical College, Cornell University, New York, USA.
authors.forename: Eric M
authors.initials: EM
authors.lastname: Jurgens
authors.affiliation: Department of Pediatrics, Weill Cornell Medical College, Cornell University, New York, USA; Department of Microbiology and Immunology, Weill Cornell Medical College, Cornell University, New York, USA.
authors.forename: Anne
authors.initials: A
authors.lastname: Moscona
authors.affiliation: Department of Pediatrics, Weill Cornell Medical College, Cornell University, New York, USA. Electronic address: map2028@med.cornell.edu.
authors.forename: Matteo
authors.initials: M
authors.lastname: Porotto
authors.affiliation: Department of Pediatrics, Weill Cornell Medical College, Cornell University, New York, USA; Department of Microbiology and Immunology, Weill Cornell Medical College, Cornell University, New York, USA.
authors.forename: Laura M
authors.initials: LM
authors.lastname: Palermo
mesh_terms: D000818:Animals; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D010252:Paramyxoviridae / Q000145:classification / Q000502:physiology*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism; D053586:Virus Internalization
chemical_list: D006023:Glycoproteins; D011956:Receptors, Cell Surface; D014764:Viral Proteins
keywords: Fusion machinery; Fusion protein; Paramyxoviridae; Receptor-binding protein; Viral entry