F Protein Paramyxovirus

Recently the atomic structure at 14 A of an extremely thermostable six-helix bundle core complex consisting of two heptad repeat regions of the F protein has been described K. Paramyxovirus F proteins together with influenza virus HA Ebola virus GP and HIV Env among others are classified as class I viral fusion proteins 35.

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01032001 The fusion F protein of the paramyxovirus SV5 promotes both viruscell and cellcell fusion.

F protein paramyxovirus. SV5 strains W3A and WR differ by three amin. Like all paramyxovirus F proteins the NDV F protein is glycosylated. For review see Lamb and Kolakofsky 2001.

Upon triggering the trimeric F protein undergoes a large irreversible conformation change to drive membrane fusion. 24062014 F proteins from different paramyxoviruses have different energy requirements for activation 24 29 33 34. Paramyxoviruses initiate infection by attaching to cell surface receptors and fusing viral and cell membranes.

Fusion of the paramyxovirus envelope and the host cell membrane is brought about by the interaction of two surface glycoproteins the hemagglutinin-neuraminidase protein HN and the fusion F protein. According to the current knowledge of paramyxovirus-induced membrane fusion the F protein is triggered by the attachment protein and undergoes a series of structural rearrangements from a prefusion to a postfusion F state passing through a putative prehairpin structural intermediate. Russell et al.

Viral attachment proteins hemagglutinin-neuraminidase HN hemagglutinin HA or glycoprotein G bind receptors while fusion F proteins direct membrane fusion. The results revealed that the pathogenicity of the virus is determined by multiple genes. The F 0 must be proteolytically cleaved to F 1 and F 2 for fusion activity reviewed in Ref.

Recently the atomic structure at 14. 08072019 This indicates that the NP protein influences virus virulence by affecting replication in chickens while the F protein might influence virus virulence in other ways not related to replication. The fusion F protein of the paramyxovirus SV5 strain W3A causes syncytium formation without coexpression of the SV5 hemagglutinin-neuraminidase HN glycoprotein whereas the F protein of the SV5 strain WR requires coexpression of HN for fusion activity.

Wang C1 Raghu G Morrison T Peeples ME. Binding sialates to hemagglutinin-neuraminidase HN activates triggers the fusion protein F to start the membrane fusion process of paramyxovirus but the mechanism by which the HN and F associate with each other to induce membrane fusion is still unclear. Paramyxovirus F protein is a type I viral fusion protein with mechanistic features common to the fusion proteins of several other viruses including human immunodeficiency virus HIV Env influenza virus hemagglutinin HA and Ebola virus glycoprotein GP 31.

It is noteworthy to study the interaction domains of HN and F of paramyxovirus. Critical role of the predicted amphipathic alpha helix adjacent to the fusion domain. The fusion F protein of the paramyxovirus SV5 promotes both virus-cell and cell-cell fusion.

Cell 3 309319 1999. The three chimeric viruses did not cause death in 4-week-old chickens but the clinical signs and lesions were more severe than those caused by the parental strain and microscopic lesions were. Of an extremely thermostable six-helix bundle core complex consisting of two heptad repeat regions of the F protein has been described K.

1Department of ImmunologyMicrobiology Rush-Presbyterian-St. Intracellular processing of the paramyxovirus F protein. Lukes Medical Center Chicago Illinois 60612.

F the fusion protein projects from the envelope surface as a trimer and mediates cell entry by inducing fusion between the viral envelope and the cell membrane by class I fusion. 11072003 Typical of paramyxovirus F proteins the NDV F protein is a 553-amino-acid protein and is synthesized as a precursor F 0 diagramed in Fig. The NP protein and F protein were found to have the strongest individual effect on virulence and this effect further enhanced when the two proteins were expressed in combination.

Cell 3 309-319 1999. 27102003 Activation of most paramyxovirus F proteins at neutral pH is thought to be triggered by a three-step process including binding of the viral receptor-binding protein RBP HN or H to its receptor HN interacting with F and the HNF interaction leading to changes in F that mediate membrane fusion Crennell et al 2000. 13082019 The zoonotic Hendra virus HeV a member of the family Paramyxoviridae utilizes the attachment protein G and the fusion protein F to perform these critical functions.

One of the defining characteristics of members of the family Paramyxoviridae is the requirement for a neutral pH for fusogenic activity.

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