Mutations located on both F1 and F2 subunits of the Newcastle disease virus fusion protein confer resistance to neutralization with monoclonal antibodies

110

New series of escape mutants of human respiratory syncytial virus were prepared with monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes, and previously identified antigenic sites, were incorporated into a refined prediction of secondary-structure motifs to generate a detailed antigenic map of the F glycoprotein.

Section: Figmentioning

confidence: 99%

Antigenic Structure of Human Respiratory Syncytial Virus Fusion Glycoprotein

López

Bustos

Örvell

et al. 1998

110

“…Thus, it seems possible that Sendai virus F2 has a noncovalent but tight association with the F1 molecule in addition to the covalent association via the intermolecular disulfide bridge. Interestingly, in this context, studies on neutralization escape mutants of Newcastle disease virus have suggested a topological interrelationship between F1 (heptad repeat A domain or cysteine-rich region) and F2 (10,19). Undoubtedly, further investigation is needed to elucidate the possible role of F2 in the fusogenic activity.…”

mentioning

confidence: 99%

Role of a single amino acid at the amino terminus of the simian virus 5 F2 subunit in syncytium formation

Ito

Nishio

Kawano

et al. 1997

“…VOL. 66, 1992 on July 6, 2020 by guest http://jvi.asm.org/ Downloaded from F protein mutants have been isolated from other strains of NDV by their ability to escape neutralization with F-specific monoclonal antibodies (33,48,53). Interestingly, a major group of antibody escape mutants (amino acids 157 to 171) lies within the AAH described here and overlaps the amino acid 153-159 region containing the DI and D2/D3 mutations and the largest group of revertants.…”

Section: Discussionmentioning

confidence: 99%

Intracellular processing of the paramyxovirus F protein: critical role of the predicted amphipathic alpha helix adjacent to the fusion domain

Wang

Raghu

Morrison

et al. 1992

At a nonpermissive temperature, the group D temperature-sensitive mutants of Newcastle disease virus strain Australia-Victoria (AV) are defective in plaque formation, in inducing infected cells to fuse, and in incorporating the cleaved fusion glycoprotein, FI +F2, into virus particles. In this study, the F protein of AV, expressed in chicken embryo cells, was able to complement these mutants in a plaque assay, identifying the F gene as the gene containing the group D temperature-sensitive lesions. The F genes of mutants Dl, D2, and D3 were found to contain single mutations relative to the AV sequence, clustered within a predicted amphipathic alpha helix (AAH) adjacent to the hydrophobic amino terminus of F,. These mutant F proteins were * Corresponding author. t Present address: Section