Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of newcastle disease virus

Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: amino acid substitutions affecting folding, transport and cleavage

“…Although the length and composition of the cleavage activation site of paramyxovirus F glycoproteins are important factors governing the ability of the F protein to be cleaved and virus pathogenicity (Glickman et al, 1987;Paterson et al, 1989;Toyoda et al, 1987), our results indicate that changes in other regions of the protein may result in altered or aberrant fusion activities. Changes in amino residues 301 or 447 of the RSV F protein, which are located proximal to a cysteine-rich region of the FI subunit, could affect protein folding mechanics by inhibiting proper intramolecular disulphide bonding and thus preventing the formation of stable F protein oligomers.…”

“…Cleavage of F glycoprotein into F1 and F 2 subunits by a cellular trypsin-like protease is essential for generating the fusion activity of the protein (Scheid & Choppin, 1977). In addition, the length and composition of amino acids at the cleavage activation site, a stretch of hydrophilic residues that precede the N-terminal hydrophobic residues of the FI subunit, are important factors that influence the ability of paramyxovirus F proteins to be cleaved (Glickman et al, 1987;Paterson et aL, 1989;Toyoda et al, 1987). A strict correlation has been demonstrated between the ability of F proteins of 0001-0700 © 1992 SGM different strains of Newcastle disease virus to be cleaved and the extent of virus pathogenicity (Nagai et al, 1976(Nagai et al, , 1979.…”

Isolation of a Recent Korean Epizootic Strain of Newcastle Disease Virus from Eurasian Scops Owls Affected with Severe Diarrhea

“…The provisional designations, including genotypes, are indicated on the right. the amino-acid sequence 112 R-R-Q-K-R-F 117 , which is a motif characteristic of virulent NDV strains (Toyoda et al, 1987;Collins et al, 1993;Nagai, 1993;Yang et al, 1999;Seal, 2004) as shown in Figure 1. These sequence results support the biologic properties of the isolate presented here with regard to virulence.…”

A serological survey of rinderpest antibody in wildlife and sheep and goats in Northern Tanzania

“…2) radius of some 30 kilometres these two populations can be considered to be distinct as far as transmission of infection is concerned. The system of ageing that we have used predicts the animals to be younger than that of Sinclair [6] [8].…”