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. 2000 Nov;74(22):10714-28.
doi: 10.1128/jvi.74.22.10714-10728.2000.

Evolution of bovine respiratory syncytial virus

J F Valarcher  1 , F Schelcher, H Bourhy
Affiliations

Evolution of bovine respiratory syncytial virus

J F Valarcher et al. J Virol. 2000 Nov.

Abstract

Until now, the analysis of the genetic diversity of bovine respiratory syncytial virus (BRSV) has been based on small numbers of field isolates. In this report, we determined the nucleotide and deduced amino acid sequences of regions of the nucleoprotein (N protein), fusion protein (F protein), and glycoprotein (G protein) of 54 European and North American isolates and compared them with the sequences of 33 isolates of BRSV obtained from the databases, together with those of 2 human respiratory syncytial viruses and 1 ovine respiratory syncytial virus. A clustering of BRSV sequences according to geographical origin was observed. We also set out to show that a continuous evolution of the sequences of the N, G, and F proteins of BRSV has been occurring in isolates since 1967 in countries where vaccination was widely used. The exertion of a strong positive selective pressure on the mucin-like region of the G protein and on particular sites of the N and F proteins is also demonstrated. Furthermore, mutations which are located in the conserved central hydrophobic part of the ectodomain of the G protein and which result in the loss of four Cys residues and in the suppression of two disulfide bridges and an alpha helix critical to the three-dimensional structure of the G protein have been detected in some recent French BRSV isolates. This conserved central region, which is immunodominant in BRSV G protein, thus has been modified in recent isolates. This work demonstrates that the evolution of BRSV should be taken into account in the rational development of future vaccines.

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Figures

FIG. 1
FIG. 1
ML phylogenetic tree showing the relationships among the G protein genes of 87 BRSV isolates, 1 ovine RSV (ORSV) isolate, and 2 human RSV isolates (18537 and hrsvA2). Horizontal branches are drawn to scale, and the tree is rooted with isolate hrsvA2. Designations at the ends of the branches refer to the identifying code of the isolate (Table 1).
FIG. 2
FIG. 2
ML phylogenetic tree showing the relationships among the N protein genes of 58 BRSV isolates, 1 ovine RSV (ORSV) isolate, and two human RSV isolates (18537 and hrsvA2). Horizontal branches are drawn to scale, and the tree is rooted with isolate hrsvA2. Designations at the ends of the branches refer to the identifying code of the isolate (Table 1).
FIG. 3
FIG. 3
ML phylogenetic tree showing the relationships among the F protein genes of 56 BRSV isolates and 2 human RSV isolates (18537 and hrsvA2). Horizontal branches are drawn to scale, and the tree is rooted with isolate hrsvA2. Designations at the ends of the branches refer to the identifying code of the isolate (Table 1).
FIG. 4
FIG. 4
Sequences of amino acids 53 to 215 of the G protein of BRSV isolates. Designations to the left of the sequences indicate the isolate code (Table 1). Subgroup designations are shown to the left of the isolate designations.
FIG. 4
FIG. 4
Sequences of amino acids 53 to 215 of the G protein of BRSV isolates. Designations to the left of the sequences indicate the isolate code (Table 1). Subgroup designations are shown to the left of the isolate designations.
FIG. 4
FIG. 4
Sequences of amino acids 53 to 215 of the G protein of BRSV isolates. Designations to the left of the sequences indicate the isolate code (Table 1). Subgroup designations are shown to the left of the isolate designations.
FIG. 5
FIG. 5
Consensus sequence of BRSV subgroups from residues 170 to 209. Horizontal arrows indicate linear epitopes from the study of Langedijk et al. (33). Vertical arrows indicate mutations determining antigen subgrouping (33). Boxes indicate α helices.
FIG. 6
FIG. 6
Representation of the superimposition of the cysteine noose of BRSV strain 391.2 (left) and of the consensus sequence of isolates from subgroup VI (right). α Helices are indicated in blue and red. Disulfide bridges are drawn in yellow. Residues 171 to 189 in the representation of strain 391.2 correspond to residues 1 to 19 in that of subgroup VI.
FIG. 7
FIG. 7
Genetic changes in the G protein gene according to codon number. ds (diamonds) and the dn/ds ratio (squares) are represented along the G protein length from codons 53 to 215, with a window of 20.
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