The G glycoprotein of human respiratory syncytial viruses of subgroups A and B: extensive sequence divergence between antigenically related proteins.

Abstract

Two major antigenic subgroups (designated A and B) have been described for human respiratory syncytial virus (RSV). Previously, on the basis of reactivity patterns with monoclonal antibodies, the greatest intersubgroup variation was shown to occur in the G protein, the putative attachment glycoprotein. To delineate the molecular basis for this variation, we have determined the nucleotide and deduced amino acid sequences of the G mRNAs and proteins representing a subgroup A (Long strain) and a subgroup B (18537 strain) virus. These sequences were compared to the available G mRNA sequence for another subgroup A (A2 strain) virus. The Long G protein shared 94% amino acid identity with the A2 G protein. In contrast, the 18537 G protein shared only 53% amino acid identity with the A2 sequence; interestingly, most of the sequence divergence occurred in the proposed extracellular domain of the G protein. This extensive divergence for the G protein was significantly greater than that observed for other

Determination of the disulfide bond arrangement of human respiratory syncytial virus attachment (G) protein by matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry

“…1. Amino acid sequences encompassing residues 149-197 of the G proteins of A (Satake et al, 1985;Wertz et al, 1985) and B (Johnson et a]., 1987;Sullender et al, 1990 subtypes of human RSV, bovine RSV (Lerch et al, 1990), and ovine RSV (Alansari & Potgeiter, 1993).…”

“…It has been suggested that the conserved portion of the ectodomain may be involved in ligand interactions with a cellular receptor for the G protein (Johnson et al, 1987;Collins, 1991Collins, , 1996. However, the disulfide linkage pattern of this region of the isolated protein remains to be elucidated.…”

“…This region also has a sequence of 13 amino acids, including two of the conserved Cys residues (Fig. l), which is identical in all wild-type isolates of RSV that infect humans (Satake et al, 1985;Wertz et al, 1985;Johnson et al, 1987;Sullender et al, 1990Cane et al, 1991;Collins, 1991Collins, , 1996Garcia et al, 1994).…”

Molecular epidemiology and genetic variability of respiratory syncytial virus (RSV) in Stockholm, 2002–2003

“…The attachment (G) glycoprotein is one of the major transmembrane glycoproteins and, together with the F protein, an important antigen that stimulates the protective immune response [Sullender, 2000;Cane, 2001]. The G protein coding gene is one of the most genetically variable regions of the genome [Johnson et al, 1987;Sullender, 2000;Cane, 2001]. The G gene consists of two variable parts, the N-terminal and the C-terminal, and a central, conserved region [Johnson et al, 1987;Cane et al, 1991;Sullender et al, 1991;Sullender, 2000;Cane, 2001].…”

In vitro expression of full-length and truncated bovine respiratory syncytial virus G proteins and their antibody responses in BALB/c mice

“…Within the mucin-like ectodomain of BRSV G exists a region spanning amino acids 166-186, that was fully-conserved among nine BRSV isolates studied [6]. This conserved region contains four cysteine residues, which are disulfide-linked, forming a characteristic "cysteine noose" that may serve to stabilize the area and be critical for receptor binding [7]. Bastien et al , identified a synthetic peptide corresponding to this conserved region that was able to induce significant BRSV-specific antibodies in calves and was capable of preventing BRSV-associated pneumonia in the natural host [8].…”