Demonstration that Glycoprotein G Is the Attachment Protein of Respiratory Syncytial Virus

Levine, Seymour; Klaiber-Franco, R.; Paradiso, Peter R.

doi:10.1099/0022-1317-68-9-2521

Cited by 315 publications

(220 citation statements)

References 15 publications

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“…It has two surface glycoproteins (G and F), which are the main targets of neutralizing and protective antibodies. The G glycoprotein is responsible for virus binding to the cell surface receptor (Levine et al, 1987). The F glycoprotein mediates the fusion of the viral and cell membranes (Walsh et al, 1985), allowing the entrance of the virus nucleocapsid into the cell cytoplasm and the initiation of a new infectious cycle.…”

Section: Introductionmentioning

confidence: 99%

Antigenic structure of the human respiratory syncytial virus G glycoprotein and relevance of hypermutation events for the generation of antigenic variants.

Martı́nez

Dopazo

Melero

1997

Journal of General Virology

133

156

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A set of monoclonal antibodies (MAbs) specific for the attachment (G) glycoprotein of a recently isolated strain of human respiratory syncytial virus (HRSV) is described. Antibody reactivity with a series of HRSV isolates belonging to antigenic groups A and B identified three epitope categories : (i) strainspecific or variable epitopes that were present in a limited set of viruses from the same antigenic group, (ii) group-specific epitopes shared by viruses from the same antigenic group and (iii) conserved epitopes present in all HRSV isolates. Sequence analysis of escape mutants was used to map relevant antigenic sites of the G glycoprotein. Strain-specific epitopes were located preferentially in the variable C-terminal third of the G polypeptide, in agreement with previous studies of the Long strain. However, a

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Section: Introductionmentioning

confidence: 99%

Antigenic structure of the human respiratory syncytial virus G glycoprotein and relevance of hypermutation events for the generation of antigenic variants.

Martı́nez

Dopazo

Melero

1997

Journal of General Virology

133

156

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“…Its genome expresses 11 known proteins, among which are three transmembrane glycoproteins (the small hydrophobic protein [SH], G, and F) and the viral M protein (14,28). G is a highly glycosylated protein that is expressed as a secreted form and a membraneanchored form, with the latter serving as a viral attachment protein (34). F resembles the prototypic paramyxovirus fusion protein but can induce membrane fusion in the absence of G (26,39).…”

mentioning

confidence: 99%

The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

Mitra

Baviskar

Duncan-Decocq

et al. 2012

J Virol

110

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An experimental system was developed to generate infectious human respiratory syncytial virus (HRSV) lacking matrix (M) protein expression (M-null virus) from cDNA. The role of the M protein in virus assembly was then examined by infecting HEp-2 and Vero cells with the M-null virus and assessing the impact on infectious virus production and viral protein trafficking. In the absence of M, the production of infectious progeny was strongly impaired. Immunofluorescence (IF) microscopy analysis using antibodies against the nucleoprotein (N), attachment protein (G), and fusion protein (F) failed to detect the characteristic virusinduced cell surface filaments, which are believed to represent infectious virions. In addition, a large proportion of the N protein was detected in viral replication factories termed inclusion bodies (IBs). High-resolution analysis of the surface of M-null virusinfected cells by field emission scanning electron microscopy (SEM) revealed the presence of large areas with densely packed, uniformly short filaments. Although unusually short, these filaments were otherwise similar to those induced by an M-containing control virus, including the presence of the viral G and F proteins. The abundance of the short, stunted filaments in the absence of M indicates that M is not required for the initial stages of filament formation but plays an important role in the maturation or elongation of these structures. In addition, the absence of mature viral filaments and the simultaneous increase in the level of the N protein within IBs suggest that the M protein is involved in the transport of viral ribonucleoprotein (RNP) complexes from cytoplasmic IBs to sites of budding.

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“…HRSV is an enveloped, nonsegmented negative-strand RNA virus, classified within the Pneumovirus genus of the Paramyxoviridae family. The virion has two main surface glycoproteins in the viral membrane: the attachment (G) protein, which mediates virus binding to the cell receptor (3), and the fusion (F) protein, which is responsible for fusion of the viral and cell membranes (4). A third small hydrophobic (SH) surface glycoprotein of unknown function is expressed abundantly at the surface of infected cells, but is incorporated only in small amounts in the virus particle (5).…”

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confidence: 99%

Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion

González-Reyes

Ruiz-Argüello

Garcı́a-Barreno

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

200

175

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Preparations of purified full-length fusion (F) protein of human respiratory syncytial virus (HRSV) expressed in recombinant vaccinia-F infected cells, or of an anchorless mutant (F TM؊) lacking the C-terminal 50 amino acids secreted from vaccinia-F TM؊-infected cells contain a minor polypeptide that is an intermediate product of proteolytic processing of the F protein precursor F0. N-terminal sequencing of the intermediate demonstrated that it is generated by cleavage at a furin-motif, residues 106 -109 of the F sequence. By contrast, the F1 N terminus derives from cleavage at residue 137 of F0 which is also C-terminal to a furin recognition site at residues 131-136. Site-directed mutagenesis indicates that processing of F0 protein involves independent cleavage at both sites. Both cleavages are required for the F protein to be active in membrane fusion as judged by syncytia formation, and they allow changes in F structure from cone-to lollipop-shaped spikes and the formation of rosettes by anchorless F.

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Demonstration that Glycoprotein G Is the Attachment Protein of Respiratory Syncytial Virus

Cited by 315 publications

References 15 publications

Antigenic structure of the human respiratory syncytial virus G glycoprotein and relevance of hypermutation events for the generation of antigenic variants.

Antigenic structure of the human respiratory syncytial virus G glycoprotein and relevance of hypermutation events for the generation of antigenic variants.

The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion

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