Further characterization of the soluble form of the G glycoprotein of respiratory syncytial virus

Hendricks, David A.; Mclntosh, Kenneth

doi:10.1016/0168-1702(88)90125-6

Cited by 41 publications

(53 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The 48K to 60K species was not detected in virions (Fig. 8b) or in the medium overlying infected cells under conditions where the previously described (Hendricks et al, 1988) 82K secreted form without an anchor was readily detected (not shown).…”

Section: P L Collins and G Mottetmentioning

confidence: 92%

“…2) comigrated with the 48K and 50K intracellular species respectively (lanes 7 and 8), suggesting that the intracellular species differed by a single N-linked side-chain. The observation that the 48K and 50K forms were each reactive with a n t i -G -N T serum (lane 7) ruled out the alternative possibilities that internal translational initiation or the endoproteolytic cleavage described by Hendricks et al (1988) could account for the two forms. Also, the idea that the difference between these species was due solely to Nglycans was supported by the observations that endo H treatment reduced the two species to a single unglycosy- …”

Section: Comparison Of G Protein Synthesized In Vitro and Intracellulmentioning

confidence: 99%

“…The intracellular compartment(s) and steps involved in O-glycosylation remained to be defined. Approximately one in six molecules of intracellular G protein is cleaved co-or post-translationally at amino acid sequence position 65 or 74 by a signalase-like activity, which releases the ectodomain from the membrane anchor and generates a secreted form (Hendricks et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A

Collins

Mottet²

1992

Journal of General Virology

105

View full text Add to dashboard Cite

Section: P L Collins and G Mottetmentioning

confidence: 92%

Section: Comparison Of G Protein Synthesized In Vitro and Intracellulmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A

Collins

Mottet²

1992

Journal of General Virology

105

View full text Add to dashboard Cite

“…The latter is composed of the extracellular domain of the G protein and is shed within hours after infection in vitro (6). Although modified RSV strains lacking G protein are still infectious in vitro, infection in vivo is highly attenuated, underscoring the importance of the G protein (7,8).…”

mentioning

confidence: 99%

Broadly Reactive Anti-Respiratory Syncytial Virus G Antibodies from Exposed Individuals Effectively Inhibit Infection of Primary Airway Epithelial Cells

Cortjens

Yasuda

et al. 2017

J Virol

View full text Add to dashboard Cite

Respiratory syncytial virus (RSV) causes severe respiratory disease in young children. Antibodies specific for the RSV prefusion F protein have guided RSV vaccine research, and in human serum, these antibodies contribute to Ͼ90% of the neutralization response; however, detailed insight into the composition of the human B cell repertoire against RSV is still largely unknown. In order to study the B cell repertoire of three healthy donors for specificity against RSV, CD27 ϩ memory B cells were isolated and immortalized using BCL6 and Bcl-xL. Of the circulating memory B cells, 0.35% recognized RSV-A2-infected cells, of which 59% were IgAexpressing cells and 41% were IgG-expressing cells. When we generated monoclonal B cells selected for high binding to RSV-infected cells, 44.5% of IgGexpressing B cells and 56% of IgA-expressing B cells reacted to the F protein, while, unexpectedly, 41.5% of IgG-expressing B cells and 44% of IgA expressing B cells reacted to the G protein. Analysis of the G-specific antibodies revealed that 4 different domains on the G protein were recognized. These epitopes predicted cross-reactivity between RSV strain A (RSV-A) and RSV-B and matched the potency of antibodies to neutralize RSV in HEp-2 cells and in primary epithelial cell cultures. G-specific antibodies were also able to induce antibody-dependent cellular cytotoxicity and antibody-dependent cellular phagocytosis of RSV-A2-infected cells. However, these processes did not seem to depend on a specific epitope. In conclusion, healthy adults harbor a diverse repertoire of RSV glycoprotein-specific antibodies with a broad range of effector functions that likely play an important role in antiviral immunity.IMPORTANCE Human RSV remains the most common cause of severe lower respiratory tract disease in premature babies, young infants, the elderly, and immunocompromised patients and plays an important role in asthma exacerbations. In developing countries, RSV lower respiratory tract disease has a high mortality. Without an effective vaccine, only passive immunization with palivizumab is approved for prophylactic treatment. However, highly potent RSV-specific monoclonal antibodies could potentially serve as a therapeutic treatment and contribute to disease control and mortality reduction. In addition, these antibodies could guide further vaccine development. In this study, we isolated and characterized several novel antibodies directed at the RSV G protein. This information can add to our understanding and treatment of RSV disease.

show abstract

“…G2 may have a lesser degree of O-linked glycosylation than G1. The RS virus G protein exists in two forms but the smaller form is soluble (Hendricks et al, 1988) whereas G1 and G2 of PVM are virion proteins (Cash et al, 1979).…”

Section: Fl-related Polypeptides Identified Under Non-reducing Conditmentioning

confidence: 99%

Polypeptides of Pneumonia Virus of Mice. II. Characterization of the Glycoproteins

Ling

Pringle

1989

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYThe kinetics of synthcsis and the naturc of the oligosaccharidcs of the glycoprotcins of pneumonia virus of mice (PVM) wcrc studied. Tryptic pcptidc mapping showed that the two major glycosylatcd polypcptidcs G 1 and G2 wcrc different forms of the samc protein, G2 was dcrivcd from GI which in turn appeared to bc dcrivcd from an unidentificd precursor. The G I/G2 protein of PVM is probably a hacmagglutinin since a monoclonal antibody directed against it has a high hacmagglutination inhibition titrc. On the basis of experiments with inhibitors and glycosidases it was dcduccd that G I and G2 havc both N-linkcd and O-linkcd oligosaccharides. Thc putative fusion protcin-cquivalent of PVM was shown to posscss N-linked oligosaccharidcs. In thc presence of tunicamycin a high mobility form (Fit) appcarcd to bc dcrivcd from a prccursor (F0t) with the samc mobility as the fully glycosylatcd protein. If by analogy with other paramyxoviruscs this rcprcscnts a clcavagc event, thc difference in mobility of the prccursor and product suggcsts that thc putative F2 product is smaller than thc corresponding F2 protein of other paramyxoviruscs. Howcvcr, no F2 candidate protein was detected and cvidcncc for an F 1,2 dimcr was inconclusive. The glycoproteins of PVM fcscmblc thosc of respiratory syncytial virus in terms of thcir pattern of glycosylation, but differ in their processing. INTRODUCTION Pneumonia virus of mice (PVM) is classified along with the human and bovine respiratory syncytial (RS) viruses and turkey rhinotracheitis (TRT) virus in the genusPneumovirus of the family Paramvxoviridae. The accompanying paper (Ling & Pringle, 1989) describes the polypeptides identified in PVM-infected cells. The kinetics of synthesis and nature of the oligosaccharides of RS virus glycoproteins have been described in some detail by various authors (e.g. Fernie et al., 1985; Gruber & Levine, 1985a, b). This paper describes the characterization of the oligosaccharides of the corresponding glycoproteins of PVM using tunicamycin to inhibit N-linked glycosylation and glycosidases to remove specifically N-linked and O-linked oligosaccharides. The analysis of glycoprotein processing by pulse-chase experiments in combination with immunoprecipitation by an antiglycoprotein (anti-G) monoclonal antibody (MAb) or polyclonal anti-PVM serum in the presence or absence of tunicamycin is also described.

show abstract

Further characterization of the soluble form of the G glycoprotein of respiratory syncytial virus

Cited by 41 publications

References 1 publication

Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A

Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A

Broadly Reactive Anti-Respiratory Syncytial Virus G Antibodies from Exposed Individuals Effectively Inhibit Infection of Primary Airway Epithelial Cells

Polypeptides of Pneumonia Virus of Mice. II. Characterization of the Glycoproteins

Contact Info

Product

Resources

About