scholarly journals Structural Characterization and Binding Studies of the Ectodomain G Protein of Respiratory Syncytial Virus Reveal the Crucial Role of pH with Possible Implications in Host–Pathogen Interactions

ACS Omega ◽  
2021 ◽  
Author(s):  
Abu Hamza ◽  
Zoya Shafat ◽  
Zahoor Ahmad Parray ◽  
Malik Hisamuddin ◽  
Wajihul Hasan Khan ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
G Protein ◽  
Structural Characterization ◽  
Crucial Role ◽  
Binding Studies ◽  
Host Pathogen Interactions ◽  
Host Pathogen ◽  
Syncytial Virus

scholarly journals Biophysical and flavonoid-binding studies of the G protein ectodomain of group A human respiratory syncytial virus

Heliyon ◽  
2019 ◽  
Vol 5 (3) ◽  
pp. e01394
Author(s):  
Vitor Brassolatti Machado ◽  
Jéssica Maróstica de Sá ◽  
Ana Karla Miranda Prado ◽  
Karina Alves de Toledo ◽  
Luis Octávio Regasini ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
G Protein ◽  
Human Respiratory Syncytial Virus ◽  
Binding Studies ◽  
Group A ◽  
Syncytial Virus

scholarly journals Multiplex Assay for Detection of Strain-Specific Antibodies against the Two Variable Regions of the G Protein of Respiratory Syncytial Virus

2002 ◽  
Vol 9 (3) ◽  
pp. 633-638 ◽  
Author(s):  
Les P. Jones ◽  
Hao-Qiang Zheng ◽  
Ruth A. Karron ◽  
Teresa C. T. Peret ◽  
Cecelia Tsou ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
G Protein ◽  
Fluorescent Dyes ◽  
Strain Differences ◽  
Variable Region ◽  
Internal Variable ◽  
Variable Regions ◽  
Syncytial Virus ◽  
Covalently Linked

ABSTRACT The role of strain differences in respiratory syncytial virus (RSV) disease has not been clearly defined. To investigate the possibility that strain differences contribute to susceptibility to repeat infections, we developed assays to detect antibodies to the two variable regions of the RSV G protein by cloning and expressing the internal variable region at amino acids (aa) 60 to 172 (g1) and the carboxy-terminal variable region at aa 193 to the carboxy terminus (g2) from different genotypes of RSV. The purified proteins were covalently linked to beads with different proportions of red and orange fluorescent dyes and reacted against serum specimens. Antibody reacting against the differently colored beads, and thus against different G polypeptides, was detected by use of flow cytometry and the Luminex system. This assay system detected group- and, to some extent, genotype-specific responses to RSV infection and can be used to investigate the role of strain differences in RSV disease.

scholarly journals Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

Molecules ◽  
2021 ◽  
Vol 26 (23) ◽  
pp. 7398
Author(s):  
Abu Hamza ◽  
Abdus Samad ◽  
Md. Ali Imam ◽  
Md. Imam Faizan ◽  
Anwar Ahmed ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Cell Membrane ◽  
Heparan Sulfate ◽  
Host Cell ◽  
G Protein ◽  
Transition Curve ◽  
Host Cell Membrane ◽  
State Process ◽  
Host Pathogen ◽  
Syncytial Virus

The global burden of disease caused by a respiratory syncytial virus (RSV) is becoming more widely recognized in young children and adults. Heparan sulfate helps in attaching the virion through G protein with the host cell membrane. In this study, we examined the structural changes of ectodomain G protein (edG) in a wide pH range. The absorbance results revealed that protein maintains its tertiary structure at physiological and highly acidic and alkaline pH. However, visible aggregation of protein was observed in mild acidic pH. The intrinsic fluorescence study shows no significant change in the λmax except at pH 12.0. The ANS fluorescence of edG at pH 2.0 and 3.0 forms an acid-induced molten globule-like state. The denaturation transition curve monitored by fluorescence spectroscopy revealed that urea and GdmCl induced denaturation native (N) ↔ denatured (D) state follows a two-state process. The fluorescence quenching, molecular docking, and 50 ns simulation measurements suggested that heparan sulfate showed excellent binding affinity to edG. Our binding study provides a preliminary insight into the interaction of edG to the host cell membrane via heparan sulfate. This binding can be inhibited using experimental approaches at the molecular level leading to the prevention of effective host–pathogen interaction.

scholarly journals Positive Selection Results in Frequent Reversible Amino Acid Replacements in the G Protein Gene of Human Respiratory Syncytial Virus

2009 ◽  
Vol 5 (1) ◽  
pp. e1000254 ◽  
Author(s):  
Viviane F. Botosso ◽  
Paolo M. de A. Zanotto ◽  
Mirthes Ueda ◽  
Eurico Arruda ◽  
Alfredo E. Gilio ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Amino Acid ◽  
Positive Selection ◽  
G Protein ◽  
Protein Gene ◽  
Human Respiratory Syncytial Virus ◽  
Syncytial Virus

RESPIRATORY SYNCYTIAL VIRUS LUNG INFECTION IN INFANTS: IMMUNOREGULATORY ROLE OF INFECTED ALVEOLAR MACROPHAGES

PEDIATRICS ◽  
1995 ◽  
Vol 96 (2) ◽  
pp. 391-391
Author(s):  
Leon S. Greos
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Lung Injury ◽  
Alveolar Macrophages ◽  
Lung Infection ◽  
Local Immune Response ◽  
Rsv Infection ◽  
Syncytial Virus

Alveolar macrophages are infected by RSV in vivo and coexpress potent immunomodulatory molecules that potentially regulate local immune response or lung injury caused by RSV infection.

scholarly journals Epitope mapping of human respiratory syncytial virus 22K transcription antitermination factor: role of N-terminal sequences in protein folding

2005 ◽  
Vol 86 (4) ◽  
pp. 1103-1107 ◽  
Author(s):  
Blanca García-Barreno ◽  
John Steel ◽  
Monica Payá ◽  
Luis Martínez-Sobrido ◽  
Teresa Delgado ◽  
...  
Keyword(s):  
Protein Folding ◽  
Respiratory Syncytial Virus ◽  
Western Blotting ◽  
Epitope Mapping ◽  
Human Respiratory Syncytial Virus ◽  
N Terminus ◽  
Transcription Antitermination ◽  
Syncytial Virus ◽  
Antibody Epitopes

The reactivity of a panel of 12 monoclonal antibodies raised against the human respiratory syncytial virus 22 kDa (22K) protein was tested by Western blotting with a set of 22K deletion mutants. The results obtained identified sequences in the C-terminal half of the 22K polypeptide required for integrity of most antibody epitopes, except for epitope 112, which was lost in mutants with short N-terminal deletions. This antibody, in contrast to the others, failed to immunoprecipitate the native 22K protein, indicating that the N terminus of this protein is buried in the native molecule and exposed only under the denaturing conditions of Western blotting. In addition, N-terminal deletions that abolished reactivity with monoclonal antibody 112 also inhibited phosphorylation of the 22K protein previously identified at Ser-58 and Ser-61, suggesting that the N terminus is important in regulating the 22K protein phosphorylation status, most likely as a result of its requirement for protein folding.

scholarly journals Role of p53/NF-κB functional balance in respiratory syncytial virus-induced inflammation response

2018 ◽  
Vol 99 (4) ◽  
pp. 489-500 ◽  
Author(s):  
Daniela Machado ◽  
Andrés Pizzorno ◽  
Jonathan Hoffmann ◽  
Aurélien Traversier ◽  
Hubert Endtz ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Inflammation Response ◽  
Functional Balance ◽  
Syncytial Virus
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