scholarly journals Human Metapneumovirus Reinfection among Children in Thailand Determined by ELISA Using Purified Soluble Fusion Protein

2008 ◽  
Vol 198 (6) ◽  
pp. 836-842 ◽  
Author(s):  
Julie A. Pavlin ◽  
Andrew C. Hickey ◽  
Nancy Ulbrandt ◽  
Yee‐Peng Chan ◽  
Timothy P. Endy ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Human Metapneumovirus ◽  
Soluble Fusion Protein

scholarly journals Characterization of Human Metapneumovirus F Protein-Promoted Membrane Fusion: Critical Roles for Proteolytic Processing and Low pH

2006 ◽  
Vol 80 (22) ◽  
pp. 10931-10941 ◽  
Author(s):  
Rachel M. Schowalter ◽  
Stacy E. Smith ◽  
Rebecca Ellis Dutch
Keyword(s):  
Fusion Protein ◽  
Cleavage Site ◽  
Low Ph ◽  
Human Metapneumovirus ◽  
Proteolytic Processing ◽  
Luciferase Reporter ◽  
Transfected Cells ◽  
F Protein ◽  
Viral Fusion Protein ◽  
Glycosylation Sites

ABSTRACT Human metapneumovirus (HMPV) is a recently described human pathogen of the pneumovirus subfamily within the paramyxovirus family. HMPV infection is prevalent worldwide and is associated with severe respiratory disease, particularly in infants. The HMPV fusion protein (F) amino acid sequence contains features characteristic of other paramyxovirus F proteins, including a putative cleavage site and potential N-linked glycosylation sites. Propagation of HMPV in cell culture requires exogenous trypsin, which cleaves the F protein, and HMPV, like several other pneumoviruses, is infectious in the absence of its attachment protein (G). However, little is known about HMPV F-promoted fusion, since the HMPV glycoproteins have yet to be analyzed separately from the virus. Using syncytium and luciferase reporter gene fusion assays, we determined the basic requirements for HMPV F protein-promoted fusion in transiently transfected cells. Our data indicate that proteolytic cleavage of the F protein is a stringent requirement for fusion and that the HMPV G protein does not significantly enhance fusion. Unexpectedly, we also found that fusion can be detected only when transfected cells are treated with trypsin and exposed to low pH, indicating that this viral fusion protein may function in a manner unique among the paramyxoviruses. We also analyzed the F protein cleavage site and three potential N-linked glycosylation sites by mutagenesis. Mutations in the cleavage site designed to facilitate endogenous cleavage did so with low efficiency, and our data suggest that all three N-glycosylation sites are utilized and that each affects cleavage and fusion to various degrees.

Prophylactic and therapeutic benefits of a monoclonal antibody against the fusion protein of human metapneumovirus in a mouse model

2010 ◽  
Vol 88 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Marie-Eve Hamelin ◽  
Constance Gagnon ◽  
Gregory A. Prince ◽  
Peter Kiener ◽  
JoAnn Suzich ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mouse Model ◽  
Fusion Protein ◽  
Human Metapneumovirus ◽  
Therapeutic Benefits

Aggregation kinetics in the presence of brain lipids of Aβ(1–40) cleaved from a soluble fusion protein

2018 ◽  
Vol 1860 (9) ◽  
pp. 1681-1686 ◽  
Author(s):  
Miriam A. Kael ◽  
Daniel K. Weber ◽  
Frances Separovic ◽  
Marc-Antoine Sani
Keyword(s):  
Fusion Protein ◽  
Aggregation Kinetics ◽  
Brain Lipids ◽  
Soluble Fusion Protein

scholarly journals Effect of sialidase fusion protein (DAS 181) on human metapneumovirus infection of Hep-2 cells

2015 ◽  
Vol 24 (5-6) ◽  
pp. 161-165 ◽  
Author(s):  
Sutthiwan Thammawat ◽  
Tania A Sadlon ◽  
Penelope Adamson ◽  
David L Gordon
Keyword(s):  
Fusion Protein ◽  
Human Metapneumovirus

scholarly journals Immunoinformatics Approach for Designing Multiple Epitope-Based Vaccine against Human Metapneumovirus Utilizing its Fusion Protein.

2020 ◽  
Author(s):  
Ibtihal A Ahmed ◽  
Mosab Y Alnour ◽  
Nafisa M Eisa ◽  
Esameldeen A Adam ◽  
Faiza A Omer ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Respiratory Infections ◽  
3D Structure ◽  
Experimental Studies ◽  
Docking Study ◽  
Human Metapneumovirus ◽  
Web Servers ◽  
Molecular Docking Study ◽  
Mhc I ◽  
Mhc Ii

Abstract BackgroundHuman Metapneumovirus is a major cause of acute respiratory infections especially in children besides it’s responsible for substantial hospitalizations associated with significant morbidity and treatment cost. Hence vaccination is required. Consequently, we aim to predict effective, safe, and universal epitope-based peptides vaccine against the HMPV using its Fusion Protein via the Immunoinformatics approach since there are no licensed vaccines or antiviral treatments yet.To achieve this goal, various Immunoinformatics databases and web servers, including, the Immune Epitope Database used the Allergen FP v.1.0, and ToxinPred web servers as well as Phyre2 web portal for the modeling of peptide 3D structure and molecular docking study on Cresset Flare software.Result According to the results, the peptide GSTVYYPN was the best predicted B-cells epitopes. Moreover, the peptide VIYMVQLPI with population coverage 48.27% in class(C) I, 35.12% in (C)II, and the peptides LIGVYGSSV with 44.03% in C II, YTNVFTLEV with 61.92% in class I were the best-predicted T-cells epitopes that will interact effectively with the MHC I and MHC II molecules respectively.Conclusions We recommend the use of them, the highest coverage, and the best -combined allele’s bindings of immunogenic multiple peptide vaccines. Also, experimental studies recommend validating the results.

scholarly journals Identification and Evaluation of a Highly Effective Fusion Inhibitor for Human Metapneumovirus

2007 ◽  
Vol 52 (1) ◽  
pp. 279-287 ◽  
Author(s):  
Céline Deffrasnes ◽  
Marie-Ève Hamelin ◽  
Gregory A. Prince ◽  
Guy Boivin
Keyword(s):  
Fusion Protein ◽  
Clinical Symptoms ◽  
Pulmonary Inflammation ◽  
Human Metapneumovirus ◽  
Heptad Repeat ◽  
Elderly Subjects ◽  
Monocyte Chemoattractant Protein 1 ◽  
Syncytial Virus ◽  
Tract Infections

ABSTRACT Human metapneumovirus (hMPV) can cause acute upper and lower respiratory tract infections that are particularly severe in young children, elderly subjects, and immunocompromised patients. To date, no treatments or vaccines are available for hMPV infections. Our objective was to assess the inhibitory potential of several peptides derived from the heptad repeat A and B (HRA and HRB) domains of the hMPV fusion protein. Nine candidate peptides were expressed in Escherichia coli or obtained synthetically and tested in vitro and in an animal model. Excellent in vitro inhibition of an hMPV strain of the A1 subgroup was obtained with five peptides, with 50% inhibitory concentrations ranging from 1.4 nM to 3.3 μM. One peptide, HRA2, displayed very potent activity against all four hMPV subgroups. It was also moderately active against human respiratory syncytial virus (strain A2) but displayed no activity against human parainfluenza virus type 3. BALB/c mice that received the HRA2 peptide and a lethal hMPV intranasal challenge simultaneously were completely protected from clinical symptoms and mortality. On day 5 postinfection, HRA2-treated mice had undetectable lung viral loads which were significantly less than those of untreated mice (3 × 104 50% tissue culture infective doses/lung). Pulmonary inflammation, levels of proinflammatory cytokines/chemokines (RANTES, gamma interferon, and monocyte chemoattractant protein 1) and airway obstruction were also significantly decreased in HRA2-treated mice. The results of this study demonstrate that potent antivirals can be derived from the hMPV fusion protein HR domains. Moreover, hMPV, compared to other paramyxoviruses and to the human immunodeficiency virus, seems to be more susceptible to HRA- than HRB-derived peptides.

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