scholarly journals Naked DNA immunization with full-length attachment gene of human respiratory syncytial virus induces safe and protective immune response

2018 ◽  
Vol 62 (02) ◽  
pp. 137-146 ◽  
Author(s):  
M. E. HAMAD ◽  
H. M. AMER ◽  
M. A. FARRAG ◽  
A. H. OSMAN ◽  
F. N. ALMAJHDI
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Protective Immune Response ◽  
Human Respiratory Syncytial Virus ◽  
Full Length ◽  
Dna Immunization ◽  
Naked Dna ◽  
Syncytial Virus

scholarly journals siRNA-Mediated Simultaneous Regulation of the Cellular Innate Immune Response and Human Respiratory Syncytial Virus Replication

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 165 ◽  
Author(s):  
María Martín-Vicente ◽  
Salvador Resino ◽  
Isidoro Martínez
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Virus Replication ◽  
Innate Immune Response ◽  
Human Respiratory Syncytial Virus ◽  
Innate Immune ◽  
Viral Fusion ◽  
Small Interfering Rnas ◽  
Syncytial Virus ◽  
Nucleoprotein N

Human respiratory syncytial virus (HRSV) infection is a common cause of severe lower respiratory tract diseases such as bronchiolitis and pneumonia. Both virus replication and the associated inflammatory immune response are believed to be behind these pathologies. So far, no vaccine or effective treatment is available for this viral infection. With the aim of finding new strategies to counteract HRSV replication and modulate the immune response, specific small interfering RNAs (siRNAs) were generated targeting the mRNA coding for the viral fusion (F) protein or nucleoprotein (N), or for two proteins involved in intracellular immune signaling, which are named tripartite motif-containing protein 25 (TRIM25) and retinoic acid-inducible gene-I (RIG-I). Furthermore, two additional bispecific siRNAs were designed that silenced F and TRIM25 (TRIM25/HRSV-F) or N and RIG-I (RIG-I/HRSV-N) simultaneously. All siRNAs targeting N or F, but not those silencing TRIM25 or RIG-I alone, significantly reduced viral titers. However, while siRNAs targeting F inhibited only the expression of the F mRNA and protein, the siRNAs targeting N led to a general inhibition of viral mRNA and protein expression. The N-targeting siRNAs also induced a drastic decrease in the expression of genes of the innate immune response. These results show that both virus replication and the early innate immune response can be regulated by targeting distinct viral products with siRNAs, which may be related to the different role of each protein in the life cycle of the virus.

Platelets Modulate Innate Immune Response Against Human Respiratory Syncytial Virus In Vitro

2017 ◽  
Vol 30 (8) ◽  
pp. 576-581 ◽  
Author(s):  
Vesla I. Kullaya ◽  
Quirijn de Mast ◽  
Andre van der Ven ◽  
Hicham elMoussaoui ◽  
Gibson Kibiki ◽  
...  
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Innate Immune Response ◽  
Human Respiratory Syncytial Virus ◽  
Innate Immune ◽  
Syncytial Virus

scholarly journals Sequence elements of the fusion peptide of human respiratory syncytial virus fusion protein required for activity

2006 ◽  
Vol 87 (6) ◽  
pp. 1649-1658 ◽  
Author(s):  
Diana Martín ◽  
Lesley J. Calder ◽  
Blanca García-Barreno ◽  
John J. Skehel ◽  
José A. Melero
Keyword(s):  
Respiratory Syncytial Virus ◽  
Membrane Fusion ◽  
Conformational Changes ◽  
Fusion Peptide ◽  
Human Respiratory Syncytial Virus ◽  
Full Length ◽  
Fusion Peptides ◽  
Sequence Elements ◽  
Syncytial Virus ◽  
Simple Molecules

We have reported previously the expression and purification of an anchorless form of the human respiratory syncytial virus (HRSV) F protein () representing the ectodomain of the full-length F. molecules are seen as unaggregated cones by electron microscopy but completion of proteolytic cleavage of the F0 monomers in the trimer leads to a change in shape from cones to lollipops that aggregate into rosettes. This aggregation apparently occurs by interaction of the fusion peptides of molecules that are exposed after cleavage. Since exposure of the fusion peptide is a key event in the process of membrane fusion, changes associated with cleavage may reflect those occurring in full-length F during membrane fusion. Deletions or substitutions that changed either the length, charge or hydrophobicity of the fusion peptide inhibited aggregation of , and these mutants remained as unaggregated cones after cleavage. In contrast, more conservative changes did not inhibit the change of shape and aggregation of . When the same changes were introduced in the fusion peptide of full-length F, only the mutations that inhibited aggregation of prevented membrane fusion. Thus, the conformational changes that follow completion of cleavage of the protein require a functional fusion peptide. These sequence constraints may restrict accumulation of sequence changes in the fusion peptide of HRSV F when compared with other hydrophobic regions of the molecule.

scholarly journals Complete Genome Sequence of Human Respiratory Syncytial Virus from Shanghai, China

2015 ◽  
Vol 3 (5) ◽  
Author(s):  
Xuemin Fu ◽  
Yanwei Cheng ◽  
Zhixiang He ◽  
Wei Dong ◽  
Ke Lan ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Respiratory Syncytial Virus ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Respiratory Symptoms ◽  
Human Respiratory Syncytial Virus ◽  
Full Length ◽  
Group A ◽  
Syncytial Virus

We report here the complete genome sequence of human respiratory syncytial virus isolated from an outpatient child with fever and respiratory symptoms in Shanghai, China, in 2014. Phylogenetic analysis showed that the full-length respiratory syncytial virus (RSV) genome sequence belongs to human RSV (HRSV) group A.

scholarly journals Evidence for an intranasal immune response to human respiratory syncytial virus infection in cynomolgus macaques

2015 ◽  
Vol 96 (4) ◽  
pp. 782-792 ◽  
Author(s):  
Clément Grandin ◽  
Marianne Lucas-Hourani ◽  
Marine Clavel ◽  
Fabrice Taborik ◽  
Astrid Vabret ◽  
...  
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Virus Infection ◽  
Respiratory Syncytial Virus Infection ◽  
Human Respiratory Syncytial Virus ◽  
Cynomolgus Macaques ◽  
Syncytial Virus

scholarly journals Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus

2016 ◽  
Vol 15 (6) ◽  
pp. 2141-2151 ◽  
Author(s):  
Elena Lorente ◽  
Alejandro Barriga ◽  
Eilon Barnea ◽  
Carmen Mir ◽  
John A. Gebe ◽  
...  
Keyword(s):  
Immune Response ◽  
Respiratory Syncytial Virus ◽  
Viral Proteins ◽  
Human Respiratory Syncytial Virus ◽  
T Helper ◽  
Syncytial Virus

scholarly journals Complete Genome Sequence of Human Respiratory Syncytial Virus from Lanzhou, China

2017 ◽  
Vol 5 (34) ◽  
Author(s):  
Chuanfeng Zhu ◽  
Shengfang Fu ◽  
Xv Zhou ◽  
Li Yu
Keyword(s):  
Phylogenetic Analysis ◽  
Respiratory Syncytial Virus ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Infectious Clone ◽  
Human Respiratory Syncytial Virus ◽  
Full Length ◽  
Full Length Cdna ◽  
Syncytial Virus

ABSTRACT A complete genome of human respiratory syncytial virus was sequenced and analyzed. Phylogenetic analysis showed that the full-length human respiratory syncytial virus (HRSV) genome sequence belongs to gene type NA1. We sequenced the genome in order to create the full-length cDNA infectious clone and develop vaccines against HRSV.

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