Partial protection to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides
François CanoHélène Plotnicky‐GilquinThien Ngoc NguyenSissela LiljeqvistPatrik SamuelsonJean‐Yves BonnefoyStefan StåhlAlain Robert
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Keywords:
Mononegavirales
Metapneumovirus
Pneumovirinae
Mononegavirales
Pneumovirus
Morbillivirus
Human Parainfluenza Virus
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Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNApolymerase (L) binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P.We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N̊-P-L) during replication, followed by the delivery of N monomers to the nascent genomic RNA chain.
Nucleoprotein
Mononegavirales
Morbillivirus
Phosphoprotein
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Canine distemper
Morbillivirus
Mononegavirales
Rinderpest virus
Hendra Virus
Pneumovirinae
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Mononegavirales
RNA virus
Canine distemper
Hendra Virus
Sendai virus
Mumps virus
Phosphoprotein
VP40
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As a delivery system for nasal immunization vaccines, biodegradable microspheres have several advantages such as extending immunization time and enhancing immune response. The recent advances in the entrapment materials and microsphere preparation methods are reviewed. The progress in research on microsphere distribution after intranasal administration, the immunization mechanisms and DNA nasal immunization microspheres are also described.
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Peste-des-petits-ruminants virus
Morbillivirus
Canine distemper
Mononegavirales
Newcastle Disease
Sendai virus
Pneumovirinae
Pneumovirus
Veterinary virology
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Nucleoprotein
Mononegavirales
Phosphoprotein
Morbillivirus
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Measles virus (MV) and canine distemper virus (CDV) are morbilliviruses that cause acute illnesses and several persistent central nervous system infections in humans and in dogs, respectively. Characteristically, the cytopathic effect of these viruses is the formation of syncytia in permissive cells. In this study, a vaccinia virus expression system was used to express MV and CDV hemagglutinin (HA) and fusion (F) envelope proteins. We found that cotransfecting F and HA genes of MV or F and HA genes of CDV resulted in extensive syncytium formation in permissive cells while transfecting either F or HA alone did not. Similar experiments with heterologous pairs of proteins, CDV-F with MV-HA or MV-F with CDV-HA, caused significant cell fusion in both cases. These results indicate that in this expression system, cell fusion requires both F and HA; however, the functions of these proteins are interchangeable between the two types of morbilliviruses. Human-mouse somatic hybrids were used to determine the human chromosome conferring susceptibility to either MV and CDV. Of the 12 hybrids screened, none were sensitive to MV. Two of the hybrids containing human chromosome 19 formed syncytia following CDV infection. In addition, these two hybrids underwent cell fusion when cotransfected with CDV-F and CDV-HA (but not MV-F and MV-HA) glycoproteins by using the vaccinia virus expression system. To discover the viral component responsible for cell specificity, complementation experiments coexpressing CDV-HA with MV-F or CDV-F with MV-HA in the CDV-sensitive hybrids were performed. We found that syncytia were formed only in the presence of CDV-HA. These results support the idea that the HA protein is responsible for cell tropism. Furthermore, while the F protein is necessary for the fusion process, it is interchangeable with the F protein from other morbilliviruses.
Canine distemper
Syncytium
Mononegavirales
Morbillivirus
Cell fusion
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Newcastle disease virus (NDV) is an enveloped paramyxovirus. The matrix protein of the virus (M-NDV) has an innate propensity to produce virus-like particles budding from the plasma membrane of the expressing cell without recruiting other viral proteins. The virus predominantly infects the host cell via fusion with the host plasma membrane or, alternatively, can use receptor-mediated endocytic pathways. The question arises as to what are the mechanisms supporting such diversity, especially concerning the assembling and membrane binding properties of the virus protein scaffold under both neutral and acidic pH conditions. Here, we suggest a novel method of M-NDV isolation in physiological ionic strength and employ a combination of small-angle X-ray scattering, atomic force microscopy with complementary structural techniques, and membrane interaction measurements to characterize the solution behavior/structure of the protein as well as its binding to lipid membranes at pH 4.0 and pH 7.0. We demonstrate that the minimal structural unit of the protein in solution is a dimer that spontaneously assembles in a neutral milieu into hollow helical oligomers by repeating the protein tetramers. Acidic pH conditions decrease the protein oligomerization state to the individual dimers, tetramers, and octamers without changing the density of the protein layer and lipid membrane affinity, thus indicating that the endocytic pathway is a possible facilitator of NDV entry into a host cell through enhanced scaffold disintegration.
VP40
Mononegavirales
Newcastle Disease
Pneumovirinae
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