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Journal articles on the topic 'Morbillivirus - Proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Bodjo, S. C., O. Kwiatek, A. Diallo, E. Albina, and G. Libeau. "Mapping and structural analysis of B-cell epitopes on the morbillivirus nucleoprotein amino terminus." Journal of General Virology 88, no. 4 (2007): 1231–42. http://dx.doi.org/10.1099/vir.0.82424-0.

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By analysing the antigenic structure of the morbillivirus nucleoprotein (N) using a competitive-binding assay of monoclonal antibodies (mAbs), six different antigenic sites were identified previously. By using Pepscan methodology complemented by analysis of truncated N proteins, a better characterization of five of these antigenic sites was provided: I, II, III, IV and VI. mAbs specific to Rinderpest virus, defining antigenic sites II, III and IV, and those common to four morbilliviruses, delineating sites I and VI, were analysed in the present study. It was found that all but one mapped to th

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2

Wang, Lin-Fa, Wojtek P. Michalski, Meng Yu, et al. "A Novel P/V/C Gene in a New Member of theParamyxoviridae Family, Which Causes Lethal Infection in Humans, Horses, and Other Animals." Journal of Virology 72, no. 2 (1998): 1482–90. http://dx.doi.org/10.1128/jvi.72.2.1482-1490.1998.

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ABSTRACT In 1994, a new member of the family Paramyxoviridaeisolated from fatal cases of respiratory disease in horses and humans was shown to be distantly related to morbilliviruses and provisionally called equine morbillivirus (K. Murray et al., Science 268:94–97, 1995). To facilitate characterization and classification, the virus was purified, viral proteins were identified, and the P/V/C gene was cloned and sequenced. The coding strategy of the gene is similar to that of Sendai and measles viruses, members of the Paramyxovirusand Morbillivirus genera, respectively, in the subfamilyParamyxo

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3

Fukuhara, Hideo, Yuri Ito, Miyuki Sako, et al. "Specificity of Morbillivirus Hemagglutinins to Recognize SLAM of Different Species." Viruses 11, no. 8 (2019): 761. http://dx.doi.org/10.3390/v11080761.

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Measles virus (MV) and canine distemper virus (CDV) are highly contagious and deadly, forming part of the morbillivirus genus. The receptor recognition by morbillivirus hemagglutinin (H) is important for determining tissue tropism and host range. Recent reports largely urge caution as regards to the potential expansion of host specificities of morbilliviruses. Nonetheless, the receptor-binding potential in different species of morbillivirus H proteins is largely unknown. Herein, we show that the CDV-H protein binds to the dog signaling lymphocyte activation molecule (SLAM), but not to the huma

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4

Diallo, A. "Morbillivirus group: genome organisation and proteins." Veterinary Microbiology 23, no. 1-4 (1990): 155–63. http://dx.doi.org/10.1016/0378-1135(90)90145-l.

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5

Kelly, James T., Stacey Human, Joseph Alderman, et al. "BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell–Cell Fusion." Viruses 11, no. 8 (2019): 692. http://dx.doi.org/10.3390/v11080692.

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The measles virus (MeV), a member of the genus Morbillivirus, is an established pathogen of humans. A key feature of morbilliviruses is their ability to spread by virus–cell and cell–cell fusion. The latter process, which leads to syncytia formation in vitro and in vivo, is driven by the viral fusion (F) and haemagglutinin (H) glycoproteins. In this study, we demonstrate that MeV glycoproteins are sensitive to inhibition by bone marrow stromal antigen 2 (BST2/Tetherin/CD317) proteins. BST2 overexpression causes a large reduction in MeV syncytia expansion. Using quantitative cell–cell fusion as

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6

von Messling, Veronika, and Roberto Cattaneo. "N-Linked Glycans with Similar Location in the Fusion Protein Head Modulate Paramyxovirus Fusion." Journal of Virology 77, no. 19 (2003): 10202–12. http://dx.doi.org/10.1128/jvi.77.19.10202-10212.2003.

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ABSTRACT N-linked glycans not only orchestrate the folding and intracellular transport of viral glycoproteins but also modulate their function. We have characterized the three glycans attached to fusion (F) proteins of the morbilliviruses canine distemper virus and measles virus. The individual Morbillivirus glycans have similar functional properties: the glycan at position 68 is essential for protein transport, and those at positions 36 and 75 modulate fusion (numbering according to the Newcastle disease virus [NDV] F protein sequence). Based on the crystal structure of the NDV F protein, we

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Kumar, Naveen, Sanjay Barua, Riyesh Thachamvally, and Bhupendra Nath Tripathi. "Systems Perspective of Morbillivirus Replication." Journal of Molecular Microbiology and Biotechnology 26, no. 6 (2016): 389–400. http://dx.doi.org/10.1159/000448842.

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Systems biology refers to system-wide changes in biological components such as RNA/DNA (genomics), protein (proteomics) and lipids (lipidomics). In this review, we provide comprehensive information about morbillivirus replication. Besides discussing the role of individual viral/host proteins in virus replication, we also discuss how systems-level analyses could improve our understanding of morbillivirus replication, host-pathogen interaction, immune response and disease resistance. Finally, we discuss how viroinformatics is likely to provide important insights for understanding genome-genome,

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8

Shrestha, Neeta, Flavio M. Gall, Jonathan Vesin, et al. "Antiviral Screen against Canine Distemper Virus-Induced Membrane Fusion Activity." Viruses 13, no. 1 (2021): 128. http://dx.doi.org/10.3390/v13010128.

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Canine distemper virus (CDV), a close relative of the human pathogen measles virus (MeV), is an enveloped, negative sense RNA virus that belongs to the genus Morbillivirus and causes severe diseases in dogs and other carnivores. Although the vaccination is available as a preventive measure against the disease, the occasional vaccination failure highlights the importance of therapeutic alternatives such as antivirals against CDV. The morbilliviral cell entry system relies on two interacting envelope glycoproteins: the attachment (H) and fusion (F) proteins. Here, to potentially discover novel e

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9

Geeraedts, Felix, Nadine Wilczak, Rob van Binnendijk, and Jacques De Keyser. "Search for morbillivirus proteins in multiple sclerosis brain tissue." NeuroReport 15, no. 1 (2004): 27–32. http://dx.doi.org/10.1097/00001756-200401190-00007.

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10

Heaney, J., T. Barrett, and S. L. Cosby. "Inhibition of In Vitro Leukocyte Proliferation by Morbilliviruses." Journal of Virology 76, no. 7 (2002): 3579–84. http://dx.doi.org/10.1128/jvi.76.7.3579-3584.2002.

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ABSTRACT Immune suppression associated with morbillivirus infections may influence the mortality rate by allowing secondary bacterial infections that are lethal to the host to flourish. Using an in vitro proliferation assay, we have shown that all members of the genus Morbillivirus inhibit the proliferation of a human B-lymphoblast cell line (BJAB). Proliferation of freshly isolated, stimulated bovine and caprine peripheral blood lymphocytes is also inhibited by UV-inactivated rinderpest (RPV) and peste-des-petits ruminants viruses. As for measles virus, coexpression of both the fusion and the

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11

Brindley, Melinda A., Sukanya Chaudhury, and Richard K. Plemper. "Measles Virus Glycoprotein Complexes Preassemble Intracellularly and Relax during Transport to the Cell Surface in Preparation for Fusion." Journal of Virology 89, no. 2 (2014): 1230–41. http://dx.doi.org/10.1128/jvi.02754-14.

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ABSTRACTMeasles virus (MeV), a morbillivirus within the paramyxovirus family, expresses two envelope glycoproteins. The attachment (H) protein mediates receptor binding, followed by triggering of the fusion (F) protein, which leads to merger of the viral envelope with target cell membranes. Receptor binding by members of related paramyxovirus genera rearranges the head domains of the attachment proteins, liberating an F-contact domain within the attachment protein helical stalk. However, morbillivirus glycoproteins first assemble intracellularly prior to receptor binding, raising the question

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12

Cox, Robert M., Julien Sourimant, Mugunthan Govindarajan, Michael G. Natchus, and Richard K. Plemper. "Therapeutic targeting of measles virus polymerase with ERDRP-0519 suppresses all RNA synthesis activity." PLOS Pathogens 17, no. 2 (2021): e1009371. http://dx.doi.org/10.1371/journal.ppat.1009371.

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Morbilliviruses, such as measles virus (MeV) and canine distemper virus (CDV), are highly infectious members of the paramyxovirus family. MeV is responsible for major morbidity and mortality in non-vaccinated populations. ERDRP-0519, a pan-morbillivirus small molecule inhibitor for the treatment of measles, targets the morbillivirus RNA-dependent RNA-polymerase (RdRP) complex and displayed unparalleled oral efficacy against lethal infection of ferrets with CDV, an established surrogate model for human measles. Resistance profiling identified the L subunit of the RdRP, which harbors all enzymat

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13

Muñoz-Alía, Miguel Angel, and Stephen J. Russell. "Probing Morbillivirus Antisera Neutralization Using Functional Chimerism between Measles Virus and Canine Distemper Virus Envelope Glycoproteins." Viruses 11, no. 8 (2019): 688. http://dx.doi.org/10.3390/v11080688.

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Measles virus (MeV) is monotypic. Live virus challenge provokes a broadly protective humoral immune response that neutralizes all known measles genotypes. The two surface glycoproteins, H and F, mediate virus attachment and entry, respectively, and neutralizing antibodies to H are considered the main correlate of protection. Herein, we made improvements to the MeV reverse genetics system and generated a panel of recombinant MeVs in which the globular head domain or stalk region of the H glycoprotein or the entire F protein, or both, were substituted with the corresponding protein domains from

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14

Duprex, W. Paul, Fergal M. Collins, and Bert K. Rima. "Modulating the Function of the Measles Virus RNA-Dependent RNA Polymerase by Insertion of Green Fluorescent Protein into the Open Reading Frame." Journal of Virology 76, no. 14 (2002): 7322–28. http://dx.doi.org/10.1128/jvi.76.14.7322-7328.2002.

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ABSTRACT Measles virus (MV) is the type species of the Morbillivirus genus and its RNA-dependent RNA polymerase complex is comprised of two viral polypeptides, the large (L) and the phospho- (P) proteins. Sequence alignments of morbillivirus L polymerases have demonstrated the existence of three well-conserved domains (D1, D2, and D3) which are linked by two variable hinges (H1 and H2). Epitope tags (c-Myc) were introduced into H1 and H2 to investigate the tolerance of the variable regions to insertions and to probe the flexibility of the proposed domain structures to spatial reorientation. In

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15

Baron, Michael D., and Thomas Barrett. "Rinderpest Viruses Lacking the C and V Proteins Show Specific Defects in Growth and Transcription of Viral RNAs." Journal of Virology 74, no. 6 (2000): 2603–11. http://dx.doi.org/10.1128/jvi.74.6.2603-2611.2000.

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ABSTRACT Rinderpest virus is a morbillivirus and the causative agent of an important disease of cattle and wild bovids. The P genes of all morbilliviruses give rise to two proteins in addition to the P protein itself: use of an alternate start translation site, in a second open reading frame, gives rise to the C protein, while cotranscriptional insertion of an extra base gives rise to the V protein, a fusion of the amino-terminal half of P to a short, highly conserved, cysteine-rich zinc binding domain. Little is known about the function of either of these two proteins in the rinderpest virus

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16

Baron, Jana, and Michael Baron. "Creation of a completely helper cell-dependent recombinant morbillivirus." Journal of General Virology 94, no. 6 (2013): 1195–99. http://dx.doi.org/10.1099/vir.0.050872-0.

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We have created a completely helper cell-dependent morbillivirus by modifying the genome to remove the coding sequence of the phosphoprotein (P) and recovering the recombinant virus in a cell line constitutively expressing the P protein. The P protein-deleted virus (P−) grew very inefficiently unless both of the viral accessory proteins (V and C) were also expressed. Growth of the virus was restricted to the P-expressing cell line. The P− virus grew more slowly than the parental virus and expressed much less viral protein in infected cells. The technique could be used to create virus-like part

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17

Bonami, François, Penny A. Rudd, and Veronika von Messling. "Disease Duration Determines Canine Distemper Virus Neurovirulence." Journal of Virology 81, no. 21 (2007): 12066–70. http://dx.doi.org/10.1128/jvi.00818-07.

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ABSTRACT The Morbillivirus hemagglutinin (H) protein mediates attachment to the target cell. To evaluate its contribution to canine distemper virus neurovirulence, we exchanged the H proteins of the wild-type strains 5804P and A75 and assessed the pathogenesis of the chimeric viruses in ferrets. Both strains are lethal to ferrets; however, 5804P causes a 2-week disease without neurological signs, whereas A75 is associated with a longer disease course and neurological involvement. We observed that both H proteins supported neuroinvasion and the subsequent development of clinical neurological si

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18

Servan de Almeida, Renata, Djénéba Keita, Geneviève Libeau, and Emmanuel Albina. "Control of ruminant morbillivirus replication by small interfering RNA." Journal of General Virology 88, no. 8 (2007): 2307–11. http://dx.doi.org/10.1099/vir.0.82981-0.

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Peste-des-petits-ruminants virus (PPRV) and rinderpest virus (RPV) are two morbilliviruses of economic relevance in African and Asian countries. Although efficient vaccines are available for both diseases, they cannot protect the animals before 14 days post-vaccination. In emergencies, it would be desirable to have efficient therapeutics for virus control. Here, two regions are described in the nucleocapsid genes of PPRV and RPV that can be targeted efficiently by synthetic short interfering RNAs (siRNAs), resulting in a >80 % reduction in virus replication. The effects of siRNAs on the pro

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19

Massé, Nicolas, Michelle Ainouze, Benjamin Néel, T. Fabian Wild, Robin Buckland, and Johannes P. M. Langedijk. "Measles Virus (MV) Hemagglutinin: Evidence that Attachment Sites for MV Receptors SLAM and CD46 Overlap on the Globular Head." Journal of Virology 78, no. 17 (2004): 9051–63. http://dx.doi.org/10.1128/jvi.78.17.9051-9063.2004.

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ABSTRACT Measles virus hemagglutinin (MVH) residues potentially responsible for attachment to the wild-type (wt) MV receptor SLAM (CD150) have been identified and localized on the MVH globular head by reference to a revised hypothetical structural model for MVH (www.pepscan.nl/downloads/measlesH.pdb ). We show that the mutation of five charged MVH residues which are conserved among morbillivirus H proteins has major effects on both SLAM downregulation and SLAM-dependent fusion. In the three-dimensional surface representation of the structural model, three of these residues (D505, D507, and R53

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20

Trudel, Michel, Francine Nadon, Cécile Séguin, Simone Ghoubril, Pierre Payment, and Pierre Trépanier. "Immunovirological studies on human respiratory syncytial virus structural proteins." Canadian Journal of Microbiology 32, no. 1 (1986): 15–21. http://dx.doi.org/10.1139/m86-004.

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Immunovirological studies suggest that human respiratory syncytial virus may well be composed of five structural proteins as are other members of the Paramyxoviridae family: the two external membrane glycoproteins H (90 000) and Fo (F1, 49 000; F2, 20 000; disulfide linked), the internal membrane protein M (34 000), the nucleoprotein N (42 000), and a protein (78 000) designated P that could be the equivalent of the polymerase of the morbillivirus and paramyxovirus genus. Neutralizing monoclonal antibodies showed, by immunoprecipitation and immunoblotting, that the fusion protein carries neutr

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von Messling, Veronika, Nicholas Svitek, and Roberto Cattaneo. "Receptor (SLAM [CD150]) Recognition and the V Protein Sustain Swift Lymphocyte-Based Invasion of Mucosal Tissue and Lymphatic Organs by a Morbillivirus." Journal of Virology 80, no. 12 (2006): 6084–92. http://dx.doi.org/10.1128/jvi.00357-06.

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ABSTRACT Experimental infections of ferrets with canine distemper virus (CDV) recapitulate many hallmarks of measles: rash, high fever, viremia, depression of delayed-type hypersensitivity responses, lowered leukocyte counts, and reduced lymphocyte proliferation activity. To understand how a morbillivirus invades the host and causes immunosuppression, we generated CDV either unable to recognize one of the receptors or incapable of expressing either one or both of the candidate interferon antagonist proteins V and C. Variants of these viruses expressing green fluorescent protein were also gener

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22

Yanagi, Yusuke, Makoto Takeda, and Shinji Ohno. "Measles virus: cellular receptors, tropism and pathogenesis." Journal of General Virology 87, no. 10 (2006): 2767–79. http://dx.doi.org/10.1099/vir.0.82221-0.

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Measles virus (MV), a member of the genus Morbillivirus in the family Paramyxoviridae, is an enveloped virus with a non-segmented, negative-strand RNA genome. It has two envelope glycoproteins, the haemagglutinin (H) and fusion proteins, which are responsible for attachment and membrane fusion, respectively. Human signalling lymphocyte activation molecule (SLAM; also called CD150), a membrane glycoprotein of the immunoglobulin superfamily, acts as a cellular receptor for MV. SLAM is expressed on immature thymocytes, activated lymphocytes, macrophages and dendritic cells and regulates productio

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Brown, D. D., F. M. Collins, W. P. Duprex, M. D. Baron, T. Barrett, and B. K. Rima. "‘Rescue’ of mini-genomic constructs and viruses by combinations of morbillivirus N, P and L proteins." Journal of General Virology 86, no. 4 (2005): 1077–81. http://dx.doi.org/10.1099/vir.0.80804-0.

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Chloramphenicol acetyltransferase (CAT)-expressing negative-sense mini-genomic constructs of measles virus (MV) and rinderpest virus (RPV) were rescued by standard technology with helper plasmids expressing the nucleocapsid (N), phospho- (P) and large (L) proteins of MV, canine distemper virus (CDV) or RPV in order to determine whether the proteins of different viruses can function together. Homogeneous sets consisting of N, P and L plasmids derived from one virus were able to generate reporter gene expression from either mini-genomic construct. Heterogeneous sets of proteins from different vi

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24

Wang, L. F., A. R. Gould, and P. W. Selleck. "Expression of equine morbillivirus (EMV) matrix and fusion proteins and their evaluation as diagnostic reagents." Archives of Virology 142, no. 11 (1997): 2269–79. http://dx.doi.org/10.1007/s007050050241.

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Crisi, Paolo Emidio, Francesco Dondi, Eliana De Luca, et al. "Early Renal Involvement in Cats with Natural Feline Morbillivirus Infection." Animals 10, no. 5 (2020): 828. http://dx.doi.org/10.3390/ani10050828.

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Feline morbillivirus (FeMV) is a newly discovered paramyxovirus infecting domestic cats and its role in the pathogenesis of feline chronic kidney disease (CKD) has been suggested, however not confirmed. The primary aim of the study was to evaluate the renal damage associated with FeMV infection in cats. In this retrospective study, clinical and clinicopathological data were compared among 14 FeMV naturally infected, 21 CKD and 22 healthy cats. FeMV positive cats had serum chemistry analytes and main urine chemistry results similar to the healthy subjects. FeMV positive cats had significantly d

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Chinnakannan, Senthil K., Sambit K. Nanda, and Michael D. Baron. "Morbillivirus V Proteins Exhibit Multiple Mechanisms to Block Type 1 and Type 2 Interferon Signalling Pathways." PLoS ONE 8, no. 2 (2013): e57063. http://dx.doi.org/10.1371/journal.pone.0057063.

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Viscone, Érica Almeida, Lígia Assunção Oliveira, Alexandra Ariadine Bittencourt Gonçalves Pereira, et al. "4-hydroxy-2-nonenal as a marker of the oxidative stress in brains of dogs with canine distemper." Brazilian Journal of Veterinary Research and Animal Science 59 (May 26, 2022): e188941. http://dx.doi.org/10.11606/issn.1678-4456.bjvras.2022.188941.

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Canine Distemper is a disease caused by Canine morbillivirus (CM), a pantropic virus that can affect the central nervous system (CNS), causing demyelination. However, the pathogenesis of this lesion remains to be clarified. Brain samples of 14 naturally infected dogs by CM were analyzed to evaluate the presence of oxidative stress and demyelination. RT-PCR assay was performed to confirm a diagnosis of canine distemper in the brain, immunohistochemistry anti-CM was used to localize the viral proteins in the tissue, and anti-4-hydroxy-2 nonenal (4-HNE) was a marker of a product of lipid peroxida

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Langedijk, J. P., F. J. Daus, and J. T. van Oirschot. "Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin." Journal of virology 71, no. 8 (1997): 6155–67. http://dx.doi.org/10.1128/jvi.71.8.6155-6167.1997.

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Sawatsky, Bevan, and Veronika von Messling. "Canine Distemper Viruses Expressing a Hemagglutinin without N-Glycans Lose Virulence but Retain Immunosuppression." Journal of Virology 84, no. 6 (2009): 2753–61. http://dx.doi.org/10.1128/jvi.01813-09.

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ABSTRACT Paramyxovirus glycoproteins are posttranslationally modified by the addition of N-linked glycans, which are often necessary for correct folding, processing, and cell surface expression. To establish the contribution of N glycosylation to morbillivirus attachment (H) protein function and overall virulence, we first determined the use of the potential N-glycosylation sites in the canine distemper virus (CDV) H proteins. Biochemical characterization revealed that the three sites conserved in all strains were N glycosylated, whereas only two of the up to five additional sites present in w

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Kovamees, J., M. Blixenkrone-Moller, B. Sharma, C. Orvell, and E. Norrby. "The Nucleotide Sequence and Deduced Amino Acid Composition of the Haemagglutinin and Fusion Proteins of the Morbillivirus Phocid Distemper Virus." Journal of General Virology 72, no. 12 (1991): 2959–66. http://dx.doi.org/10.1099/0022-1317-72-12-2959.

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Curran, M. D., Y. J. L�, and B. K. Rima. "The fusion protein gene of phocine distemper virus: nucleotide and deduced amino acid sequences and a comparison of morbillivirus fusion proteins." Archives of Virology 126, no. 1-4 (1992): 159–69. http://dx.doi.org/10.1007/bf01309692.

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Gaafar, Bothina B. M., Sumaia A. Ali, Khoubieb Ali Abd-elrahman, and Yassir A. Almofti. "Immunoinformatics Approach for Multiepitope Vaccine Prediction from H, M, F, and N Proteins of Peste des Petits Ruminants Virus." Journal of Immunology Research 2019 (October 30, 2019): 1–18. http://dx.doi.org/10.1155/2019/6124030.

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Background. Small ruminant morbillivirus or peste des petits ruminants virus (PPRV) is an acute and highly contagious viral disease of goats, sheep, and other livestock. This study aimed at predicting an effective multiepitope vaccine against PPRV from the immunogenic proteins haemagglutinin (H), matrix (M), fusion (F), and nucleoprotein (N) using immunoinformatics tools. Materials and Methods. The sequences of the immunogenic proteins were retrieved from GenBank of the National Center for Biotechnology Information (NCBI). BioEdit software was used to align each protein from the retrieved sequ

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Gassen, Uta, Fergal M. Collins, W. Paul Duprex, and Bert K. Rima. "Establishment of a Rescue System for Canine Distemper Virus." Journal of Virology 74, no. 22 (2000): 10737–44. http://dx.doi.org/10.1128/jvi.74.22.10737-10744.2000.

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ABSTRACT Canine distemper virus (CDV) has been rescued from a full-length cDNA clone. Besides Measles virus (MV) andRinderpest virus, a third morbillivirus is now available for genetic analysis using reverse genetics. A plasmid p(+)CDV was constructed by sequential cloning using the Onderstepoort vaccine strain large-plaque-forming variant. The presence of a T7 promoter allowed transcription of full-length antigenomic RNA by a T7 RNA polymerase, which was provided by a host range mutant of vaccinia virus (MVA-T7). Plasmids expressing the nucleocapsid protein, the phosphoprotein, and the viral

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Singethan, K., E. Topfstedt, S. Schubert, W. P. Duprex, B. K. Rima, and Jürgen Schneider-Schaulies. "CD9-dependent regulation of Canine distemper virus-induced cell–cell fusion segregates with the extracellular domain of the haemagglutinin." Journal of General Virology 87, no. 6 (2006): 1635–42. http://dx.doi.org/10.1099/vir.0.81629-0.

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Antibodies to CD9, a member of the tetraspan transmembrane-protein family, selectively inhibit Canine distemper virus (CDV)-induced cell–cell fusion. Neither CDV-induced virus–cell fusion nor cell–cell fusion induced by the closely related morbillivirus Measles virus (MV) is affected by anti-CD9 antibodies. As CDV does not bind CD9, an unknown, indirect mechanism is responsible for the observed inhibition of cell–cell fusion. It was investigated whether this effect was restricted to only one viral glycoprotein, either the haemagglutinin (H) or the fusion (F) protein, which form a fusion comple

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Nwalozie, Rhoda, Michael Uzoechi, RoseMary Kaiso Esiere, and Brenda Anyakwe Nnokam. "Biology of Measles Virus: Epidemiology and Clinical Manifestations." International Journal of Pathogen Research 12, no. 4 (2023): 1–10. http://dx.doi.org/10.9734/ijpr/2023/v12i4231.

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Measles virus is a highly infectious RNA virus belonging to the genus Morbillivirus in the family Paramyxoviridae. It causes measles, a respiratory disease that is one of the leading causes of childhood mortality worldwide. The virus has a pleomorphic structure and a genome consisting of a single strand of negative-sense RNA. The genome encodes six structural proteins, including the nucleocapsid (N), phosphoprotein (P), matrix (M), fusion (F), hemagglutinin (H), and the large polymerase (L) proteins. Measles virus enters host cells through the interaction of the viral H protein with cellular r

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Rennick, Linda J., W. Paul Duprex, and Bert K. Rima. "Measles virus minigenomes encoding two autofluorescent proteins reveal cell-to-cell variation in reporter expression dependent on viral sequences between the transcription units." Journal of General Virology 88, no. 10 (2007): 2710–18. http://dx.doi.org/10.1099/vir.0.83106-0.

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Transcription from morbillivirus genomes commences at a single promoter in the 3′ non-coding terminus, with the six genes being transcribed sequentially. The 3′ and 5′ untranslated regions (UTRs) of the genes (mRNA sense), together with the intergenic trinucleotide spacer, comprise the non-coding sequences (NCS) of the virus and contain the conserved gene end and gene start signals, respectively. Bicistronic minigenomes containing transcription units (TUs) encoding autofluorescent reporter proteins separated by measles virus (MV) NCS were used to give a direct estimation of gene expression in

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Ramachandran, Aparna, Jean-Patrick Parisien, and Curt M. Horvath. "STAT2 Is a Primary Target for Measles Virus V Protein-Mediated Alpha/Beta Interferon Signaling Inhibition." Journal of Virology 82, no. 17 (2008): 8330–38. http://dx.doi.org/10.1128/jvi.00831-08.

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ABSTRACT Measles virus, a member of the Morbillivirus family, infects millions of people each year despite the availability of effective vaccines. The V protein of measles virus is an important virulence factor that can interfere with host innate immunity by inactivating alpha/beta interferon (IFN-α/β) and IFN-γ signaling through protein interactions with signal transducer and activator of transcription proteins STAT1 and STAT2. Here we demonstrate that although STAT1 interference results from protein interactions within a V protein N-terminal region encompassed by amino acids 110 to 130, dete

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Bhella, David, Adam Ralph, Lindsay B. Murphy, and Robert P. Yeo. "Significant differences in nucleocapsid morphology within the Paramyxoviridae." Journal of General Virology 83, no. 8 (2002): 1831–39. http://dx.doi.org/10.1099/0022-1317-83-8-1831.

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Nucleocapsid (N) proteins from representative viruses of three genera within the Paramyxoviridae were expressed in insect cells using recombinant baculoviruses. RNA-containing structures, which appear morphologically identical to viral nucleocapsids, were isolated and subsequently imaged under a transmission electron microscope. Analysis of these images revealed marked differences in nucleocapsid morphology among the genera investigated, most notably between viruses of the Paramyxovirinae and the Pneumovirinae subfamilies. Helical pitch measurements were made, revealing that measles virus (MV,

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Takeda, Makoto, Shinji Ohno, Fumio Seki, Yuichiro Nakatsu, Maino Tahara, and Yusuke Yanagi. "Long Untranslated Regions of the Measles Virus M and F Genes Control Virus Replication and Cytopathogenicity." Journal of Virology 79, no. 22 (2005): 14346–54. http://dx.doi.org/10.1128/jvi.79.22.14346-14354.2005.

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ABSTRACT Measles is still a major cause of mortality mainly in developing countries. The causative agent, measles virus (MeV), is an enveloped virus having a nonsegmented negative-sense RNA genome, and belongs to the genus Morbillivirus of the family Paramyxoviridae. One feature of the moribillivirus genomes is that the M and F genes have long untranslated regions (UTRs). The M and F mRNAs of MeV have 426-nucleotide-long 3′ and 583-nucleotide-long 5′ UTRs, respectively. Though these long UTRs occupy as much as ∼6.4% of the virus genome, their function remains unknown. To elucidate the role of

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von Messling, Veronika, Christoph Springfeld, Patricia Devaux, and Roberto Cattaneo. "A Ferret Model of Canine Distemper Virus Virulence and Immunosuppression." Journal of Virology 77, no. 23 (2003): 12579–91. http://dx.doi.org/10.1128/jvi.77.23.12579-12591.2003.

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ABSTRACT Canine distemper virus (CDV) infects many carnivores, including ferrets and dogs, and is the member of the Morbillivirus genus most easily amenable to experimentation in a homologous small-animal system. To gain insights into the determinants of CDV pathogenesis, we isolated a strain highly virulent for ferrets by repeated passaging in these animals. Sequence comparison of the genome of this strain with that of its highly attenuated precursor revealed 19 mutations distributed almost evenly in the six genes. We then recovered a virus from a cDNA copy of the virulent CDV strain's consen

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Thakkar, Vidhi D., Robert M. Cox, Bevan Sawatsky, et al. "The Unstructured Paramyxovirus Nucleocapsid Protein Tail Domain Modulates Viral Pathogenesis through Regulation of Transcriptase Activity." Journal of Virology 92, no. 8 (2018): e02064-17. http://dx.doi.org/10.1128/jvi.02064-17.

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ABSTRACTThe paramyxovirus replication machinery comprises the viral large (L) protein and phosphoprotein (P-protein) in addition to the nucleocapsid (N) protein, which encapsidates the single-stranded RNA genome. Common to paramyxovirus N proteins is a C-terminal tail (Ntail). The mechanistic role and relevance for virus replication of the structurally disordered central Ntail section are unknown. Focusing initially on members of theMorbillivirusgenus, a series of measles virus (MeV) and canine distemper virus (CDV) N proteins were generated with internal deletions in the unstructured tail sec

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Selvaraj, Muneeswaran, Mana Mahapatra, and Satya Parida. "Exchange of C-Terminal Variable Sequences within Morbillivirus Nucleocapsid Protein Are Tolerated: Development and Evaluation of Two Marker (DIVA) Vaccines (Sungri/96 DIVA, Nigeria/75/1 DIVA) against PPR." Viruses 13, no. 11 (2021): 2320. http://dx.doi.org/10.3390/v13112320.

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Across Africa, the Middle East, and Asia, peste des petits ruminants virus (PPRV) places a huge disease burden on agriculture, affecting, in particular, small ruminant production. The recent PPR outbreaks in Northern Africa, the European part of Turkey, and Bulgaria represent a significant threat to mainland Europe, as a source of disease. Although two safe and efficacious live attenuated vaccines (Sungri/96 and Nigeria/75/1) are available for the control of PPR, current serological tests do not enable the differentiation between naturally infected and vaccinated animals (DIVA). The vaccinated

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Brown, Brent, Tanya Gravier, Ingo Fricke, et al. "Immunopathogenesis of Nipah Virus Infection and Associated Immune Responses." Immuno 3, no. 2 (2023): 160–81. http://dx.doi.org/10.3390/immuno3020011.

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Pandemics in the last two centuries have been initiated by causal pathogens that include Severe Acute Coronavirus 2 (SARS-CoV-2) and Influenza (e.g., the H1N1 pandemic of 2009). The latter is considered to have initiated two prior pandemics in 1918 and 1977, known as the “Spanish Flu” and “Russian Flu”, respectively. Here, we discuss other emerging infections that could be potential public health threats. These include Henipaviruses, which are members of the family Paramyxoviridae that infect bats and other mammals. Paramyxoviridae also include Parainfluenza and Mumps viruses (Rubulavirus) but

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Navaratnarajah, Chanakha K., Quincy Rosemarie, and Roberto Cattaneo. "A Structurally Unresolved Head Segment of Defined Length Favors Proper Measles Virus Hemagglutinin Tetramerization and Efficient Membrane Fusion Triggering." Journal of Virology 90, no. 1 (2015): 68–75. http://dx.doi.org/10.1128/jvi.02253-15.

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ABSTRACTParamyxoviruses include several insidious and ubiquitous pathogens of humans and animals, with measles virus (MeV) being a prominent one. The MeV membrane fusion apparatus consists of a receptor binding protein (hemagglutinin [H]) tetramer and a fusion (F) protein trimer. Four globular MeV H heads are connected to a tetrameric stalk through flexible linkers. We sought here to characterize the function of a 17-residue H-head segment proximal to the stalk that was unresolved in all five MeV H-head crystal or cocrystal structures. In particular, we assessed whether its primary sequence an

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Saikia, Paramananda, and M. S. Shaila. "Identification of functional domains of phosphoproteins of two morbilliviruses using chimeric proteins." Virus Genes 37, no. 1 (2008): 1–8. http://dx.doi.org/10.1007/s11262-008-0231-3.

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Tatsuo, Hironobu, Nobuyuki Ono, and Yusuke Yanagi. "Morbilliviruses Use Signaling Lymphocyte Activation Molecules (CD150) as Cellular Receptors." Journal of Virology 75, no. 13 (2001): 5842–50. http://dx.doi.org/10.1128/jvi.75.13.5842-5850.2001.

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ABSTRACT Morbilliviruses comprise measles virus, canine distemper virus, rinderpest virus, and several other viruses that cause devastating human and animal diseases accompanied by severe immunosuppression and lymphopenia. Recently, we have shown that human signaling lymphocyte activation molecule (SLAM) is a cellular receptor for measles virus. In this study, we examined whether canine distemper and rinderpest viruses also use canine and bovine SLAMs, respectively, as cellular receptors. The Onderstepoort vaccine strain and two B95a (marmoset B cell line)-isolated strains of canine distemper

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Yamamoto, Yuta, Shogo Nakano, Fumio Seki, et al. "Computational Analysis Reveals a Critical Point Mutation in the N-Terminal Region of the Signaling Lymphocytic Activation Molecule Responsible for the Cross-Species Infection with Canine Distemper Virus." Molecules 26, no. 5 (2021): 1262. http://dx.doi.org/10.3390/molecules26051262.

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Infection of hosts by morbilliviruses is facilitated by the interaction between viral hemagglutinin (H-protein) and the signaling lymphocytic activation molecule (SLAM). Recently, the functional importance of the n-terminal region of human SLAM as a measles virus receptor was demonstrated. However, the functional roles of this region in the infection process by other morbilliviruses and host range determination remain unknown, partly because this region is highly flexible, which has hampered accurate structure determination of this region by X-ray crystallography. In this study, we analyzed th

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Chinnakannan, Senthil K., Barbara Holzer, Beatriz Sanz Bernardo, Sambit K. Nanda, and Michael D. Baron. "Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling." Journal of General Virology 95, no. 1 (2014): 44–51. http://dx.doi.org/10.1099/vir.0.056739-0.

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The V proteins of paramyxoviruses are composed of two evolutionarily distinct domains, the N-terminal 75 % being common to the viral P, V and W proteins, and not highly conserved between viruses, whilst the remaining 25 % consists of a cysteine-rich V-specific domain, which is conserved across almost all paramyxoviruses. There is evidence supporting a number of different functions of the V proteins of morbilliviruses in blocking the signalling pathways of type I and II IFNs, but it is not clear which domains of V are responsible for which activities and whether all these activities are require

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Parida, Satya, Madhuchhanda Mahapatra, Sai Kumar, et al. "Rescue of a chimeric rinderpest virus with the nucleocapsid protein derived from peste-des-petits-ruminants virus: use as a marker vaccine." Journal of General Virology 88, no. 7 (2007): 2019–27. http://dx.doi.org/10.1099/vir.0.82913-0.

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The nucleocapsid (N) protein of all morbilliviruses has a highly conserved central region that is thought to interact with and encapsidate the viral RNA. The C-terminal third of the N protein is highly variable among morbilliviruses and is thought to be located on the outer surface and to be available to interact with other viral proteins such as the phosphoprotein, the polymerase protein and the matrix protein. Using reverse genetics, a chimeric rinderpest virus (RPV)/peste-des-petits-ruminants virus (PPRV) was rescued in which the RPV N gene open reading frame had been replaced with that of

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Karlin, David, Sonia Longhi, Véronique Receveur, and Bruno Canard. "The N-Terminal Domain of the Phosphoprotein of Morbilliviruses Belongs to the Natively Unfolded Class of Proteins." Virology 296, no. 2 (2002): 251–62. http://dx.doi.org/10.1006/viro.2001.1296.

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