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Relevant bibliographies by topics / Morbillivirus - Proteins

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Academic literature on the topic 'Morbillivirus - Proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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Journal articles on the topic "Morbillivirus - Proteins"

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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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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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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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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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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7

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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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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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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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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Dissertations / Theses on the topic "Morbillivirus - Proteins"

1

Collins, Fergal M. "Investigation of the morbillivirus large protein by reverse genetics." Thesis, Queen's University Belfast, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326404.

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Zhang, Xinsheng. "Structural and functional interactions between measles virus nucleocapsid protein and cellular heat shock protein." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1078417800.

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Thesis (Ph. D.)--Ohio State University, 2004.<br>Title from first page of PDF file. Document formatted into pages; contains xv, 155 p.; also includes graphics (some col.) Includes bibliographical references (p. 147-155). Available online via OhioLINK's ETD Center

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Mahapatra, Madhuchhanda. "Application of reverse genetics to study the role of the matrix (M) protein in morbillivirus replication : chimeric viruses as potential marker vaccines." Thesis, Royal Veterinary College (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.407453.

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Vidya, Harini V. "Structural Studies Of Functional Domains Of Morbillivirus Proteins And Designed Peptides Folding Into Helices And β-Hairpins". Thesis, 2005. https://etd.iisc.ac.in/handle/2005/2390.

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Vidya, Harini V. "Structural Studies Of Functional Domains Of Morbillivirus Proteins And Designed Peptides Folding Into Helices And β-Hairpins". Thesis, 2005. http://etd.iisc.ernet.in/handle/2005/2390.

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Singh, Piyush Kumar. "Identification of the Minimal Domain of RNA Trihosphastase Activity in the L Protien of Rinderpest Virus and Charecterization of its Enzymatic Activities." Thesis, 2013. http://etd.iisc.ac.in/handle/2005/3328.

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Morbilliviruses belong to the family Paramyxoviridae of the Mononegavirale order of viruses. The Mononegavirale order contains viruses which contain negatively-polar, non-segmented and single stranded RNA genomes. This order contains some of most lethal pathogens known to the humankind. Ebola virus and Marburg virus are perhaps the most lethal human pathogens. Rinderpest virus, declared eradicated in 2011, was known to be the most significant cattle killer. Similarly the Canine distemper virus and Rabies virus, two topmost canine pathogens belong to this order. The L protein in the viruses of

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Singh, Piyush Kumar. "Identification of the Minimal Domain of RNA Trihosphastase Activity in the L Protien of Rinderpest Virus and Charecterization of its Enzymatic Activities." Thesis, 2013. http://etd.iisc.ernet.in/2005/3328.

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Abstract:

Morbilliviruses belong to the family Paramyxoviridae of the Mononegavirale order of viruses. The Mononegavirale order contains viruses which contain negatively-polar, non-segmented and single stranded RNA genomes. This order contains some of most lethal pathogens known to the humankind. Ebola virus and Marburg virus are perhaps the most lethal human pathogens. Rinderpest virus, declared eradicated in 2011, was known to be the most significant cattle killer. Similarly the Canine distemper virus and Rabies virus, two topmost canine pathogens belong to this order. The L protein in the viruses of

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