scholarly journals Nucleotide sequence of the genes encoding the matrix protein of two wild-type measles virus strains

1991 ◽  
Vol 72 (9) ◽  
pp. 2279-2282 ◽  
Author(s):  
K. Baczko ◽  
U. Brinckmann ◽  
I. Pardowitz ◽  
B. K. Rima ◽  
V. ter Meulen
Keyword(s):  
Nucleotide Sequence ◽  
Measles Virus ◽  
Matrix Protein ◽  
Wild Type ◽  
The Matrix ◽  
Genes Encoding ◽  
Virus Strains

scholarly journals Complete Genome Sequences of Six Measles Virus Strains

2018 ◽  
Vol 6 (13) ◽  
Author(s):  
My V. T. Phan ◽  
Claudia M. E. Schapendonk ◽  
Bas B. Oude Munnink ◽  
Marion P. G. Koopmans ◽  
Rik L. de Swart ◽  
...  
Keyword(s):  
Next Generation Sequencing ◽  
Complete Genome ◽  
Measles Virus ◽  
Genetic Characterization ◽  
Critical Component ◽  
Wild Type ◽  
Genome Sequences ◽  
Virus Strains ◽  
Generation Sequencing

ABSTRACT Genetic characterization of wild-type measles virus (MV) strains is a critical component of measles surveillance and molecular epidemiology. We have obtained complete genome sequences of six MV strains belonging to different genotypes, using random-primed next generation sequencing.

Adaptation of wild-type measles virus to cotton rat lung cells: E89K mutation in matrix protein contributes to its fitness

Virus Genes ◽  
2009 ◽  
Vol 39 (3) ◽  
pp. 330-334 ◽  
Author(s):  
Jian-bao Dong ◽  
Akatsuki Saito ◽  
Yuta Mine ◽  
Yuta Sakuraba ◽  
Kazumi Nibe ◽  
...  
Keyword(s):  
Measles Virus ◽  
Matrix Protein ◽  
Lung Cells ◽  
Rat Lung ◽  
Wild Type ◽  
Cotton Rat

scholarly journals PPEY Motif within the Rabies Virus (RV) Matrix Protein Is Essential for Efficient Virion Release and RV Pathogenicity

2008 ◽  
Vol 82 (19) ◽  
pp. 9730-9738 ◽  
Author(s):  
Christoph Wirblich ◽  
Gene S. Tan ◽  
Amy Papaneri ◽  
Peter J. Godlewski ◽  
Jan Marc Orenstein ◽  
...  
Keyword(s):  
Viral Replication ◽  
Rabies Virus ◽  
Rna Synthesis ◽  
Matrix Protein ◽  
Virus Production ◽  
Wild Type Virus ◽  
Wild Type ◽  
Conserved Sequence ◽  
Virion Release ◽  
The Matrix

ABSTRACT Late (L) domains containing the highly conserved sequence PPXY were first described for retroviruses, and later research confirmed their conservation and importance for efficient budding of several negative-stranded RNA viruses. Rabies virus (RV), a member of the Rhabdoviridae family, contains the sequence PPEY (amino acids 35 to 38) within the N terminus of the matrix (M) protein, but the functions of this potential L-domain in the viral life cycle, viral pathogenicity, and immunogenicity have not been established. Here we constructed a series of recombinant RVs containing mutations within the PPEY motif and analyzed their effects on viral replication and RV pathogenicity. Our results indicate that the first proline at position 35 is the most important for viral replication, whereas P36 and Y38 have a lesser but still noticeable impact. The reduction in viral replication was most likely due to inhibition of virion release, because initially no major impact on RV RNA synthesis was observed. In addition, results from electron microscopy demonstrated that the M4A mutant virus (PPEY→SAEA) displayed a more cell-associated phenotype than that of wild-type RV. Furthermore, all mutations within the PPEY motif resulted in reduced spread of the recombinant RVs as indicated by a reduction in focus size. Importantly, recombinant PPEY L-domain mutants were highly attenuated in mice yet still elicited potent antibody responses against RV G protein that were as high as those observed after infection with wild-type virus. Our data indicate that the RV PPEY motif has L-domain activity essential for efficient virus production and pathogenicity but is not essential for immunogenicity and thus can be targeted to increase the safety of rabies vaccine vectors.

scholarly journals Transmembrane communication in cells chronically infected with measles virus.

1979 ◽  
Vol 81 (2) ◽  
pp. 396-402 ◽  
Author(s):  
D L Tyrrell ◽  
A Ehrnst
Keyword(s):  
Nucleocapsid Protein ◽  
Measles Virus ◽  
Matrix Protein ◽  
Cytochalasin B ◽  
Viral Proteins ◽  
Surface Proteins ◽  
Nucleocapsid Proteins ◽  
Viral Antigens ◽  
The Matrix ◽  
Viral Inclusions

The transmembrane association of the measles virus hemagglutinin and hemolysin surface proteins with intracellular viral antigens was studied. Rabbit antisera monospecific for measles virus matrix and nucleocapsid proteins and a human antiserum containing specificities for both the hemagglutinin and hemolysin proteins were used to study the co-capping of these proteins in human Lu 106 cell-line, chronically infected with measles virus. Capping of the surface-associated envelope components was accompanied by co-capping of the matrix and nucleocapsid proteins, the latter being localized mainly within the inclusions. This demonstrated transmembrane communication between surface-associated envelope components and the intracellular measles virus matrix and nucleocapsid proteins. The results demonstrated the existence of a linkage between viral inclusions and viral proteins associated with cell membranes. In the presence of cytochalasin B (1--2 micrograms/ml), co-capping of the matrix protein was unchanged or slightly enhanced, whereas co-capping of the nucleocapsid protein decreased, indicating that actin filaments may mediate the communication between viral nucleocapsids and the cell membrane.

scholarly journals The unique degradation pathway of the PTS2 receptor, Pex7, is dependent on the PTS receptor/coreceptor, Pex5 and Pex20

2014 ◽  
Vol 25 (17) ◽  
pp. 2634-2643 ◽  
Author(s):  
Danielle Hagstrom ◽  
Changle Ma ◽  
Soumi Guha-Polley ◽  
Suresh Subramani
Keyword(s):  
Matrix Protein ◽  
Protein Import ◽  
Degradation Pathway ◽  
Matrix Proteins ◽  
Receptor Recycling ◽  
Wild Type ◽  
The Matrix ◽  
Peroxisomal Targeting ◽  
Targeting Signals ◽  
The Stability

Peroxisomal matrix protein import uses two peroxisomal targeting signals (PTSs). Most matrix proteins use the PTS1 pathway and its cargo receptor, Pex5. The PTS2 pathway is dependent on another receptor, Pex7, and its coreceptor, Pex20. We found that during the matrix protein import cycle, the stability and dynamics of Pex7 differ from those of Pex5 and Pex20. In Pichia pastoris, unlike Pex5 and Pex20, Pex7 is constitutively degraded in wild-type cells but is stabilized in pex mutants affecting matrix protein import. Degradation of Pex7 is more prevalent in cells grown in methanol, in which the PTS2 pathway is nonessential, in comparison with oleate, suggesting regulation of Pex7 turnover. Pex7 must shuttle into and out of peroxisomes before it is polyubiquitinated and degraded by the proteasome. The shuttling of Pex7, and consequently its degradation, is dependent on the receptor recycling pathways of Pex5 and Pex20 and relies on an interaction between Pex7 and Pex20. We also found that blocking the export of Pex20 from peroxisomes inhibits PTS1-mediated import, suggesting sharing of limited components in the export of PTS receptors/coreceptors. The shuttling and stability of Pex7 are divergent from those of Pex5 and Pex20, exemplifying a novel interdependence of the PTS1 and PTS2 pathways.

scholarly journals The Matrix Protein of Measles Virus Regulates Viral RNA Synthesis and Assembly by Interacting with the Nucleocapsid Protein

2009 ◽  
Vol 83 (20) ◽  
pp. 10374-10383 ◽  
Author(s):  
Masaharu Iwasaki ◽  
Makoto Takeda ◽  
Yuta Shirogane ◽  
Yuichiro Nakatsu ◽  
Takanori Nakamura ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Mammalian Cells ◽  
Measles Virus ◽  
Rna Synthesis ◽  
Matrix Protein ◽  
Viral Rna ◽  
M Protein ◽  
Ribonucleoprotein Complex ◽  
N Protein ◽  
The Matrix

ABSTRACT The genome of measles virus (MV) is encapsidated by the nucleocapsid (N) protein and associates with RNA-dependent RNA polymerase to form the ribonucleoprotein complex. The matrix (M) protein is believed to play an important role in MV assembly by linking the ribonucleoprotein complex with envelope glycoproteins. Analyses using a yeast two-hybrid system and coimmunoprecipitation in mammalian cells revealed that the M protein interacts with the N protein and that two leucine residues at the carboxyl terminus of the N protein (L523 and L524) are critical for the interaction. In MV minigenome reporter gene assays, the M protein inhibited viral RNA synthesis only when it was able to interact with the N protein. The N protein colocalized with the M protein at the plasma membrane when the proteins were coexpressed in plasmid-transfected or MV-infected cells. In contrast, the N protein formed small dots in the perinuclear area when it was expressed without the M protein, or it was incapable of interacting with the M protein. Furthermore, a recombinant MV possessing a mutant N protein incapable of interacting with the M protein grew much less efficiently than the parental virus. Since the M protein has an intrinsic ability to associate with the plasma membrane, it may retain the ribonucleoprotein complex at the plasma membrane by binding to the N protein, thereby stopping viral RNA synthesis and promoting viral particle production. Consequently, our results indicate that the M protein regulates MV RNA synthesis and assembly via its interaction with the N protein.

SSPE, measles virus, and the matrix protein: Report of a case with unusual immunochemical findings

1981 ◽  
Vol 10 (4) ◽  
pp. 351-354 ◽  
Author(s):  
David E. Mandelbaum ◽  
William W. Hall ◽  
Nigel Paneth ◽  
Robert R. Wolff ◽  
Darryl C. DeVivo
Keyword(s):  
Measles Virus ◽  
Matrix Protein ◽  
The Matrix

Altered translation of the matrix genes in Niigata and Yamagata neurovirulent measles virus strains

Virology ◽  
1991 ◽  
Vol 180 (1) ◽  
pp. 166-174 ◽  
Author(s):  
Minoru Ayata ◽  
Akiko Hirano ◽  
Timothy C. Wong
Keyword(s):  
Measles Virus ◽  
The Matrix ◽  
Virus Strains

scholarly journals Novel Gene Product of Thogoto Virus Segment 6 Codes for an Interferon Antagonist

2003 ◽  
Vol 77 (4) ◽  
pp. 2747-2752 ◽  
Author(s):  
Kathrin Hagmaier ◽  
Stephanie Jennings ◽  
Johanna Buse ◽  
Friedemann Weber ◽  
Georg Kochs
Keyword(s):  
Transcriptional Activation ◽  
Matrix Protein ◽  
Wild Type ◽  
Interferon Inducer ◽  
Double Stranded Rna ◽  
Unspliced Transcript ◽  
A Genome ◽  
The Matrix ◽  
Alpha Beta ◽  
Type Strains

ABSTRACT Thogoto virus (THOV) is a tick-transmitted orthomyxovirus with a genome of six negative-stranded RNA segments. The sixth segment encodes two different transcripts: a spliced transcript that is translated into the matrix protein (M) and an unspliced transcript. Here, we report that the unspliced transcript encodes an elongated form of M named ML. A THOV isolate deficient in ML expression was an efficient interferon inducer, whereas ML-expressing wild-type strains were poor interferon inducers. These results were confirmed with recombinant THOVs rescued from cDNAs. Expression of ML efficiently suppressed activation of the beta interferon promoter by double-stranded RNA. These results indicate that ML is an accessory protein that functions as a potent interferon antagonist by blocking transcriptional activation of alpha/beta interferons.

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