scholarly journals Cell Membrane-Associated Measles Virus Components Inhibit Antigen Processing

Virology ◽  
2001 ◽  
Vol 279 (2) ◽  
pp. 422-428 ◽  
Author(s):  
Jane Marttila ◽  
Ari Hinkkanen ◽  
Thedi Ziegler ◽  
Raija Vainionpää ◽  
Aimo Salmi ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Measles Virus ◽  
Antigen Processing

A Study of the Measles Virus-Induced Proteins Incorporated into the Cell Membrane

Intervirology ◽  
1979 ◽  
Vol 11 (5) ◽  
pp. 275-281 ◽  
Author(s):  
Fabian Wild ◽  
Tim Greenland
Keyword(s):  
Cell Membrane ◽  
Measles Virus ◽  
Induced Proteins

Short-stalk isoforms of CADM1 and CADM2 trigger neuropathogenic measles virus-mediated membrane fusion by interacting with the viral hemagglutinin

2021 ◽  
Author(s):  
Ryuichi Takemoto ◽  
Tateki Suzuki ◽  
Takao Hashiguchi ◽  
Yusuke Yanagi ◽  
Yuta Shirogane
Keyword(s):  
Cell Membrane ◽  
Membrane Fusion ◽  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Febrile Illness ◽  
Host Factors ◽  
F Protein ◽  
Short Stalk ◽  
Head Domain ◽  
H Protein

Measles virus (MeV), an enveloped RNA virus in the family Paramyxoviridae , usually causes acute febrile illness with skin rash, but in rare cases persists in the brain, causing a progressive neurological disorder, subacute sclerosing panencephalitis (SSPE). MeV bears two envelope glycoproteins, the hemagglutinin (H) and fusion (F) proteins. The H protein possesses a head domain that initially mediates receptor binding and a stalk domain that subsequently transmits the fusion-triggering signal to the F protein. We have recently shown that cell adhesion molecule 1 (CADM1, also known as IGSF4A, Necl-2, SynCAM1) and CADM2 (also known as IGSF4D, Necl-3, SynCAM2) are host factors enabling cell-cell membrane fusion mediated by hyperfusogenic F proteins of neuropathogenic MeVs as well as MeV spread between neurons lacking the known receptors. CADM1 and CADM2 interact in cis with the H protein on the same cell membrane, triggering hyperfusogenic F protein-mediated membrane fusion. Multiple isoforms of CADM1 and CADM2 containing various lengths of their stalk regions are generated by alternative splicing. Here we show that only short-stalk isoforms of CADM1 and CADM2 predominantly expressed in the brain induce hyperfusogenic F protein-mediated membrane fusion. While the known receptors interact in trans with the H protein through its head domain, these isoforms can interact in cis even with the H protein lacking the head domain and trigger membrane fusion, presumably through its stalk domain. Thus, our results unveil a new mechanism of viral fusion triggering by host factors. Importance Measles, an acute febrile illness with skin rash, is still an important cause of childhood morbidity and mortality worldwide. Measles virus (MeV), the causative agent of measles, may also cause a progressive neurological disorder, subacute sclerosing panencephalitis (SSPE), several years after acute infection. The disease is fatal, and no effective therapy is available. Recently, we have reported that cell adhesion molecule 1 (CADM1) and CADM2 are host factors enabling MeV cell-to-cell spread in neurons. These molecules interact in cis with the MeV attachment protein on the same cell membrane, triggering the fusion protein and causing membrane fusion. CADM1 and CADM2 are known to exist in multiple splice isoforms. In this study, we report that their short-stalk isoforms can induce membrane fusion by interacting in cis with the viral attachment protein independently of its receptor-binding head domain. This finding may have important implications for cis -acting fusion triggering by host factors.

scholarly journals Moesin: A Cell Membrane Protein Linked with Susceptibility to Measles Virus Infection

Virology ◽  
1994 ◽  
Vol 198 (1) ◽  
pp. 265-274 ◽  
Author(s):  
Lee M. Dunster ◽  
Jürgen Schneider-Schaulies ◽  
Sieglinde Lüffler ◽  
Wolfgang Lankes ◽  
Reinhard Schwartz-Albiez ◽  
...  
Keyword(s):  
Virus Infection ◽  
Cell Membrane ◽  
Membrane Protein ◽  
Measles Virus ◽  
A Cell ◽  
Cell Membrane Protein

scholarly journals Structural changes in the membrane of vero cells infected with a paramyxovirus.

1975 ◽  
Vol 67 (3) ◽  
pp. 551-565 ◽  
Author(s):  
M Dubois-Dalcq ◽  
T S Reese
Keyword(s):  
Cell Membrane ◽  
Measles Virus ◽  
Structural Changes ◽  
Vero Cells ◽  
Small Particles ◽  
Freeze Fracturing ◽  
Viral Antigens ◽  
Viral Budding ◽  
Membrane Surfaces ◽  
Viral Maturation

Vero cells productively infected with the Halle strain of measles virus have been studied by means of surface replication, freeze-fracturing, and surface labeling with horseradish peroxidase-measles antibody conjugate in order to examine changes in the structure of the cell membrane during viral maturation. Early in infection, the surfaces of infected cells are embossed by scattered groups of twisted strands, and diffuse patches of label for viral antigens cover regions marked by these strands. At later stages, when numerous nucleocapsids become aligned under the plasmalemmal strands, the strands increase in number and width and become more convoluted. At this stage, label for viral antigens on the surface of the cell membrane is organized into stripes lying on the crests of strands. Finally, regions of the membrane displaying twisted strands protrude to form ridges or bulges, and the freeze-fractured membrane surrounding these protrusions is characterized by an abundance of particles small than those found on the rest of the cell membrane. The fractured membranes of viral buds are continuous sheets of these small particles, and the spacing between both nucleocapsids and stripes of surface antigen in buds is less than in the surrounding cell membrane. Detached virus is covered with a continuous layer of viral antigen, has unusually large but no small particles on its membrane surfaces exposed by freeze-fracturing, and no longer has nucleocapsids aligned under its surface. Thus, surface antigens, membrane particles, and nucleocapsids attached to the cell membrane are mobile within the plane of the membrane during viral maturation. All three move simutaneously in preparation for viral budding.

scholarly journals The Distal Short Consensus Repeats 1 and 2 of the Membrane Cofactor Protein CD46 and Their Distance from the Cell Membrane Determine Productive Entry of Species B Adenovirus Serotype 35

2005 ◽  
Vol 79 (15) ◽  
pp. 10013-10022 ◽  
Author(s):  
Christoph Fleischli ◽  
Sandra Verhaagh ◽  
Menzo Havenga ◽  
Dominique Sirena ◽  
Walter Schaffner ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Measles Virus ◽  
Transgene Expression ◽  
Membrane Cofactor Protein ◽  
Virus Binding ◽  
Short Consensus Repeats ◽  
As Species ◽  
Binding Surface ◽  
Short Consensus Repeat ◽  
Type 3

ABSTRACT The human regulator of complement activation membrane cofactor protein (CD46) has recently been identified as an attachment receptor for most species B adenoviruses (Ads), including Ad type 3 (Ad3), Ad11, and Ad35, as well as species D Ad37. To characterize the interaction between Ad35 and CD46, hybrid receptors composed of different CD46 short consensus repeat (SCR) domains fused to immunoglobulin-like domains of CD4 and a set of 36 CD46 mutants containing semiconservative changes of single amino acids within SCR domains I and II were tested in binding and in Ad35-mediated luciferase transduction assays. In addition, anti-CD46 antibodies and soluble polypeptides constituting various CD46 domains were used in binding inhibition studies. Our data indicate that (i) CD46 SCR I or SCR II alone confers low but significant Ad35 binding; (ii) the presence of SCR I and II is required for optimal binding and transgene expression; (iii) transduction efficiencies equivalent to that of full-length CD46 are obtained if SCR I and II are at an appropriate distance from the cell membrane; (iv) ablation of the N-glycan attached to SCR I has no influence on receptor function, whereas ablation of the SCR II N-glycan results in about a two- to threefold reduction of binding and transgene expression; (v) most putative Ad35 binding residues are located on the same solvent-exposed face of the SCR I or SCR II domain, which are twisted by about 90°; and (vi) the putative Ad35 binding sites partly overlap with the measles virus binding surface.

scholarly journals Measles virus and canine distemper virus target proteins into a TAP-independent MHC class I-restricted antigen-processing pathway

2001 ◽  
Vol 82 (2) ◽  
pp. 441-447 ◽  
Author(s):  
Claudia Neumeister ◽  
Ralph Nanan ◽  
Tatjana I. Cornu ◽  
Carsten G. K. Lüder ◽  
Volker ter Meulen ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Measles Virus ◽  
Canine Distemper Virus ◽  
Antigen Processing ◽  
Matrix Protein ◽  
Cytotoxic T Cells ◽  
Viral Proteins ◽  
Canine Distemper ◽  
The Matrix

After infection of CEM174.T2 cells [deficient for the transporter of antigen presentation (TAP)] with measles virus (MV) the nucleocapsid protein is recognized by Ld-restricted cytotoxic T cells in a TAP-independent, chloroquine-sensitive fashion. Presentation via the TAP-independent pathway requires virus replication. During MV infection of the cell the nucleocapsid as well as the matrix protein enter the endolysosomal compartment as indicated by colocalization with the lysosomal-associated membrane protein 1 (LAMP-1). Similarly, the nucleocapsid protein of canine distemper virus (CDV) is recognized in a TAP-independent fashion. In addition, a recombinant MV expressing bacterial β-galactosidase protein is able to introduce the recombinant antigen into the TAP-independent pathway whereas a vaccinia virus expressing β-galactosidase is not. These data and a report about TAP-independent recognition of parainfluenza virus type 1 suggest that members of the Paramyxoviridae family regularly introduce viral proteins into the TAP-independent antigen-processing pathway.

scholarly journals In Vivo Efficacy of Measles Virus Fusion Protein-Derived Peptides Is Modulated by the Properties of Self-Assembly and Membrane Residence

2016 ◽  
Vol 91 (1) ◽  
Author(s):  
T. N. Figueira ◽  
L. M. Palermo ◽  
A. S. Veiga ◽  
D. Huey ◽  
C. A. Alabi ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Target Cell ◽  
Self Assembly ◽  
Measles Virus ◽  
Structural Transition ◽  
Target Cells ◽  
Fusion Inhibitor ◽  
Inhibitory Peptides ◽  
Target Cell Membrane

ABSTRACT Measles virus (MV) infection is undergoing resurgence and remains one of the leading causes of death among young children worldwide despite the availability of an effective measles vaccine. MV infects its target cells by coordinated action of the MV hemagglutinin (H) and fusion (F) envelope glycoproteins; upon receptor engagement by H, the prefusion F undergoes a structural transition, extending and inserting into the target cell membrane and then refolding into a postfusion structure that fuses the viral and cell membranes. By interfering with this structural transition of F, peptides derived from the heptad repeat (HR) regions of F can inhibit MV infection at the entry stage. In previous work, we have generated potent MV fusion inhibitors by dimerizing the F-derived peptides and conjugating them to cholesterol. We have shown that prophylactic intranasal administration of our lead fusion inhibitor efficiently protects from MV infection in vivo. We show here that peptides tagged with lipophilic moieties self-assemble into nanoparticles until they reach the target cells, where they are integrated into cell membranes. The self-assembly feature enhances biodistribution and the half-life of the peptides, while integration into the target cell membrane increases fusion inhibitor potency. These factors together modulate in vivo efficacy. The results suggest a new framework for developing effective fusion inhibitory peptides. IMPORTANCE Measles virus (MV) infection causes an acute illness that may be associated with infection of the central nervous system (CNS) and severe neurological disease. No specific treatment is available. We have shown that fusion-inhibitory peptides delivered intranasally provide effective prophylaxis against MV infection. We show here that specific biophysical properties regulate the in vivo efficacy of MV F-derived peptides.

Use of Protein a Conjugated to Peroxidase to Localize Immunoglobulin G in SSPE Ferret Brain

1982 ◽  
Vol 40 ◽  
pp. 350-351
Author(s):  
Hannah R. Brown ◽  
Anthony F. Nostro ◽  
Halldor Thormar
Keyword(s):  
Immunoglobulin G ◽  
Human Disease ◽  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Protein A ◽  
Inflammatory Lesions ◽  
Sspe Virus ◽  
Specific Immunoglobulin ◽  
Antibody Titers ◽  
The Brain

Subacute sclerosing panencephalitis (SSPE) is a slowly progressing disease of the CNS in children which is caused by measles virus. Ferrets immunized with measles virus prior to inoculation with the cell associated, syncytiogenic D.R. strain of SSPE virus exhibit characteristics very similar to the human disease. Measles virus nucleocapsids are present, high measles antibody titers are found in the sera and inflammatory lesions are prominent in the brains. Measles virus specific immunoglobulin G (IgG) is present in the brain,and IgG/ albumin ratios indicate that the antibodies are synthesized within the CNS.

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