scholarly journals Identification of a Second Major Site for CD46 Binding in the Hemagglutinin Protein from a Laboratory Strain of Measles Virus (MV): Potential Consequences for Wild-Type MV Infection

2003 ◽  
Vol 77 (11) ◽  
pp. 6585-6585
Author(s):  
Nicolas Massé ◽  
Thomas Barrett ◽  
Claude P. Muller ◽  
T. Fabian Wild ◽  
Robin Buckland
Keyword(s):  
Measles Virus ◽  
Laboratory Strain ◽  
Wild Type ◽  
Major Site ◽  
Hemagglutinin Protein

scholarly journals Identification of a Second Major Site for CD46 Binding in the Hemagglutinin Protein from a Laboratory Strain of Measles Virus (MV): Potential Consequences for Wild-Type MV Infection

2002 ◽  
Vol 76 (24) ◽  
pp. 13034-13038 ◽  
Author(s):  
Nicolas Massé ◽  
Thomas Barrett ◽  
Claude P. Muller ◽  
T. Fabian Wild ◽  
Robin Buckland
Keyword(s):  
Measles Virus ◽  
Laboratory Strain ◽  
Cell Receptor ◽  
Respiratory Epithelium ◽  
Wild Type ◽  
Major Site ◽  
Hemagglutinin Protein ◽  
A Cell ◽  
H Protein

ABSTRACT Natural or wild-type (wt) measles virus (MV) infection in vivo which is restricted to humans and certain monkeys represents an enigma in terms of receptor usage. Although wt MV is known to use the protein SLAM (CD150) as a cell receptor, many human tissues, including respiratory epithelium in which the infection initiates, are SLAM negative. These tissues are CD46 positive, but wt MV strains, unlike vaccinal and laboratory MV strains, are not thought to use CD46 as a receptor. We have identified a novel CD46 binding site at residues S548 and F549, in the hemagglutinin (H) protein from a laboratory MV strain, which is also present in wt H proteins. Our results suggest that although wt MV interacts with SLAM with high affinity, it also possesses the capacity to interact with CD46 with low affinity.

scholarly journals A Single Amino Acid Change in the Hemagglutinin Protein of Measles Virus Determines Its Ability To Bind CD46 and Reveals Another Receptor on Marmoset B Cells

1998 ◽  
Vol 72 (4) ◽  
pp. 2905-2916 ◽  
Author(s):  
Eric C. Hsu ◽  
Farida Sarangi ◽  
Caterina Iorio ◽  
Mohinderjit S. Sidhu ◽  
Stephen A. Udem ◽  
...  
Keyword(s):  
B Cells ◽  
Measles Virus ◽  
Insect Cells ◽  
Binding Assay ◽  
Laboratory Strain ◽  
Single Amino Acid ◽  
Wild Type ◽  
Human B Cells ◽  
Single Amino Acid Change ◽  
Direct Binding

ABSTRACT This paper provides evidence for a measles virus receptor other than CD46 on transformed marmoset and human B cells. We first showed that most tissues of marmosets are missing the SCR1 domain of CD46, which is essential for the binding of Edmonston measles virus, a laboratory strain that has been propagated in Vero monkey kidney cells. In spite of this deletion, the common marmoset was shown to be susceptible to infections by wild-type isolates of measles virus, although they did not support Edmonston measles virus production. As one would expect from these results, measles virus could not be propagated in owl monkey or marmoset kidney cell lines, but surprisingly, both a wild-type isolate (Montefiore 89) and the Edmonston laboratory strain of measles virus grew efficiently in B95-8 marmoset B cells. In addition, antibodies directed against CD46 had no effect on wild-type infections of marmoset B cells and only partially inhibited the replication of the Edmonston laboratory strain in the same cells. A direct binding assay with insect cells expressing the hemagglutinin (H) proteins of either the Edmonston or Montefiore 89 measles virus strains was used to probe the receptors on these B cells. Insect cells expressing Edmonston H but not the wild-type H bound to rodent cells with CD46 on their surface. On the other hand, both the Montefiore 89 H and Edmonston H proteins adhered to marmoset and human B cells. Most wild-type H proteins have asparagine residues at position 481 and can be converted to a CD46-binding phenotype by replacement of the residue with tyrosine. Similarly, the Edmonston H protein did not bind CD46 when its Tyr481 was converted to asparagine. However, this mutation did not affect the ability of Edmonston H to bind marmoset and human B cells. The preceding results provide evidence, through the use of a direct binding assay, that a second receptor for measles virus is present on primate B cells.

scholarly journals Mutations in the H, F, or M Proteins Can Facilitate Resistance of Measles Virus to Neutralizing Human Anti-MV Sera

2014 ◽  
Vol 2014 ◽  
pp. 1-18 ◽  
Author(s):  
Hasan Kweder ◽  
Michelle Ainouze ◽  
Sara Louise Cosby ◽  
Claude P. Muller ◽  
Camille Lévy ◽  
...  
Keyword(s):  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Laboratory Strain ◽  
Viral Escape ◽  
Wild Type ◽  
Immune Resistance ◽  
M Proteins ◽  
Escape Mutants ◽  
Shed Light

Although there is currently no evidence of emerging strains of measles virus (MV) that can resist neutralization by the anti-MV antibodies present in vaccinees, certain mutations in circulating wt MV strains appear to reduce the efficacy of these antibodies. Moreover, it has been hypothesized that resistance to neutralization by such antibodies could allow MV to persist. In this study, we use a novelin vitrosystem to determine the molecular basis of MV’s resistance to neutralization. We find that both wild-type and laboratory strain MV variants that escape neutralization by anti-MV polyclonal sera possess multiple mutations in their H, F, and M proteins. Cytometric analysis of cells expressing viral escape mutants possessing minimal mutations and their plasmid-expressed H, F, and M proteins indicates that immune resistance is due to particular mutations that can occur in any of these three proteins that affect at distance, rather than directly, the native conformation of the MV-H globular head and hence its epitopes. A high percentage of the escape mutants contain mutations found in cases of Subacute Sclerosing Panencephalitis (SSPE) and our results could potentially shed light on the pathogenesis of this rare fatal disease.

scholarly journals Wild-Type Measles Virus with the Hemagglutinin Protein of the Edmonston Vaccine Strain Retains Wild-Type Tropism in Macaques

2012 ◽  
Vol 86 (6) ◽  
pp. 3027-3037 ◽  
Author(s):  
K. Takeuchi ◽  
N. Nagata ◽  
S.-i. Kato ◽  
Y. Ami ◽  
Y. Suzaki ◽  
...  
Keyword(s):  
Vaccine Strain ◽  
Measles Virus ◽  
Wild Type ◽  
Hemagglutinin Protein

scholarly journals Hemagglutinin Protein of Wild-Type Measles Virus Activates Toll-Like Receptor 2 Signaling

2002 ◽  
Vol 76 (17) ◽  
pp. 8729-8736 ◽  
Author(s):  
Karen Bieback ◽  
Egil Lien ◽  
Ingo M. Klagge ◽  
Elita Avota ◽  
Jürgen Schneider-Schaulies ◽  
...  
Keyword(s):  
Measles Virus ◽  
Surface Expression ◽  
Single Amino Acid ◽  
Wild Type ◽  
Monocytic Cells ◽  
Viral Spread ◽  
Tlr2 Activation ◽  
Hemagglutinin Protein ◽  
Antigen Presenting ◽  
H Protein

ABSTRACT Pattern recognition via Toll-like receptors (TLR) by antigen-presenting cells is an important element of innate immunity. We report that wild-type measles virus but not vaccine strains activate cells via both human and murine TLR2, and this is a property of the hemagglutinin (H) protein. The ability to activate cells via TLR2 by wild-type MV H protein is abolished by mutation of a single amino acid, asparagine at position 481 to tyrosine, as is found in attenuated strains, which is important for interaction with CD46, the receptor for these strains. TLR2 activation by MV wild-type H protein stimulates induction of proinflammatory cytokines such as interleukin-6 (IL-6) in human monocytic cells and surface expression of CD150, the receptor for all MV strains. Confirming the specificity of this interaction, wild-type H protein did not induce IL-6 release in macrophages from TLR2−/− mice. Thus, the unique property of MV wild-type strains to activate TLR2-dependent signals might essentially contribute not only to immune activation but also to viral spread and pathogenicity by upregulating the MV receptor on monocytes.

scholarly journals Recombinant Wild-Type and Edmonston Strain Measles Viruses Bearing Heterologous H Proteins: Role of H Protein in Cell Fusion and Host Cell Specificity

2002 ◽  
Vol 76 (10) ◽  
pp. 4891-4900 ◽  
Author(s):  
Kaoru Takeuchi ◽  
Makoto Takeda ◽  
Naoko Miyajima ◽  
Fumio Kobune ◽  
Kiyoshi Tanabayashi ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Fusion ◽  
Measles Virus ◽  
Laboratory Strain ◽  
Vero Cells ◽  
Cellular Receptor ◽  
Wild Type ◽  
Cell Specificity ◽  
H Protein

ABSTRACT Wild-type measles virus (MV) isolated from B95a cells has a restricted host cell specificity and hardly replicates in Vero cells, whereas the laboratory strain Edmonston (Ed) replicates in a variety of cell types including Vero cells. To investigate the role of H protein in the differential MV host cell specificity and cell fusion activity, H proteins of wild-type MV (IC-B) and Ed were coexpressed with the F protein in Vero cells. Cell-cell fusion occurred in Vero cells when Ed H protein, but not IC-B H protein, was expressed. To analyze the role of H protein in the context of viral infection, a recombinant IC-B virus bearing Ed H protein (IC/Ed-H) and a recombinant Ed virus bearing IC-B H protein (Ed/IC-H) were generated from cloned cDNAs. IC/Ed-H replicated efficiently in Vero cells and induced small syncytia in Vero cells, indicating that Ed H protein conferred replication ability in Vero cells on IC/Ed-H. On the other hand, Ed/IC-H also replicated well in Vero cells and induced small syncytia, although parental Ed induced large syncytia in Vero cells. These results indicated that an MV protein(s) other than H protein was likely involved in determining cell fusion and host cell specificity of MV in the case of our recombinants. SLAM (CDw150), a recently identified cellular receptor for wild-type MV, was not expressed in Vero cells, and a monoclonal antibody against CD46, a cellular receptor for Ed, did not block replication or syncytium formation of Ed/IC-H in Vero cells. It is therefore suggested that Ed/IC-H entered Vero cells through another cellular receptor.

scholarly journals Measles Virus Infects and Suppresses Proliferation of T Lymphocytes from Transgenic Mice Bearing Human Signaling Lymphocytic Activation Molecule

2003 ◽  
Vol 77 (6) ◽  
pp. 3505-3515 ◽  
Author(s):  
Bumsuk Hahm ◽  
Nathalie Arbour ◽  
Denise Naniche ◽  
Dirk Homann ◽  
Marianne Manchester ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Division ◽  
Transgenic Mice ◽  
Measles Virus ◽  
Laboratory Strain ◽  
Proximal Promoter ◽  
Wild Type ◽  
Natural Reservoir ◽  
Signaling Lymphocytic Activation Molecule

ABSTRACT Humans are the only natural reservoir of measles virus (MV), one of the most contagious viruses known. MV infection and the profound immunosuppression it causes are currently responsible for nearly one million deaths annually. Human signaling lymphocytic activation molecule (hSLAM) was identified as a receptor for wild-type MV as well as for MV strains prepared as vaccines. To better evaluate the role of hSLAM in MV pathogenesis and MV-induced immunosuppression, we created transgenic (tg) mice that expressed the hSLAM molecule under the control of the lck proximal promoter. hSLAM was expressed on CD4+ and CD8+ T cells in the blood and spleen and also on CD4+, CD8+, CD4+ CD8+, and CD4− CD8− thymocytes. Wild-type MV, after limited passage on B95-8 marmoset B cells, and the Edmonston laboratory strain of MV infected hSLAM-expressing cells. There was a direct correlation between the amount of hSLAM expressed on the cells' surface and the degree of viral infection. Additionally, MV infection induced downregulation of receptor hSLAM and inhibited cell division and proliferation of hSLAM+ but not hSLAM− T cells. Therefore, these tg mice provide the opportunity for analyzing and comparing MV-T cell interactions and MV pathogenesis in cells expressing only the hSLAM MV receptor with those of tg mice whose T cells selectively express another MV receptor, CD46.

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