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PubMed1981

Examination of the immunological relationship between measles virus and canine distemper virus using monospecific measles antisera.

Indirect immunofluorescence titrations were performed with measles virus, the Rockborn strain of canine distemper virus (CDV), and a large plaque variant of the Onderstepoort strain of CDV (Ond-LP) using monospecific antisera prepared against either the haemagglutinin (anti-HA), the haemolysin (anti-HL), or the ribonucleoprotein (anti-RNP) of measles virus. Tests with anti-HA showed that the Rockborn strain of CDV was more closely related to measles virus than Ond-LP. The ribonucleoprotein antigens of the CDV strains were closely related to each other but were both related to and distinct from measles virus RNP. The use of measles anti-HL serum demonstrated that CDV possesses an antigenically related acetone-sensitive component equivalent to the haemolysin of measles virus. Absorption of human convalescent serum with excess quantities of acetone-fixed CDV antigens had no effect on measles-specific anti-HA, HL, or RNP activity in the serum. Absorption with measles antigens on the other hand, totally removed all measles and CDV-specific HA and RNP activity. CDV was not neutralised by any of the monospecific antisera when tested either as individual antisera or as mixtures. Our results demonstrate the occurrence of antigenic variation between different strains of CDV, they also reveal unique antigenic determinants in both measles virus and CDV.

Antigens, Viral↗
PubMed2004

Influence of HLA-DRB1 alleles on lymphoproliferative responses to a naturally processed and presented measles virus phosphoprotein in measles immunized individuals.

Identification of stimulatory T-cell epitopes recognized by CD4+ T lymphocytes is important for vaccine development. Our previous studies using mass spectrometry identified a naturally processed HLA class II restricted DRB1*0301 T cell epitope in the measles virus phosphoprotein, MV-P1 (residues 179-197). Here we provide lymphocyte proliferation data from peripheral blood mononuclear cells (PBMC) obtained from 131 HLA-DRB1*0301-positive and HLA-DRB1*0301-negative (HLA discordant) individuals previously immunized against measles and report that a single amino acid substitution in the MV-P1 T cell epitope can reduce T cell proliferation and CD4+ T-cell recognition. Measles virus and measles peptide-specific lymphoproliferative responses and HLA-DRB1 allele associations reveal that the DRB1*0701 allele provided suggestive evidence of association with both measles virus (p = 0.03) and MV-P1 peptide (p = 0.06) lymphoproliferation. A marginally significant increase in the frequency of the *0301 allele (p = 0.10) was found among subjects who demonstrated low cellular responses to the measles virus. We found no associations between proliferation levels to the MV-P1 and MV-P2 peptides with *0301 alleles. We speculate that the glutamic acid at position 192 of the measles phosphoprotein is a critical immunogenicity factor and may influence the antigenicity of the naturally processed HLA class II MV-P1 epitope.

Alleles↗
PubMed2004

Lack of evidence of measles virus shedding in people with inapparent measles virus infections.

Serological evidence of measles virus infection has been detected among people exposed to measles who do not exhibit classical clinical symptoms. Throat swabs, lymphocytes, and serum and urine samples were collected from contacts of individuals with confirmed measles 12-16 days after exposure, during measles outbreaks occurring in 1998. Follow-up serum samples were drawn 2 weeks later. Samples were tested for measles IgM antibody by enzyme immunoassays and plaque reduction neutralization testing. Virus isolation and reverse transcriptase-polymerase chain reaction testing was attempted for all samples. None of the 133 contacts developed classical measles disease; 11 (8%) had serological evidence of infection. Duration of exposure of >or=3 h was the only significant risk factor for developing serological response (24% vs. 4% among contacts exposed for 1-2 h; relative risk, 6.0; 95% confidence interval, 1.9-19.2). None of the 133 contacts had virological evidence of infection by culture or polymerase chain reaction. We found no evidence that persons with inapparent measles virus infections shed measles virus.

Adolescent↗
PubMed2000

Human parainfluenza virus type 3 (PIV3) expressing the hemagglutinin protein of measles virus provides a potential method for immunization against measles virus and PIV3 in early infancy.

Recombinant human parainfluenza virus type 3 (PIV3) was used as a vector to express the major protective antigen of measles virus, the hemagglutinin (HA) glycoprotein, in order to create a bivalent PIV3-measles virus that can be administered intranasally. The measles virus HA open reading frame (ORF) was inserted as an additional transcriptional unit into the N-P, P-M, or HA-neuraminidase (HN)-L gene junction of wild-type PIV3 or into the N-P or P-M gene junction of an attenuated derivative of PIV3, termed rcp45L. The recombinant PIV3 (rPIV3) viruses bearing the HA inserts replicated more slowly in vitro than their parental viruses but reached comparable peak titers of >/=10(7.5) 50% tissue culture infective doses per ml. Each of the wild-type or cold-passaged 45L (cp45L) PIV3(HA) chimeric viruses replicated 5- to 10-fold less well than its respective parent virus in the upper respiratory tract of hamsters. Thus, insertion of the approximately 2-kb ORF itself conferred attenuation, and this attenuation was additive to that conferred by the cp45L mutations. The attenuated cp45L PIV3(HA) recombinants induced a high level of resistance to replication of PIV3 challenge virus in hamsters and induced very high levels of measles virus neutralizing antibodies (>1:8,000) that are well in excess of those known to be protective in humans. rPIV3s expressing the HA gene in the N-P or P-M junction induced about 400-fold more measles virus-neutralizing antibody than did the rPIV3 with the HA gene in the HN-L junction, indicating that the N-P or P-M junction appears to be the preferred insertion site. Previous studies indicated that the PIV3 cp45 virus, a more attenuated version of rcp45L, replicates efficiently in the respiratory tract of monkeys and is immunogenic and protective even when administered in the presence of very high titers of passively transferred PIV3 antibodies (A. P. Durbin, C. J. Cho, W. R. Elkins, L. S. Wyatt, B. Moss, and B. R. Murphy, J. Infect. Dis. 179:1345-1351, 1999). This suggests that this intranasally administered PIV3(HA) chimeric virus can be used to immunize infants with maternally acquired measles virus antibodies in whom the current parenterally administered live measles virus vaccine is ineffective.

Animals↗
PubMed2003

Manganese superoxide dismutase induction during measles virus infection.

Measles virus infection of B-cells results in marked alterations in proliferation and immunoglobulin production. Very little is known about the changes of gene expression, if any, during acute measles virus infection. To elucidate cellular genes that are induced during measles virus infection, we carried out a subtraction technique, representational differential analysis. The mitochondrial protein, manganese superoxide dismutase (MnSOD), was upregulated in B-cells during measles virus infection. Although measles virus-infected B-cells did not secrete MnSOD into the environment, it was found, using an MnSOD mimetic, that intracellular MnSOD did inhibit proliferation of the B-cells. MnSOD also decreases the titer of virus produced from infected cells. Therefore, MnSOD seems to play a role in the alteration of immune function seen upon infection of B-cells with measles virus.

B-Lymphocytes↗
PubMed1994

Moesin: a cell membrane protein linked with susceptibility to measles virus infection.

Measles virus is a highly contagious virus causing acute and persistent diseases in man, the receptor of which is still not well characterized. We have isolated a monoclonal antibody (mAb), designated mAb 119, which specifically inhibits measles virus infection of susceptible cell lines in a dose-dependent manner. This antibody precipitates a protein with an apparent molecular mass of 75 kDa from 125I surface-labeled cells and its epitope is present on human peripheral blood mononuclear cells, human cell lines, and the African green monkey cell line Vero. Affinity chromatography of detergent-solubilized cell membrane proteins over a Sepharose column with covalently bound mAb 119 led to the partial purification of the 75-kDa protein. Preincubation of measles virus with this affinity-purified protein inhibited measles virus infection dose dependently. Amino acid microsequencing of this protein revealed its identity with the human membrane-organizing extension spike protein moesin, a protein intra- and extracellularly associated with the plasma membrane of cells. Subsequently, an antibody raised against purified moesin (mAb 38/87) was also found to specifically inhibit measles virus infection of susceptible cells and confirmed our data obtained with mAb 119. Our data suggest that moesin is acting as a receptor for measles virus.

Amino Acid Sequence↗
PubMed1992

Construction of vaccinia virus recombinants expressing several measles virus proteins and analysis of their efficacy in vaccination of mice.

Measles virus genes encoding the haemagglutinin (HA), fusion protein (F) or nucleoprotein (NP) have been inserted into the vaccinia virus genome either alone or in various combinations. In each case the measles virus genes were expressed from the 7.5K promoter and were incorporated into the thymidine kinase (tk) or K1L loci of the Copenhagen strain of vaccinia virus. Cells infected by the recombinants synthesized measles virus proteins indistinguishable from those induced in measles virus-infected cells. However, in some instances the level of expression in cells infected by recombinants expressing more than one measles virus gene was reduced when compared to those encoding a single gene. The sera from mice immunized with recombinants containing either HA, HA.F, HA.NP or HA.F.NP had similar levels of measles virus neutralizing antibodies which remained constant throughout a 7 month period. Analysis of these sera by immunoprecipitation of radiolabelled measles virus confirmed the presence of specific antibody to each of the antigens where appropriate. The introduction of the measles virus genes into the K1L and the tk sites despite attenuating the virus for mice by 10-fold and 1000-fold respectively did not affect the vaccination efficiency, i.e. ability to induce measles virus antibody and protect mice. Vaccination of BALB/c (H2d) mice with HA and F, but not NP, recombinants completely protected the animals against a lethal measles virus challenge. In contrast, although the HA recombinant protected CBA (H2k) mice, the F recombinant did so poorly. However, by immunizing CBA mice with a recombinant expressing both F and NP, protection was increased to more than 75%. Our findings demonstrate the ability of three measles virus antigens expressed from the vaccinia virus genome alone or in combination to contribute to protective immunity against measles virus infection of mice. They also suggest that the association of measles virus antigens in a single recombinant DNA vaccine could be beneficial to overcome host-related restriction of the immune response to particular antigens.

Animals↗
PubMed2001

[Nucleotide sequence of the noncoding regions of measles virus stain CC-47 and comparison with other measles viruses].

BACKGROUND: To determine the nucleotide sequence of noncoding regions of Measles virus strain Changchun-47 (CC-47) and to compare them with other measles virus for revealing some vaccine-related information. METHODS: Six overlapped fragments, that covers complete genome of CC-47 were amplified by using RT-PCR, all of the amplified fragments have been cloned and sequenced. RESULTS: Seven noncoding regions lie in the genome sequence of CC-47 separated by six structure genes. The noncoding regions of CC-47 contain 1791 nucleotides totally. Comparing of the noncoding regions of CC-47 with other wild type strains and five Edmonston-derived vaccine strains, four nucleotide substitutions were shared by nearly all vaccine strains. Two of these were in the genomic 3 terminal transcriptional control region: position 26 (U->G), 42 (U->G); the other were in the F mRNA 5 -untranslated region of M/F intergenic region. These site substitutions may influence the efficiency of mRNA synthesis, processing, and translation, as wel l as genome replication and encapsidation. CONCLUSIONS: The nucleotide substitutions shared by different genotype measles virus vaccine strains may be related to virus growth in semipermissive cell or process of attenuation, which provide useful data for molecular epidemiology of measles virus. The nucleotide substitutions for attenuation were involved in several regions other than one definite region.

3' Untranslated Regions↗
PubMed1991

Role of biased hypermutation in evolution of subacute sclerosing panencephalitis virus from progenitor acute measles virus.

We identified an acute measles virus (Nagahata strain) closely related to a defective virus (Biken strain) isolated from a patient with subacute sclerosing panencephalitis (SSPE). The proteins of Nagahata strain measles virus are antigenically and electrophoretically similar to the proteins of Edmonston strain measles virus. However, the nucleotide sequence of the Nagahata matrix (M) gene is significantly different from the M genes of all the acute measles virus strains studied to date. The Nagahata M gene is strikingly similar to the M gene of Biken strain SSPE virus isolated several years later in the same locale. Eighty percent of the nucleotide differences between the Nagahata and Biken M genes are uridine-to-cytosine transitions known as biased hypermutation, which has been postulated to be caused by a cellular RNA-modifying activity. These biased mutations account for all but one of the numerous missense genetic changes predicted to cause amino acid substitutions. As a result, the Biken virus M protein loses conformation-specific epitopes that are conserved in the M proteins of Nagahata and Edmonston strain acute measles viruses. These conformation-specific epitopes are also absent in the cryptic M proteins encoded by the hypermutated M genes of two other defective SSPE viruses (Niigata and Yamagata strains). Nagahata-like sequences are found in the M genes of at least five other SSPE viruses isolated from three continents. These data indicate that Biken strain SSPE virus is derived from a progenitor closely resembling Nagahata strain acute measles virus and that biased hypermutation is largely responsible for the structural defects in the Biken virus M protein.

Animals↗
PubMed1994

The role of N-glycosylation in cell fusion induced by a vaccinia recombinant virus expressing both measles virus glycoproteins.

We have evaluated the effect of inhibitors of N-glycosylation on syncytia formation in HeLa cell infected by a recombinant vaccinia virus expressing the measles virus hemagglutinin (HA) and fusion (F) glycoproteins (VV-HA/F). Inhibitors which block glucose trimming of oligosaccharides side chains of glycoproteins (glucosidase inhibitors) prevented syncytium formation. On the other hand, inhibitors which block trimming of mannose residues (mannosidase inhibitors) did not prevent syncytium formation. The HA and F synthesized in the presence of either glucosidase or mannosidase inhibitors oligomerized and were transported to the cell surface. Concanavalin A, a mannose-specific lectin, inhibited syncytium formation. The inhibitors did not block the cleavage of the F protein, but in fact enhanced it. These studies demonstrate the importance of protein N-glycosylation in the process of membrane fusion and suggest that trimming of glucose residues and the presence of terminal mannose residues are required for VV-HA/F syncytium induction.

Cell Fusion↗
PubMed1991

Assembly of nucleocapsidlike structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein.

A vaccinia virus recombinant containing the measles virus nucleoprotein gene was shown to induce the synthesis of a 60 kDa phosphorylated nucleoprotein similar to authentic measles virus nucleoprotein. Mammalian or avian cells infected with the recombinant virus displayed tubular structures reminiscent of viral nucleocapsids both in the cytoplasm and in the nucleus. Such structures could be labelled in situ by using an immunogold detection method specific for measles virus proteins. Electron microscopic examination of tubular structures purified from cells infected with the vaccinia virus recombinant indicated that they displayed most of the features of measles virus nucleocapsids, although their length was on the average shorter. These results demonstrate the spontaneous assembly of measles virus nucleocapsids in the absence of viral leader RNA and provide a means for a detailed molecular analysis of the requirements for nucleocapsid assembly. Furthermore, these findings raise the possibility of achieving complete assembly of measles virus particles, devoid of infectious RNA, by using a vaccinia virus vector.

Animals↗