Phase Fraction Estimation in Multicomponent Alloy from EDS Measurement Data.

To perform quality assessments of both metal alloys and many other engineering materials, measurements of the volume fractions of phases or microstructure components are utilized. For this purpose, quantitative analysis of the evaluated components' distribution on metallographic specimens is often employed. Phases or components of the microstructure are identified based on the variation in signal received in the band of light seen.

Benefit of Contact Force Sensing Catheter Technology for Successful Left Atrial Anterior Line Formation: A Prospective Randomized Trial.

Introduction: The value of contact force information for ablation of LA anterior line is unknown. In a prospective randomized clinical trial, we investigated if information on contact force during left atrial (LA) anterior line ablation reduces total radiofrequency time and results in higher rates of bidirectional line block in patients undergoing pulmonary vein isolation (PVI) plus substrate modification.

Methods: We included patients with indication for pulmonary vein isolation (PVI) and additional substrate modification.

Antigenic diversity of the glycoprotein and nucleocapsid proteins of rabies and rabies-related viruses: implications for epidemiology and control of rabies.

Rabies virus-specific monoclonal antibodies (MAbs) have served to describe operationally the topography of the antigenic structure of the glycoprotein and nucleocapsid proteins of rabies virus. With the use of nucleocapsid protein-specific MAbs and cleavage fragments of the nucleoprotein and phosphoprotein, it has been possible to identify the chemical structure of two antigenic sites of the nucleoprotein and one antigenic site of the phosphoprotein. Antisera produced to synthetic peptides that make up the structure of these antigenic sites exhibited reactivities similar to those of MAbs.

Epidemiology of rabies virus variants. Differentiation using monoclonal antibodies and discriminant analysis.

Rabies virus was isolated by cell culture from the brains of 104 confirmed rabies cases diagnosed by the fluorescent-antibody staining technique in the United States during 1974-1984. Eighty-seven isolates were obtained from wild-life species, 10 from humans, and seven from domestic animals. These isolates were tested in virus neutralization and immunofluorescence assays using a panel of 34 monoclonal antibodies specific for rabies virus nucleocapsid protein, 44 monoclonal antibodies specific for rabies virus glycoprotein, and two monoclonal antibodies specific for rabies virus nucleocapsid-associated phosphoprotein.

Immune response in skunks to a vaccinia virus recombinant expressing the rabies virus glycoprotein.

Striped skunks (Mephitis mephitis) were vaccinated with a vaccinia virus recombinant expressing the rabies virus glycoprotein. Virus neutralizing antibodies to rabies virus were present at 14 days postvaccination by the following routes: scarification (6/6), intramuscular (4/4) and intestinal (5/8). Six out of seven skunks that ate vaccine filled baits had virus neutralizing antibodies at 28 days.

Oral immunization and protection of raccoons (Procyon lotor) with a vaccinia-rabies glycoprotein recombinant virus vaccine.

Animal rabies control has been frustrated by the existence of multiple wildlife reservoirs and the lack of efficacious oral vaccines. In this investigation, raccoons fed a vaccinia-rabies glycoprotein recombinant virus in a sponge bait developed rabies virus-neutralizing antibody (0.6-54.

Molecular mimicry: frequency of reactivity of monoclonal antiviral antibodies with normal tissues.

More than 600 monoclonal antiviral antibodies made against 11 different viruses were screened against 14 different organs from normal uninfected mice. Of these antiviral antibodies, 21, or approximately 3.5%, reacted with specific cells in these organs.

Isolation and characterization of human T cell lines and clones reactive to rabies virus: antigen specificity and production of interferon-gamma.

By using a preparation of inactivated rabies virus, the blood mononuclear cells from five rabies vaccine recipients were stimulated in vitro in the presence of interleukin 2. T cell lines that displayed significant proliferative responses to whole rabies virus and to preparations of rabies glycoprotein and nucleocapsid were obtained from all the individuals. Other antigens, such as diphtheria and tetanus toxoids, influenza A virus, hepatitis B surface antigen, and serum albumin, failed to induce the proliferation of the T cell lines.

Amplification of rabies virus-induced stimulation of human T-cell lines and clones by antigen-specific antibodies.

The effect of antigen-specific antibodies on the response of human T-cell lines and clones to rabies virus was studied. Plasmas from rabies-immune vaccine recipients, but not those from nonimmune individuals, enhanced the proliferative response of rabies-reactive T cells to whole inactivated virus or to the purified glycoprotein and nucleocapsid from the rabies virion. Rabies-immune plasma also increased the antigen-induced production of gamma interferon by the rabies-specific T-cell lines.

Differences in cell-to-cell spread of pathogenic and apathogenic rabies virus in vivo and in vitro.

Pathogenic parental rabies virus and apathogenic variant virus were shown to differ in their ability to infect neurons in vivo and neuroblastoma cells in vitro. After intracerebral inoculation, the distribution of infected neurons in the brain was similar for both viruses, but the rate of spread throughout the brain, the number of infected neurons, and the degree of cellular necrosis were much lower in the case of apathogenic virus. After adsorption to mouse neuroblastoma cells, apathogenic virus was less rapidly internalized than pathogenic virus, and cell-to-cell spread of apathogenic variant virus was completely prevented by the addition of rabies virus-neutralizing antibody, whereas the spread of pathogenic virus was not affected.

Antigenic sites on the ERA rabies virus nucleoprotein and non-structural protein.

Thirty-one monoclonal antibodies, specific for either the nucleoprotein (N) or the non-structural protein (NS; nucleocapsid-associated protein) of the nucleocapsid of the ERA strain of rabies virus, were used to investigate the topography of antigenic sites on the nucleocapsid complex. Based on the results of a competitive enzyme immunoabsorbent assay using these antibodies, five spatially distinct antigenic sites were defined: three on the N protein (groups N I, N II and N III) and two on the NS protein (groups NS I and NS II). Antigenic variations among various street and laboratory strains of rabies virus were analysed by indirect immunofluorescence assay with the monoclonal antibodies specific for the nucleocapsid.

Antigenic variants of rabies virus in isolates from eastern, central and northern Canada.

Street rabies virus isolated from 51 specimens from Ontario, Quebec, Manitoba and the Northwest Territories have been typed by a panel of 36 antinucleocapsid monoclonal antibodies. Three main groups were found. The first group comprised those terrestrial mammals originating in Ontario, Quebec and the Northwest Territories.

Expression of rabies virus glycoprotein from a recombinant vaccinia virus.

Rabies is one of the oldest diseases know to man, but its successful control has remained elusive. Although effective vaccines of tissue culture origin against rabies do exist, such preparations are expensive. Live vaccinia virus (VV) recombinants expressing influenza or hepatitis B antigens have recently been used to immunize against these diseases.

T cell responses to cleaved rabies virus glycoprotein and to synthetic peptides.

The antigenic structure of the rabies virus glycoprotein has been studied. A limited number of fragments were obtained by cyanogen bromide (CNBr) cleavage of viral glycoprotein, and eight large peptides were isolated by using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. These were tested for their capacity to stimulate the proliferation of nylon wool-purified T cells obtained from spleens of rabies-immune A/J mice.

Protection from rabies by a vaccinia virus recombinant containing the rabies virus glycoprotein gene.

Inoculation of rabbits and mice with a vaccinia-rabies glycoprotein recombinant (V-RG) virus resulted in rapid induction of high concentrations of rabies virus-neutralizing antibodies and protection from severe intracerebral challenge with several strains of rabies virus. Protection from virus challenge also was achieved against the rabies-related Duvenhage virus but not against the Mokola virus. Effective immunization by V-RG depended on the expression of a rabies glycoprotein that registered proline rather than leucine as the eighth amino acid from its NH2 terminus (V-RGpro8).

Use of monoclonal antibodies to confirm vaccine-induced rabies in ten dogs, two cats, and one fox.

A panel of 8 monoclonal antibodies to rabies glycoprotein antigen was used to characterize the modified-live virus vaccines marketed in the United States during the last 10 years. Thirteen of 14 rabies virus isolates from 11 dogs, 2 cats, and 1 fox suspected of developing vaccine-induced rabies were shown to have reactivity patterns that were identical to the vaccine administered. Reactivity patterns for 20 rabies isolates from human beings, wild animals, or domestic animals with no history of recent vaccination with modified-live virus rabies vaccine were different from those obtained for vaccines.

Antigenic analysis of rabies and Mokola virus from Zimbabwe using monoclonal antibodies.

Eighteen strains of virus were recovered by tissue culture techniques from 20 samples of mouse brain received from Harare, Zimbabwe, and typed with monoclonal antibodies at The Wistar Institute. On the basis of reactivity with these monoclonal antibodies specific for rabies and rabies-related viruses, seven strains were identified as Mokola viruses, and the remaining 11, as rabies viruses. Seventeen of 36 monoclonal antibodies against the nucleocapsid antigen reacted with the Mokola strains, but none of 42 monoclonal antibodies against the glycoprotein that neutralized rabies virus was active against Mokola strains.

Anti-idiotypic antibodies induce neutralizing antibodies to rabies virus glycoprotein.

Rabbit anti-idiotypic antibodies (alpha Id Ab) were prepared against five murine monoclonal antibodies (mAb) specific for the rabies virus glycoprotein. Four of the mAb were directed against three known, type-specific, neutralizing sites on the glycoprotein, and the other mAb was directed against a topographically uncharacterized, nonneutralizing epitope. An absence of significant cross-reactivity among the alpha Id Ab for heterologous mAb suggested that the alpha Id Ab were highly specific for unique variable region determinants.

Epidemiologic analysis of antigenic variations of street rabies virus: detection by monoclonal antibodies.

The nucleocapsid antigen of 204 strains of street rabies virus, which originated in Europe, Africa and Asia, was analyzed by fluorescent antibody staining technique with a panel of 20 monoclonal antibodies specific for nucleocapsid of rabies and rabies-related viruses. A definite pattern of reactivity was observed with strains of the same geographic origin with the exception of strains originating from Madagascar, Thailand and Iran which were more diversified. Mice immunized with a vaccine prepared from a Pasteur PV-11 strain of virus were well protected against challenge with representative strains from Europe and Africa, and a partial protection was observed following challenge with strains from Madagascar and Thailand.

Antigenic sites on the CVS rabies virus glycoprotein: analysis with monoclonal antibodies.

Antigenic variation in the glycoprotein of rabies (CVS-11) virus was studied. Neutralization-resistant variant viruses were isolated in vitro at high frequency (10(-4) to 10(-5)) in the presence of anti-glycoprotein monoclonal antibody. Analysis of these variants identified at least three functionally independent antigenic sites, based on the grouping of variants that were no longer neutralized by one or more of a panel of 24 monoclonal antibodies.

Chemical and immunological analysis of the rabies soluble glycoprotein.

Soluble glycoprotein (Gs), purified from virion-depleted, rabies-infected tissue culture fluid, was chemically and immunologically analyzed. A comparison of this antigen with the virion-associated glycoprotein showed that Gs lacks 58 amino acid residues from the carboxy terminus of the virion-associated glycoprotein. Analysis with monoclonal antibodies revealed that all the epitopes of the viral glycoprotein are also present in the soluble glycoprotein.

Characterization of an antigenic determinant of the glycoprotein that correlates with pathogenicity of rabies virus.

The pathogenicity of fixed rabies virus strains for adult mice depends on the presence of an antigenic determinant on the viral glycoprotein. Two virus-neutralizing monoclonal antibodies have been used to identify this determinant. All pathogenic strains of fixed rabies virus bind to these antibodies and are neutralized by them, whereas nonpathogenic strains fail to react with these monoclonal antibodies and are not neutralized by them.