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PubMed1990

Paget's disease of bone and previous pet ownership in the United States: dogs exonerated.

Paget's disease of bone is currently believed to be the result of a paramyxovirus infection of osteoclasts. Previously reported immunohistological data have suggested that a virus resembling either the measles virus or a respiratory syncytial virus is the probable causative agent, but no organism has been isolated or definitively identified to date. A recent study reporting an increased exposure to dogs during childhood and adolescence in a small series of cases from the North West of England proposed that a canine virus, possibly distemper, might be the primarily infectious agent. To study this hypothesis further, we examined prior dog and cat ownership from childhood through adulthood in 433 cases of Paget's disease and an equal number of matched controls living in the US. We found no differences related to prior pet ownership. We conclude that past dog (or cat) ownership is not a risk factor for the development of Paget's disease.

Adolescent↗
PubMed2005

Veterinary immunology as colonial science: method and quantification in the investigation of horsesickness in South Africa, C. 1905-1945.

This article examines the practice of veterinary immunology in South Africa during the first half of the twentieth century through an analysis of research into a horsesickness vaccine at the Onderstepoort Veterinary Institute. From the early 1900s, Arnold Theiler prioritized research into horsesickness, by then defined as an insect-borne disease caused by an ultravisible virus. He succeeded in devising a means of prophylaxis using a simultaneous injection of infective blood and immune serum, but he discovered antigenically different strains of the virus, which could overcome the immunity produced by his treatment. The practical value of Theiler's methods was further limited by difficulties in standardizing the biological material used in immunization, the results of which remained too erratic for application on a large scale. No further advances were made until the 1930s, by which time Onderstepoort had been drawn more closely into international scientific networks. Using techniques derived from research into yellow fever in America and canine distemper in Britain, the Onderstepoort scientist Raymond Alexander invented a method of immunization that utilized the propagation of the horsesickness virus in the brains of mice. Alexander's methods, which were characterized by successful technical adaptation and innovation, depended upon methods of quantification first developed by Paul Ehrlich to standardize diphtheria antitoxin during the 1890s. During the 1940s, vaccination expanded rapidly in South Africa, and Onderstepoort later exported the vaccine and associated technology to other countries affected by horsesickness.

Academies and Institutes↗
PubMed2001

Infectobesity: obesity of infectious origin.

In the U.S., the prevalence of obesity increased by 30% from 1980 to 1990, and this increase appears to be continuing. Although obesity has multiple etiologies, an overlooked possibility is obesity of an infectious origin. Six pathogens are reported to cause obesity in animals. Canine distemper virus was the first virus reported to cause obesity in mice, followed by Rous-associated virus-7, an avian retrovirus, which has been shown to cause stunting, obesity and hyperlipidemia in chickens. Next, the obesity-promoting effect of Borna disease virus was demonstrated in rats. Scrapie agents were reported to induce obesity in mice and hamsters. The final two reports were of SMAM-1, an avian adenovirus, and Ad-36, a human adenovirus that caused obesity in animals. Additionally, an association with human obesity is the unique feature of SMAM-1 and Ad-36. Although the exact mechanism of pathogen-induced obesity is unclear, infection attributable to certain organisms should be included in the long list of potential etiological factors for obesity. In addition, the involvement of some pathogens in etiology of obesity suggests the possibility of a similar role for additional pathogens.

Animals↗
PubMed2003

Supplementation of food with Enterococcus faecium (SF68) stimulates immune functions in young dogs.

The gut microflora play a crucial role in several physiologic functions of the host, including maturation of the gut-associated lymphoid tissues during the first months of life. Oral administration of probiotic lactic acid bacteria (LAB) modulates the immune system of humans and some laboratory animals. This effect has never been examined in dogs; therefore, our aim was to study the capacity of a probiotic LAB to stimulate immune functions in young dogs. Puppies were allotted to two groups receiving either a control diet or a diet supplemented with 5 x 10(8) colony forming units (cfu)/d of probiotic Enterococcus faecium (SF68) from weaning to 1 y of age. Fecal and blood samples were collected from the dogs at different time points for the measurement of fecal immunoglobulin (Ig)A, circulating IgG and IgA, and the proportions of lymphoid cell subsets. Fecal IgA and canine distemper virus (CDV) vaccine-specific circulating IgG and IgA were higher in the group receiving the probiotic than in controls. There were no differences in the percentages of CD4(+) and CD8(+) T cells between the groups, but the proportion of mature B cells [CD21(+)/major histocompatibility complex (MHC) class II(+)] was greater in those fed the probiotic. These data show for the first time that a dietary probiotic LAB enhance specific immune functions in young dogs, thus offering new opportunities for the utilization of probiotics in canine nutrition.

Animal Feed↗
PubMed1986

Nucleotide sequence of the gene encoding the matrix protein of Newcastle disease virus.

The nucleotide sequence of the gene encoding the matrix (M) protein of the Beaudette C strain of Newcastle disease virus (NDV) has been determined from overlapping cDNA clones. Control sequences typical of paramyxovirus mRNA start and polyadenylation signals have been identified. Assuming that the M gene starts and finishes at these sequences, the M gene is 1241 nucleotides long and encodes one long open reading frame of 364 amino acids, corresponding to a polypeptide of molecular weight 39605, in good agreement with estimates from SDS gels. The M protein has an amino acid sequence that is both hydrophobic and highly basic. The NDV M protein has sequence homologies to the M proteins of Sendai, measles, canine distemper and respiratory syncytial viruses.

Amino Acid Sequence↗
PubMed2004

Search for morbillivirus proteins in multiple sclerosis brain tissue.

We investigated brain samples of patients with multiple sclerosis (MS) and controls with immunohistochemistry using monoclonal antibodies (MoAbs) against canine distemper virus (CDV) and measles virus (MV) proteins. All stained negative except for MoAb F3-5, which recognises a conserved epitope on the fusion protein of morbilliviruses. F3-5 immunostaining was found in 8/9 MS plaques and 2/5 herpes simplex virus encephalitis brain samples, but not in six controls or four patients with ischaemic stroke. Using RT-PCR we found no evidence for the presence of MV in MS plaques. The F3-5 epitope may represent a protein that is upregulated during inflammation or point to a yet unrecognised morbillivirus in the human central nervous system that might be implicated in MS pathogenesis.

Adult↗
PubMedDate not supplied

Urogranoic acid as a radiopaque additive to the cyanoacrylic adhesive in transcatheter obliteration of renal arteries.

The purpose of the investigation was to study the application of radiopaque materials to the tissue adhesive base of the ester of n-butylic-alpha-cyanoacrylic acid for use in direct transcatheter renal artery obliteration. Lipiodol Ultra-fluid (Ethiodol) and urogranoic acid in quantities of 30--55% by weight of the adhesive were used as the radiopaque agents. The study was performed on seven dogs; obliterative material was administered through a telescopic, coaxial catheter system. Two dogs treated with the Lipiodol adhesive material died, which confirmed the inefficacy of Lipiodol for this purpose. In the other five dogs, treated by adding urogranoic acid to the adhesive, complete and permanent occlusion occurred and the adhesive remained radiopaque for 60--90 days. One of these dogs died of canine distemper infection. The complication of unpredictable embolization of the femoral artery appeared in a second dog. The same material has been used in two cases of nonoperative hypernephroma in humans. Permanent occlusion of the renal artery and elimination of hematuria were achieved. The obliterative material was sufficiently opaque for radiographic visualization.

Adenocarcinoma↗
PubMed1979

Morphology and morphogenesis of a new paramyxovirus (PMV 107).

The morphology of the virions and nucleocapsids of paramyxovirus 107 (PVM 107) and the replication of the virus were investigated by electron microscopy. The virions and nucleocapsids exhibited the same structural properties as other paramyxoviruses. Nuclecapsids were found in the nucleus and cytoplasm of infected bovine embryonic lung (BEL) cell cultures. A similar situation has been described for the morbilliviruses measles, SSPE, distemper and rinderpest. Alignment of nucleocapsids beneath the plasma membrane and budding of PMV 107 in the productive BEL cell infections were also similar to the morbillivirus-infected cells. In a line of monkey cells (CV1) persistently infected with PMV 107 only cytoplasmic nucleocapsids could be demonstrated. On the basis of its morphology and morphogenesis it is suggested that PMV 107 should be classified as a paramyxovirus. Since nucleocapsids could also be found in the nucleus of infected BEL cells the morphogenesis of PMV 107 closely resembles that of viruses of the morbillivirus group.

Animals↗
PubMed1980

Radioimmunoassay of measles virus nucleocapsid antigen.

A double antibody competitive binding radioimmunoassay (RIA) was developed as a tool for investigating the involvement of measles virus in persistent virus infections. The assay employs 125I-labelled measles virus nucleocapsids as the labelled antigen. Nucleocapsids were purified from cytoplasmic extracts of virus-infected Vero cells, treated with trypsin to prevent clumping and iodinated to a specific activity of about 15 microCi/microgram. Electrophoretic analysis of iodinated trypsin-treated nucleocapsids revealed only labelled polypeptide with a relative mol. wt. (Mr) 40 000, indicating that trypsin had cleaved the 60 000 mol. wt. native polypeptide to a 40 000 mol. wt. subunit. The assay could detect as little as 0.1 ng of nucleocapsid protein. Either native (Mr 60 000) or cleaved Mr 40 000) nucleocapsid polypeptide was detected in the assay. As much as 100 micrograms of protein from uninfected Vero cells did not react in the RIA. Another measure of specificity was the fact that 400 ng of purified nucleocapsid protein from simian virus 5, Newcastle disease virus or canine distemper virus did not react in the assay. In the RIA, nucleocapsid antigen of virus isolated from subacute sclerosing panencephalitis (SSPE) was indistinguishable from that of Edmonston strain measles virus, indicating antigenic homology between the 40 000 mol. wt. nucleocapsid polypeptide of the SSPE virus and that of measles virus.

Animals↗
PubMed1981

Monoclonal antibodies against measles virus.

Monoclonal antibodies were produced in vitro by fusing mouse myeloma cells (SP2) with spleen cells derived from Balb/c mice immunized with purified measles virus. Fifteen independent hybrid cell lines, isolated from two separate fusions, were maintained in culture for up to 5 months without loss of their antibody-secreting activity. Radioimmunoprecipitation and polyacrylamide gel electrophoresis showed that in five of the hybrid lines the antibodies were directed against haemagglutinin, in two against the nucleoprotein, and in one against L protein. The remaining seven hybridomas did not precipitate viral antigens under the experimental conditions employed even though they gave positive immunofluorescence against measles virus-infected cells. Monoclonal haemagglutinin antibodies displayed anti-haemagglutinating activity and neutralized measles virus infectivity but not canine distemper virus (CDV).

Antibodies, Monoclonal↗
PubMed1984

Immunoassays for measles virus nucleocapsid antigen: effect of antigen-antibody complexes.

An inhibition radioimmunoassay and a two-site immunoradiometric (four-layer) assay for the quantification of measles virus nucleocapsid antigen were established and their sensitivities compared. Both assays exhibited threshold sensitivities of from 1 to 10 ng nucleocapsid antigen per ml. Concentrations of reagents used in the assays were shown to be an important factor determining the sensitivities of the assays. Purified mumps or parainfluenza 2 virus nucleocapsids did not compete with measles virus nucleocapsids in the inhibition assay but some degree of cross-reactivity with canine distemper virus nucleocapsid was observed. Pretreatment of virus-infected cells with detergent had a significant effect on the amount of antigen detectable by the assays. SDS greatly decreased the reactivity of measles virus nucleocapsid but Triton X-100 and, to a larger degree, sodium deoxycholate released antigen from the cells in quantities greater than that detected when no detergent pretreatment was employed. Complexing of antibodies to measles virus nucleocapsids in vitro decreased dramatically the threshold sensitivity of the nucleocapsid assays. The antigen-antibody complexes could be disrupted and the components separated but the conditions employed destroyed 90% of the antigenic reactivity of the nucleocapsid and also had a deleterious effect on the antibody. Nucleocapsid antigen was readily detected in brains from hamsters with acute measles encephalitis. The assays, however, were not sensitive enough for routine detection of antigen in brains from hamsters with chronic measles encephalitis.

Animals↗
PubMed1986

Complete sequence of the major nucleocapsid protein gene of human parainfluenza type 3 virus: comparison with other negative strand viruses.

The sequence of the major nucleocapsid protein (NP) mRNA and its encoded protein were deduced by sequencing a cDNA clone representing the complete mRNA. The cDNA sequence was confirmed by dideoxynucleotide sequencing of purified viral genomic RNA by primer extension using synthetic oligonucleotides. The NP mRNA contains 1,641 nucleotides exclusive of poly(A) and encodes an NP protein of 515 amino acids. Alignment of the human parainfluenza type 3 virus (PF3) NP protein sequence with that of Sendai virus showed that the two proteins shared considerable sequence identity (58.8%). Additional comparisons provided highly significant statistical evidence that the PF3 NP protein sequence is related to those of measles and canine distemper viruses, but there was no evidence of relatedness with the nucleocapsid proteins of respiratory syncytial virus, influenza B virus, or vesicular stomatitis virus.

Amino Acid Sequence↗
PubMed1987

Sequence analysis of the matrix protein gene of human parainfluenza virus type 3: extensive sequence homology among paramyxoviruses.

The sequences of the human parainfluenza virus type 3 (PIV3) matrix (M) mRNA [1150 nucleotides exclusive of poly(A)] and predicted M protein (353 amino acids) were determined by sequence analysis of cloned cDNA and viral genomic RNA. The gene-end sequence of the M gene differed from the semi-conserved gene-end sequence of the other PIV3 genes by an apparent insertion of eight nucleotides. The PIV3 M protein shared high sequence homology with Sendai virus and moderate homology with measles virus and canine distemper virus. Statistical analysis of the available sequences showed that the M protein was the most highly conserved parainfluenza viral protein.

Amino Acid Sequence↗
PubMed1987

Comparison of proteins induced in cells infected with rinderpest and peste des petits ruminants viruses.

The two morbilliviruses rinderpest virus (RPV) and peste des petits ruminants virus (PPRV) are closely related and cause severe disease in large and small ruminants, respectively. They show distinct epidemiological patterns and are distinguishable by reciprocal cross-neutralization tests. We have analysed the proteins induced by these viruses in infected cells and have shown that they can be distinguishable by a very marked difference in the apparent mol. wt. of the nucleocapsid (N) protein. The N protein of PPRV is almost identical in mobility on polyacrylamide gels to the N proteins of measles virus and canine distemper virus (60K). Several strains of RPV and PPRV from widespread geographical locations were studied and found to show this difference in the N protein.

Antibodies, Monoclonal↗
PubMed1988

Parainfluenza virus type 2 haemagglutinin-neuraminidase glycoprotein characterized with monoclonal antibodies.

Thirteen monoclonal antibodies (MAbs) were prepared against human parainfluenza virus type 2 (PIV2). These MAbs reacted with the haemagglutinin-neuraminidase glycoprotein with an Mr of 84K. The MAbs defined one antigenic site which could be divided into five epitopes. A correlation between haemagglutination inhibition (HI) and neutralization activity could be seen although one MAb, which recognized a distinct epitope, showed neutralization and no HI activity to PIV2. The reactivity of the MAbs was tested against Sendai virus, parainfluenza virus type 3, simian virus 5 (SV5), mumps virus, Newcastle disease virus, measles virus and canine distemper virus. Only one MAb showed any cross-reaction with a low HI titre to SV5.

Antibodies, Monoclonal↗
PubMed1989

Characterization of monoclonal antibodies against four structural proteins of rinderpest virus.

Twenty-four monoclonal antibodies (MAbs) against rinderpest virus (RPV) were established and characterized by several serological tests. Of the 24 MAbs. 10 recognized the nucleoprotein (NP), six the phosphoprotein (P), four the haemagglutinin (H), and two the fusion (F) protein as determined by radioimmunoprecipitation assay. The specificities of the remaining two MAbs could not be determined. From a competitive binding assay using MAbs against each structural protein, at least five, four and two separate antigenic sites were identified on the NP, P and H proteins, respectively. MAbs against the H protein neutralized the infectivity of the virus, but those against the F protein were only neutralizing in the presence of guinea-pig complement. The reactivities of each of the MAbs for other strains of morbillivirus were tested using an indirect immunofluorescent antibody assay. The MAbs against four out five antigenic sites on the NP showed cross-reactivity amongst all the strains of morbillivirus tested whereas the fifth antibody reacted only with RPV. Of the antibodies specific for the P protein, the antibody against one site was cross-reactive with all the strains of RPV, measles virus (MV) and canine distemper virus (CDV), the antibody against another site was reactive with RPV and MV but not with CDV, and the antibodies against the other two sites were specific for RPV.

Antibodies, Monoclonal↗
PubMed1991

Antigenic and functional characterization of rinderpest virus envelope proteins using monoclonal antibodies.

A total of 24 monoclonal antibodies (MAbs) against the haemagglutinin (H) and the fusion protein (F) of rinderpest virus (RPV) were used to characterize their antigenic structure and biological properties, and to analyse natural variation in the envelope proteins of morbilliviruses. The anti-H and anti-F MAbs defined seven and three distinct antigenic sites, respectively. The MAbs to six sites on H were able to neutralize the infectivity of RPV. The addition of guinea-pig complement or anti-mouse immunoglobulin increased the virus-neutralizing antibody titre of most of the anti-H MAbs, including those lacking neutralizing activity. One of the antigenic sites on H was conserved among morbilliviruses and the MAbs to this site had haemagglutination inhibition activity against measles virus (MV). The remaining sites were specific for RPV and varied antigenically between strains of RPV. The anti-F MAbs lacked neutralizing activity, but two of the five MAbs did show activity in the presence of complement or anti-mouse immunoglobulin. On the whole, the antigenic sites on F were conserved in some strains of MV, but not in canine distemper virus. All of the sites on the surface proteins were sensitive to SDS and, although those on F were not affected by 2-mercaptoethanol, five of the seven sites on H were destroyed by it. These results suggest that the epitopes on the envelope proteins are conformation-dependent.

Animals↗
PubMed1993

Characterization of morbilliviruses isolated from dolphins and porpoises in Europe.

A previously unidentified morbillivirus was isolated from two harbour porpoises (Phocoena phocoena) that had died in the Dutch Waddensea (North Sea) in 1990. This porpoise morbillivirus (PMV) and a dolphin morbillivirus (DMV), which had recently caused a heavy mortality in Mediterranean striped dolphins (Stenella coeruleoalba), were compared antigenically with other members of the genus Morbillivirus, including the newly recognized phocine distemper virus type 1. DMV and PMV proved to be similar but distinct morbillivurses, closely related to rinderpest virus and peste-des-petitsruminants virus. Cell cultures of cetacean, pinniped, ruminant and canine origin showed a different pattern of susceptibility to DMV and PMV infection. Ruminants and dogs proved to be susceptible to experimental infection with DMV and PMV, which both caused a transient leukopenia most pronounced in the ruminants. Pre-exposure of dogs to DMV and PMV protected them from developing CDV viraemia and clinical signs upon challenge infection with virulent CDV. A serological survey among stranded animals of different cetacean species in Europe indicated that infections with DMV- and PMV-like morbilliviruses are not uncommon among these aquatic mammals.

Animals↗