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Biomedical subjects

M Ackermann

Publications and source records attributed to M Ackermann.

At least 109 records · Page 6Linked to original sources
PubMed1989

[Serologic and virologic studies of selected cattle with antibodies to bovine herpesviruses].

In order to investigate the specificity of low titer antibodies to BHV 1, twelve cattle were subjected to stress and dexamethasone treatment. They were monitored virologically by inoculating cell cultures with naso-pharyngeal-, ocular- and vaginal- or preputial swabs and serologically by assessing the prevalence and incidence of antibodies to bovine, caprine-, porcine-, and equine herpesviruses and to bovine leukemia virus. Antibodies were classified as specific for BHV 1 if the animals excreted IBR virus, or if the antibodies neutralized BHV 1 and reacted with BHV 1 antigens, or if they reacted additionally with CapHV antigens. Animals whose sera recognized BHV 1 and BHV 2 but not other herpesviruses, were judged to have experienced both infections. Nine of the twelve animals had specific BHV 1 antibodies. With three animals the question for specificity of their antibodies remains open. Two animals experienced several herpesvirus infections. Therefore, the induction of crossreacting antibodies, directed against epitopes common to herpesviruses, could not be ruled out. The sera of one animal reacted with BHV 1 and BHV 4 antigens in ELISA tests. They did, however, not neutralize BHV 1.

Animals↗
PubMed1989

[The effectiveness of foot-and-mouth disease vaccines in Switzerland. I. Screening tests and herd immunity].

Protection of the Swiss national cattle herd against foot-and mouth disease is attempted by annual vaccination with inactivated trivalent (O, A, C) vaccines. With the serotype A5 as an example, this paper demonstrates the procedure of potency testing. Serological data obtained with two vaccines in primovaccinated feeder bulls showed that neutralizing antibodies developed within 7 to 14 days post vaccination. There was no statistically significant difference in the anti-serotype antibody titers induced by each of the vaccines; differences were seen between anti-O serotype and anti-A serotype antibody titers, regardless of which vaccine was used. Epidemiological analyses with about 3000 cattle demonstrated that single-vaccinated, and to a lesser degree twice-vaccinated, animals often had short lived immunity; that is, the antibody titers waned within a few months. In contrast, the majority of thrice and multiple vaccinated animals maintained relatively high antibody titers throughout the twelve month period of observation.

Animals↗
PubMed1989

[The effectiveness of foot-and-mouth disease vaccines in Switzerland. II. Stability problems].

One of the vaccines that were used in 1988 to immunize the Swiss national cattle population against foot-and mouth disease (FMD) was apparently not stable. Data, provided by the manufacturer, indicated a high initial antigenic content for serotype O. Protection experiments at the end of the vaccination campaign, however, indicated a substantial loss of serotype O antigen in the vaccine. Serological data, obtained during the campaign indicated that only 12% of the primovaccinated animals and 63% of previously vaccinated animals received an amount of FMD viral antigen sufficient to induce protective immunity. The primovaccinated animals were revaccinated in fall 1988 with a new batch provided by the same manufacturer. The new vaccine induced high titers of neutralizing antibodies in primo- and an anamnestic response in revaccinated cattle.

Animals↗
PubMed1989

[The control of infectious bovine rhinotracheitis (IBR) in Switzerland from 1978 to 1988].

The eradication of Infectious bovine rhinotracheitis/Infectious pustular vulvovaginitis (IBR/IPV) in Switzerland is reviewed. In 1978 IBR was reported in dairy cattle in the Eastern part of Switzerland. No preexisting eradication program was available at that time. In 1983, following a period of hesitation, the legal basis for the eradication of IBR was issued. This aim was achieved by: i) Controls and restrictions of the traffic of susceptible animals in order to prevent further transmission of IBR. ii) Slaughter of seropositive cattle, based on the assumption that animals with antibodies to BHV 1 were virus carriers and therefore an IBR-virus-reservoir. iii) The fact that besides the cattle population no BHV 1 reservoir existed in Switzerland. iv) Never licensing IBR-vaccines because they were not able to prevent the infection and the establishment of latency. The costs of the eradication program amounted to approx. SFr. 114,000,000. A total of 51,911 animals were slaughtered in order to eradicate IBR. An amount of SFr. 5,000,000 per annum is estimated to be necessary in order to maintain the favourable situation concerning IBR. In the future, the experience concerning IBR is applied for the prevention and control of other infectious diseases in the Swiss cattle population.

Animals↗
PubMed1988

Reduction of the number of mice used for potency testing of human and animal rabies vaccines.

Eight different rabies vaccines were tested for their potency in the standard mouse potency test using 3-, 5- and 7-week-old mice. 5-week-old mice seem to be best suited for this purpose, variability from test to test could be reduced considerably. An ELISA was used in parallel for the evaluation of the rabies glycoprotein content of rabies vaccines. Results of the mouse potency test correlated well with those of the ELISA if highly purified human vaccines were tested. Unspecific reactions in the ELISA caused by adjuvanted veterinary vaccines could not be blocked. Further experiments will be needed in order to evaluate the potency of inactivated veterinary rabies vaccines by a in vitro test.

Aging↗
PubMed1988

Acute fibrinopurulent blepharitis and conjunctivitis associated with Staphylococcus hyicus, Escherichia coli, and Streptococcus sp. in chickens and turkeys.

Multiple outbreaks of acute severe fibrinopurulent lesions of the eyelids occurred in chickens and turkeys. Lesions began as tiny foci of epidermal necrosis and ulceration and spread to involve the entire eyelid. Scabs overlying the epidermis contained large gram-positive cocci; lesser numbers of small cocci and gram-negative bacilli were in more superficial areas. Staphylococcus hyicus was isolated from birds in all stages of the disease. Escherichia coli and Streptococcus sp. were isolated only during severe stages; no anaerobic bacterial pathogens were isolated. Vasculitis and perivascular lymphocytic infiltrates in deep layers of the dermis suggested that a staphylococcal toxin may have been involved. The disease was not reproduced by scarifying S. hyicus onto the eyelids or by intravenous inoculation of retrovirus-infected chickens.

Animals↗
PubMed1987

Conserved antigenic and functional domains on glycoprotein B of herpes simplex virus 1 and bovine herpesvirus 2. Brief report.

A panel of monoclonal antibodies to glycoprotein B (gB) of herpes simplex virus 1 (HSV-1) reacted in immune precipitation and in immunofluorescence tests with a glycoprotein 130,000 in apparent molecular weight specified by bovine herpesvirus 2 (BHV-2). Two cross reactive antibodies neutralized the heterologous virus. These results suggest that the BHV-2 glycoprotein is the homologue of HSV-1 gB and shares structural and functional domains expressed on the gB gene product.

Antibodies, Monoclonal↗
PubMed1987

Cell type dependence of herpes simplex virus gene expression and of processing of viral protein.

R325, a recombinant virus constructed from the wild type herpes simplex virus 1 strain F [HSV-1(F)] carries a 500 bp deletion in the alpha 22 gene. Both viruses are temperature sensitive for growth and late gene expression in HEp-2 cells. To determine the properties of alpha 22 protein and to identify the product of the non deleted 5' portion of the alpha 22 gene in R325, infected BHK and HEp-2 cells incubated at permissive and non-permissive temperatures were electrophoretically separated in denaturing polyacrylamide gels, electrically transferred to a nitrocellulose sheet and reacted with rabbit polyclonal antibody to an oligopeptide synthesized according to the predicted aminoacid sequence of the 5' terminus of alpha 22. The results were as follows: the authentic alpha 22 protein was detected in infected BHK and HEp-2 cells maintained at either 34 degrees C (permissive) or 39 degrees C (non-permissive) temperatures, the truncated protein specified by R325 accumulated at 39 degrees C but not at 34 degrees C. Furthermore, the proteins made in BHK cells were processed to higher apparent molecular weights and formed several bands in contrast to the single band formed by the protein made in HEp-2 cells; the temporal pattern of expression of HSV-1(F) and R325 at the 39 degrees C was more advanced in BHK cells than in HEp-2 cells. Specifically, in BHK cells at the non-permissive temperature alpha protein synthesis was shut off earlier and gamma proteins not made in infected HEp-2 cells were detected. These studies suggest that folding of viral proteins may be in part cell dependent and either compensate or exacerbate the effects of mutations in specific genes.

Animals↗
PubMed1986

Identification, properties, and gene location of a novel glycoprotein specified by herpes simplex virus 1.

We report the identification of a novel herpes simplex virus 1 (HSV-1) glycoprotein reactive with type specific monoclonal antibody H1379. The monoclonal antibody reacted with two broad bands with apparent mol wt of 60K to 68K and 44K to 48K formed by infected cell lysates subjected to electrophoresis in denaturing polyacrylamide gels and electrically transferred to a nitrocellulose sheet. Early in infection the H1379 reactive protein was found in the faster migrating band. The rate of accumulation was highest late in infection and only the slower migrating form incorporates significant amounts of glucosamine. The epitopic site recognized by H1379 was not uniformly distributed among strains. Analyses of HSV-1 X HSV-2 recombinants with monoclonal antibodies to HSV-1 and HSV-2 glycoproteins mapping in the S component of the HSV genomes and marker transfer experiments indicated that the gene specifying the H1379 reactive protein maps within BamHI fragment J to the left of gD most probably within the open reading frame designated as US4 (D. J. McGeoch, A Dolan, S. Donald, and F. J. Rixon, 1985, J. Mol. Biol. 181, 1-13). The gene specifying a recently discovered HSV-2 glycoprotein designated as gG-2 (B. Roizman, B. Norrild, C. Chan, and L. Pereira, 1984, Virology 133, 242-247) maps in the corresponding domain of the HSV-2 genome and marker transfer experiments suggest that the H1379 reactive protein and gG-2 are collinear. We have therefore designated the novel HSV-1 glycoprotein as gG-1.

Antibodies, Monoclonal↗
PubMed1986

Transmission of IBR/IPV virus in bovine semen: A case report.

The transmission of IBR/IPV virus in imported semen is reported. Some of the inseminated animals showed seroconversion and, in accordance with Swiss law, had to be eliminated. To avoid such cases in international sperm exchange, methods of detecting IBR/IPV virus need to be improved. In the longer term, AI centres must be established in which all bovine stock is seronegative for IBR/IPV.

Journal Article↗
PubMed1986

Human antibody response to herpes simplex virus-specific polypeptides after primary and recurrent infection.

Human antibody responses to specific polypeptides of herpes simplex virus types 1 and 2 (HSV-1 and HSV-2, respectively) were assessed in serial serum specimens from 18 infected patients by immunoblot technology. Nine patients had HSV-1 infections (six genital and three oral) and nine had HSV-2 genital infections. Antibodies to homologous and heterologous HSV antigens were studied and correlated with total microneutralization and enzyme-linked immunosorbent assay antibodies as well as correlated directly to purified glycoproteins. The data indicated a sequential appearance of antibodies to specific polypeptides, according to virus type and site of infection. After HSV-1 infection, the initial response was to glycoprotein B, but the same was not true for HSV-2 infection, where the initial response appeared to be to the type-specific glycoprotein G. A difference in sequential appearance of antibodies for the two viruses indicated greater reactivity to lower-molecular-weight polypeptides after genital infection, irrespective of type, in contrast to nongenital HSV-1 infections. The antibody responses for selected sera to purified glycoproteins B and D were verified by enzyme-linked immunosorbent assay antibody determinations.

Antibodies, Viral↗
PubMed1986

Identification by antibody to a synthetic peptide of a protein specified by a diploid gene located in the terminal repeats of the L component of herpes simplex virus genome.

In the course of studies on the a sequences located at the termini of and at the junction between the L and S components of herpes simplex virus 1 DNA, J. Chou and B. Roizman (J. Virol. 57:629-637, 1986) noted that the a sequence acted as a gamma 1 promoter when fused to the structural sequence of the thymidine kinase gene, the b inverted repeat sequences located in the L component next to the a sequences contained an open reading frame predicted to encode the protein of 358 amino acids with a molecular weight of 37,054, and the transcription of an RNA homologous to the open reading frame initiated within the a sequence. The nucleotide sequence of the open reading frame predicted the presence of the triplet Ala-Thr-Pro repeated 10 times. To verify the existence of the predicted gene, designated gamma 134.5, a synthetic peptide consisting of the triplet Ala-Thr-Pro repeated 10 times was synthesized and used to raise antibodies in rabbits. The results were as follows. The antiserum to the peptide reacted with a 43,500-apparent-molecular-weight protein present in lysates of cells infected with herpes simplex virus 1 but not present in mock-infected or herpes simplex virus 2-infected cells. We genetically engineered a recombinant virus containing a single copy of a truncated gene. Concordant with predictions, the antibody reacted with a faster-migrating protein in cells infected with this recombinant. The gamma 134.5 gene product was soluble, and it accumulated primarily in the cytoplasm late in infection. The overlap of the domain of the gamma 134.5 gene with the a sequence raises the possibility that it acts in trans on the a sequence and is associated with one of the functions currently ascribed to the a sequences.

Amino Acid Sequence↗
PubMed1986

Construction and properties of a viable herpes simplex virus 1 recombinant lacking coding sequences of the alpha 47 gene.

The five alpha genes, alpha 0, alpha 4, alpha 22, alpha 27, and alpha 47, are the first set of herpes simplex virus 1 genes to be transcribed and expressed in productively infected cells. We report here the construction of a viral recombinant from which all of the coding sequences of the alpha 47 gene were deleted. In addition to the alpha 47 protein, infected cell lysates did not contain detectable amounts of two polypeptide bands with apparent molecular weights of 18,000 and 21,000 which could be specified by a gene whose regulatory domain and 5' transcribed noncoding sequences overlap with the coding sequences of the alpha 47 gene. The alpha 47- virus grew as well as the wild-type parent virus in Vero, baby hamster kidney, and Rat-1 cell lines.

Animals↗
PubMed1986

Transcription initiation sites and nucleotide sequence of a herpes simplex virus 1 gene conserved in the Epstein-Barr virus genome and reported to affect the transport of viral glycoproteins.

Earlier reports have localized mutations which affect the processing and transport of herpes simplex virus 1 glycoproteins to a region located between the genes specifying glycoprotein B and the major viral DNA-binding protein (beta 8). The nucleotide sequence of this region contains a single long open reading frame encoding a 780-amino-acid protein with a predicted molecular weight of 83,845. To confirm the existence of this protein, rabbit polyclonal antibody was made against a synthetic peptide made according to the predicted sequence of a hydrophilic domain near the carboxy terminal of the protein. This antibody reacted with an infected cell protein of an apparent molecular weight of 95,500. We designated this protein infected cell protein 18.5 (ICP18.5). S1 nuclease analysis suggested that the 5.6-kilobase mRNA encoding ICP18.5 is initiated predominantly from one site, but three weaker initiation sites also seemed to occur within a 74-base-pair stretch of DNA. This gene appears to be conserved in the Epstein-Barr virus (EBV) genome, inasmuch as 174 of the 780 amino acids of ICP18.5 align with corresponding amino acids predicted by the EBV open reading frame BALF3. The EBV gene is located adjacent to the gene specifying a homolog of the herpes simplex virus 1 glycoprotein B.

Amino Acid Sequence↗