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1.
Clin Diagn Lab Immunol ; 3(5): 554-62, 1996 Sep.
Article in English | MEDLINE | ID: mdl-8877134

ABSTRACT

While viral infections and their impact are well studied in domestic cats, only limited information is available on their occurrence in free-ranging lions. The goals of the present study were (i) to investigate the prevalence of antibodies to feline calicivirus (FCV), herpesvirus (FHV), coronavirus (FCoV), parvovirus (FPV), and immunodeficiency virus (FIV) and of feline leukemia virus (FeLV) antigen in 311 serum samples collected between 1984 and 1991 from lions inhabiting Tanzania's national parks and (ii) to evaluate the possible biological importance and the interrelationship of these viral infections. Antibodies to FCV, never reported previously in free-ranging lions, were detected in 70% of the sera. In addition, a much higher prevalence of antibodies to FCoV (57%) was found than was previously reported in Etosha National Park and Kruger National Park. Titers ranged from 25 to 400. FeLV antigen was not detectable in any of the serum samples. FCoV, FCV, FHV, and FIV were endemic in the Serengeti, while a transient elevation of FPV titers pointed to an outbreak of FPV infection between 1985 and 1987. Antibody titers to FPV and FCV were highly prevalent in the Serengeti (FPV, 75%; FCV, 67%) but not in Ngorongoro Crater (FPV, 27%; FCV, 2%). These differences could be explained by the different habitats and biological histories of the two populations and by the well-documented absence of immigration of lions from the Serengeti plains into Ngorongoro Crater after 1965. These observations indicate that, although the pathological potential of these viral infections seemed not to be very high in free-ranging lions, relocation of seropositive animals by humans to seronegative lion populations must be considered very carefully.


Subject(s)
Antibodies, Viral/blood , Antigens, Viral/immunology , Calicivirus, Feline/immunology , Coronavirus/immunology , Feline Panleukopenia Virus/immunology , Herpesviridae/immunology , Immunodeficiency Virus, Feline/immunology , Leukemia Virus, Feline/immunology , Africa, Eastern/epidemiology , Animals , Coronavirus, Feline/immunology , Lions
2.
Schweiz Arch Tierheilkd ; 138(12): 579-85, 1996.
Article in German | MEDLINE | ID: mdl-9045289

ABSTRACT

There are several felidae amongst the numerous endangered species. Means of aiding survival are the reintroduction to the wild of animals bred under the auspices of man and their relocation from densely populated to thinly populated areas. It is unlikely that the dangers of such reintroduction or relocation projects have been examined sufficiently in respect to the risks of virus infections confronting individuals kept in zoos or similar situations. This report presents three examples to illustrate that accidental virus infections may be expected to occur when relocating and reintroducing wild cats. The first example is the reintroduction of captive snow leopards. Zoo bred snow leopards may be infected with FIV, a virus infection that is highly unlikely to occur in the original himalayan highlands of Tibet and China. A second example is of several cases of FIP that occurred in European wild cats bred in groups in captivity. The third example mentioned is the relocation of lions from East Africa where all the commonly known feline viruses are wide-spread to the Etosha National Park. In the latter, virus infections such as FIV, FCV and FPV do not occur. The indiscriminate relocation and reintroduction of the wild cats mentioned here harbours a potential of undesirable consequences.


Subject(s)
Animals, Wild , Animals, Zoo , Carnivora , Lions , Virus Diseases/veterinary , Animals , Cats , Feline Acquired Immunodeficiency Syndrome/transmission , Feline Infectious Peritonitis/transmission , Virus Diseases/transmission
3.
J Virol ; 64(10): 5123-31, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2398536

ABSTRACT

Semliki Forest virus capsid (C) protein molecules (Mr, 33,000) can be introduced efficiently into the cytoplasm of various target cells by electroporation, liposome, and erythrocyte ghost-mediated delivery (M. Elgizoli, Y. Dai, C. Kempf, H. Koblet, and M.R. Michel, J. Virol. 63:2921-2928, 1989). Here, we show that the transferred C protein molecules partition rapidly from the cytosolic compartment into the nucleus. Transport of the C protein molecules into the nucleus was reversibly arrested by metabolic inhibitors, indicating that the transfer process is energy dependent. Fractionation of isolated nuclei revealed that the delivered C protein preferentially associates with the nucleoli. This finding was confirmed by morphological studies, showing that in an in vitro system containing ATP isolated nuclei rapidly accumulated rhodamine-labeled C protein in their nucleoli. Furthermore, in this assay system, the lectin wheat germ agglutinin prevented transfer of C protein through nuclear pores. These results are in agreement with our observation that nucleoli contain measurable amounts of newly synthesized C protein as early as 5 h after infection of cells with SFV. Thereafter, nucleolar-associated C protein increased progressively during the course of infection.


Subject(s)
Capsid/biosynthesis , Cell Transformation, Viral , Semliki forest virus/genetics , Adenosine Triphosphate/metabolism , Amino Acid Sequence , Animals , Blotting, Western , Capsid/isolation & purification , Cell Line , Cell Nucleolus/metabolism , Cell Nucleus/metabolism , Cytosol/metabolism , Electrophoresis, Polyacrylamide Gel , HeLa Cells/metabolism , Humans , Kinetics , Methionine/metabolism , Molecular Sequence Data , Sequence Homology, Nucleic Acid , Vero Cells
4.
J Virol ; 63(7): 2921-8, 1989 Jul.
Article in English | MEDLINE | ID: mdl-2724418

ABSTRACT

The Semliki Forest virus capsid (C) protein was introduced into various target cells by electroporation-, liposome-, and erythrocyte-ghost-mediated delivery. Data are presented which show that the incorporated C protein is biologically active and, at low concentrations (10(3) to 10(4) molecules per cell), markedly induces host cellular protein synthesis (average value, up to 90%). On the other hand, high concentrations (10(5) to 10(6) molecules per cell) led to a significant inhibition (average value, up to 60%). The cellular response to C protein was found to be identical in P3X63Ag8 suspension cells, CV-1 cells, and GpBind4 cells. Following electroporation-mediated delivery of C-protein molecules, both induction and repression of cellular protein synthesis were immediate, whereas with liposome-mediated delivery these events were delayed by about 1 h. Maximum stimulation and repression occurred between 0 and 1 h after delivery of C protein and decreased thereafter to reach control values at about 4 h. The analysis of the proteins synthesized suggests that low amounts of microinjected C protein are responsible for the induction of classes with specific Mrs, whereas high amounts lead to an inhibition of overall protein synthesis.


Subject(s)
Capsid/physiology , Cell Transformation, Viral , Genes, Regulator , Protein Biosynthesis , Semliki forest virus/genetics , Animals , Capsid/isolation & purification , Cell Line , Erythrocyte Membrane/metabolism , Kinetics , Liposomes , Molecular Weight , Neoplasm Proteins/biosynthesis
5.
Experientia ; 44(3): 199-203, 1988 Mar 15.
Article in English | MEDLINE | ID: mdl-2450774

ABSTRACT

Using the suspension cell line P3X63Ag8 we have studied the impact of the composition of the diffusion medium on cellular protein synthesis under standard electroporation conditions in TBS-Na. This buffer contains the high saline concentration usually present in electroporation-mediated DNA transfection. Electroporation in the presence of TBS-Na resulted in an immediate shut-off of protein synthesis, even though both FITC-dextran (Mr 40 kD) and Semliki Forest virus core protein (Mr 33 kD) were incorporated efficiently into the cytoplasm across the electropores at 0 degrees C. Subsequent resealing of the pores was completed after a 5-min incubation at 37 degrees C. When compared with control cells, overall protein synthesis of electroporated cells recovered slowly to resume a 30% activity after 1 h of incubation at 37 degrees C. We have determined optimal conditions for diffusion loading (which necessitates the presence of ATP, GTP, amino acids, K+, Mg2+, and Ca2+) and resealing (in the presence of K+, Mg2+, and Ca2+), leading to a full and lasting recovery of protein synthesis within 5 min after pore closure.


Subject(s)
Cell Membrane Permeability , Cell Membrane/physiology , Electricity , Protein Biosynthesis , Adenosine Triphosphate/metabolism , Animals , Cell Line , Dextrans , Diffusion , Guanosine Triphosphate/metabolism , In Vitro Techniques , Kinetics , Mice
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