NR ABMI
AU Bons,N.; Mestre-Frances,N.; Charnay,Y.; Tagliavini,F.
TI Spontaneous spongiform encephalopathy in a young adult rhesus monkey
QU Lancet 1996 Jul 6; 348(9019): 55
KI Lancet. 1996 Oct 5;348(9032):955-6. PMID: 8843820
PT letter
VT
Sir - Although human and animal prion diseases have been experimentally transmitted to various monkey species, spontaneous occurrence of a spongiform encephalopathy in non-human primates has not been reported. We describe the development of a spongiform encephalopathy without known cause in a rhesus monkey (Macaca mulatta).
The monkey was born in 1982 and was acquired from Ravensden zoo, Rushend, Northants, UK, in October, 1986, by the zoological park in Montpelier, France where it was housed in the primate colony. In Montpelier, the monkey was fed standard monkey feed including Singe 107 (UAR, Paris, France) which contains meat products declared fit for human consumption. In summer, 1991, aged 9, the previously healthy monkey became lethargic and developed mood changes, in particular, aggressiveness. The monkey became isolated from its companions and hid itself away. In June, 1992, the monkey was anaesthetised with pentobarbital and perfused intracardially with saline followed by 4% paraformaldehyde.
The brain was dissected into 5 mm coronal blocks, which were embedded in paraplast. 6 µm serial sections were stained with haematoxylin and eosin and thioflavine S for amyloid, or immunolabelled with antibodies: monoclonal antibody to a synthetic peptide homologous to residues 106-126 of human prion protein (PrP), supernatant 1:2 dilution; polyclonal antibody to a synthetic peptide homologous to residues 1-40 of the ß protein (R1280, provided by Dr D Selkoe), 1:1000 dilution; and antiserum to glial fibrillary acidic protein (GFAP, Dako, Denmark), 1:1000 dilution. Immunoreactions were revealed by the avidin-biotin method. The sections were treated with formic acid before immunostaining, and were counterstained with Harris' haematoxylin. Negative control sections were incubated with normal mouse or rabbit sera as primary antibody. There were conspicuous spongiform changes and gliosis in the grey matter, particularly in the cerebral cortex where the deep layers were mostly involved. A number of neurons in the affected areas contained large vacuoles; these were single or multiple and distended the soma to produced ballooned cells with a marrow rim of cytoplasm. Immunohistochemistry showed that vacuolated neurons and distended nerve-cell processes were surrounded by PrP-immunoreactive material (figure). The severe vacuolation of neurons observed in this rhesus monkey is similar to the vacuolation seen in squirrel monkeys after inoculation with brain material of patients with Creutzfeldt-Jakob disease (CJD).1 Immunological labelling of neurons in this monkey also resembled those seen in the brains of patients with CJD.2 Immunostaining showed anti-ß protein immunoreactive deposits in the neuropil of the cerebral cortex.
Figure: Prion spongiform encephalopathy [Image] in a rhesus monkey
Vacuolated neurons with PrP deposits (arrows) in temporal cortex; anti-PrP immunocytochemistry - Harris' haematoxylin counterstain.
As far as we are aware, this is the first reported case of spontaneously developed spongiform encephalopathy in a monkey. The feeding of this monkey with animal protein raises the possibility of cross-species transmission of the disease through contaminated foodstuff, similar to that suggested for bovine spongiform encephalopathy.
1 Zlotnik I, Grant DP, Dayan AD, Earl CJ. Transmission of Creutzfeldt-Jakob from a man to squirrel monkey. Lancet 1974; 24: 435-38.
2 Bruton CJ, Bruton RK, Gentleman SM, Roberts GW. Diagnosis and incidence of prion (Creutzfeldt-Jakob) disease: a retrospective archival survey with implications for future research. Neurodegeneration 1995; 4: 357-68.
ZR 2 Zitate
MH Animal; Brain/pathology; *Macaca mulatta; Monkey Diseases/*pathology/transmission; Prion Diseases/*pathology/transmission/*veterinary
AD *Noëlle Bons, Nadine Mestre-Francés, Yves Charnay, Fabrizio Tagliavini, *Neuromorphologie Fonctionelle, Ecole Pratique des Hautes Etudes, Université Montpellier II, 34095 Montpellier cedex 5, France; H.U.G., Belle-Idée, Division de Neuropsychiatrie, Chène-Bourg, Genève, Switzerland; and Istituto Nazionale Neurologico C Besta, Milano, Italy
SP englisch
PO England
OR Prion-Krankheiten 2