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Abstract
Bovine spongiform encephalopathy (BSE) or ‘mad cow disease’ is a new disease with an elusive transmissible agent. However, a ‘Prion protein’ (PrP) of about 27K Dalton has been observed to play an essential role in the pathogenecity of BSE. Friesian cattle of 3–6 years of age have been found susceptible. Common symptoms include weight loss, unmanageable behaviour, traumatic damage due to locomotor deficits and prolonged recumbency. Recent studies suggest that amino acid substitutions in PrP may modulate the development of prion diseases. Histopathology of brain stem grey matter showed moderate number of discrete ovoid and spherical vacuoles in the neuropil causing spongiform change. The electron microscopic detection of abnormal fibrils called scrapie-associated fibrils' in the extracts of affected brain may be used as an additional diagnostic ceiterion. Transmission has been suspected due to feeding of offals meal, meat meal and bone meal of diseased animals Susceptibility of BSE is probably inherited. However, extensive investigations are required for the establishment of aetiology, transmission, pathogenicity and zoonotic potential of BSE, a new nervous disorder of bovines.