Accession Number : ADA432993


Title :   Characterization of Antibody Specific for Disease Associated Prion Protein


Descriptive Note : Annual rept. 25 Jun 2003-24 Jun 2004


Corporate Author : CASE WESTERN RESERVE UNIV CLEVELAND OH


Personal Author(s) : Chen, Shu G.


Full Text : http://www.dtic.mil/get-tr-doc/pdf?AD=ADA432993


Report Date : JUL 2004


Pagination or Media Count : 16


Abstract : Prion diseases are characterized by the presence of the abnormal scrapie isoform of prion protein (Prp(exp Sc)) in affected brains. A conformational change is believed to convert the normal cellular prion protein (PrP (expC)) into PrP(exp Sc). Detection of PrP(exp Sc) for diagnosis and prophylaxis is impaired because available antibodies recognizing epitopes on PrP fail to distinguish between PrP(exp sc) and PrP (exp c). We have discovered a novel antibody oCD4 that may overcome the above deficiency. The objective in year I is to characterize the specificity and selectivity of OCD4. We have accomplished this objective for year I. The major findings and work in progress are summarized here. We have found that OCD4 is an anti-DNA antibody OCD4 that capture PrP from brains affected by prion diseases in both humans and animals but not from unaffected controls. OCD4 appears to immunoreact with DNA (or a DNA- associated molecule) that forms a conformation-dependent complex with PrP in prion diseases. We have also found that g5p, a well-established DNA-binding protein, can be used for recognizing PrP(exp Sc). Therefore, OCD4 and g5p specifically target disease-associated DNA PrP complexes in prion diseases. Our finding opens new avenues in the study and diagnosis of prion diseases.


Descriptors :   *ANTIBODIES , *VIRUS DISEASES , *PRIONS(PATHOGENS) , BRAIN , HUMANS , PROTEINS , DEOXYRIBONUCLEIC ACIDS , ANTIGENS , RECEPTOR SITES(PHYSIOLOGY) , ABNORMALITIES , PREVENTIVE MEDICINE , SHEEP.


Subject Categories : MEDICINE AND MEDICAL RESEARCH


Distribution Statement : APPROVED FOR PUBLIC RELEASE