ABSTRACT
The primary and secondary structures of the pp65 phosphoprotein of human cytomegalovirus coded by the UL83 gene were studied by the methods of computer-aided analysis. An immunodominant protein fragment with 3 antigenic determinant was detected. The UL83 fragment coding the selected region was amplified and cloned in bacterial expressing vector. The recombinant protein was obtained and purified. On the basis of ELISA findings it was acknowledged as possible to use the pp65 recombinant protein jointly with pp150 and p52 in the diagnosis of antibodies specific to human cytomegalovirus.
Subject(s)
Cytomegalovirus/metabolism , Phosphoproteins/genetics , Viral Matrix Proteins/genetics , Amino Acid Sequence , Enzyme-Linked Immunosorbent Assay , Epitopes/chemistry , Molecular Sequence Data , Phosphoproteins/chemistry , Phosphoproteins/metabolism , Protein Structure, Secondary , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid , Viral Matrix Proteins/chemistry , Viral Matrix Proteins/metabolismABSTRACT
W/SSM rats which are characterized by hereditary abnormal changes in the lungs, hepato- and splenomegalia and some other disturbances have also alpha 1-antitrypsin (AAT) deficiency. A study of AAT in these rats by means of isoelectrofocusing and immunoblotting with anti-AAT antibodies labelled with peroxidase has demonstrated that deficiency of the protease inhibitor is not associated with any disturbances of its synthesis or any changes of its electrophoretic properties. A higher activity of lysosomal glycosidases and proteinases was found in the liver and leukocytes of W/SSM rats. It is suggested that AAT deficiency is due to its modification under the influence of lysosomal enzymes. The described biochemical distances seem to be associated with an increased hexose transport into the cells, which is controlled by a mutant gene.
