Biomedical subjects
B Sina
Publications and source records attributed to B Sina.
Parapsoriasis.
Parapsoriasis is a term which encompasses a number of differing pathologic states clinically manifesting chronic recalcitrant erythematous scaling lesions. Although these various diseases have some similar clinical and histopathological features, they are obviously quite different from the standpoint of malignant potential and prognosis. The classification suggested herein has been developed in an attempt to resolve the existing confusion and to offer a simplified approach to the study of a complex problem.
Common epitopes in the circumsporozoite proteins of Plasmodium berghei and Plasmodium gallinaceum identified by monoclonal antibodies to the P. gallinaceum circumsporozoite protein.
Monoclonal antibodies that react with the circumsporozoite protein of the avian malaria Plasmodium gallinaceum sporozoites also reacted with circumsporozoite protein of the rodent malaria Plasmodium berghei. Two types of reactivity were identified: 1) two monoclonal antibodies reacted with P. berghei sporozoite protein by enzyme-linked immunosorbent assay, Western blot and indirect immunofluorescence antibody, 2) six other monoclonal antibodies reacted with P. berghei sporozoites by ELISA and Western blot only. We studied whether these differences could be explained by reactivity in enzyme-linked immunosorbent assay with different P. berghei circumsporozoite peptides. Although all P. gallinaceum monoclonal antibodies reacted with the P. berghei repeats, the first group reacted with a conserved peptide sequence, N1, whereas the second group did not. These results suggest that circumsporozoite proteins from P. gallinaceum and P. berghei share common epitopes. The biological significance of our finding is not yet clear. Indeed, the cross-reactive monoclonal antibodies giving a positive indirect immunofluorescence antibody with the P. berghei sporozoites only caused a borderline effect on the living P. berghei parasites in vitro as measured by inhibition of sporozoite infectivity.