作者: K Tanabe , S Takasaki , J Watanabe , A Kobata , K Egawa
DOI: 10.1128/IAI.57.5.1363-1368.1989
关键词: Gel electrophoresis 、 Isoelectric point 、 Biology 、 Microbiology 、 Pneumocystis carinii 、 Pneumocystosis 、 Glycoprotein 、 Epitope 、 Membrane glycoproteins 、 Glycosylation 、 Molecular biology
摘要: Pneumocystis carinii is a pathogen which causes fatal pneumonia in patients with acquired immune deficiency syndrome. To facilitate the basic study of P. carinii, we analyzed major surface proteins by immunochemical and biochemical methods. The protein components both cysts (resting form) trophozoites (vegetative are part group called P115 apparent masses 105 to 120 kilodaltons. They represent an unusually large portion total this organism. purified exhibited six isoelectric variants when two-dimensional gel electrophoresis. A monoclonal antibody raised against recognized all reacted epitopes that were located cell wall, thereby indicating immunoreactive component. Data presented contain identical or closely related they mannose-rich glycoproteins. Deglycosylated migrates primarily as single more acidic gels, suggesting may be due differences glycosylation. majority sera tested from humans diagnosed pneumocystosis strongly proteins.