Jeavons L, Hunt L, Hamilton A
Dermatology Unit, St Johns Institute of Dermatology, Guy's Hospital, London, UK.
J Med Vet Mycol. 1994;32(1):47-57. doi: 10.1080/02681219480000071.
A monoclonal antibody (MAb) of the IgG1 subclass, with greater activity to the yeast than the mycelial phase of Histoplasma capsulatum was raised and was found to predominantly recognize a molecule of 80 kDa by immunoblot. Enzymatic deglycosylation and chemical degradation, followed by reaction with MAb 69F on Western blots showed the molecule to be O-glycosylated, and immunofluorescence studies showed it to be heat-inducible and its distribution to be cytoplasmic and possibly cell membraneous. There was no apparent staining of the cell wall. Culture filtrate was positive by ELISA and Western blot when reacted with MAb 69F. In addition, ELISA and Western blot demonstrated that a similar epitope was present in other fungal species. The glycoprotein had a pI of approximately 4.7. N-terminal amino acid sequencing revealed this molecule to be homologous to members of the heat-shock protein 70 family and to a recently described antigen from H. capsulatum.
制备了一种IgG1亚类的单克隆抗体（MAb），该抗体对荚膜组织胞浆菌酵母相的活性高于菌丝相，通过免疫印迹发现其主要识别一种80 kDa的分子。酶促去糖基化和化学降解后，在Western印迹上与单克隆抗体69F反应表明该分子为O-糖基化，免疫荧光研究表明它是热诱导性的，其分布在细胞质中，可能也存在于细胞膜上。细胞壁没有明显的染色。当与单克隆抗体69F反应时，培养滤液通过ELISA和Western印迹呈阳性。此外，ELISA和Western印迹表明其他真菌物种中存在类似的表位。该糖蛋白的pI约为4.7。N端氨基酸测序显示该分子与热休克蛋白70家族成员以及最近描述的荚膜组织胞浆菌抗原同源。
