Linggood M A, Ellis M L, Porter P
Immunology. 1979 Sep;38(1):123-7.
The heat-labile K88 antigen, a virulence determinant coded for by a transmissible plasmid, was eliminated from enteropathogenic strains of Escherichia coli by passage through media containing antibodies to the heat stable antigens of an Abbotstown (O149:K91,K88ac) strain. The plasmid-curing activity of O149 antisera was not O-antigen specific as O149, O45, O8 and O138 strains of E. coli could be 'cured' of their K88 plasmids by this technique. The curing activity was differentiated from the O-antibody by gel filtration, the O149 antibodies were eluted in the IgM peak while the curing activity was found in the IgG peak. In view of the lack of O-specificity and the absence of K88 antibodies it appears that antibodies to a common heat-stable antigenic determinant were involved in this phenomenon.
热不稳定的K88抗原是一种由可传递质粒编码的毒力决定因素,通过将产肠毒素大肠杆菌菌株传代于含有针对阿伯茨敦(O149:K91,K88ac)菌株热稳定抗原的抗体的培养基中,可将其从该菌株中消除。O149抗血清的质粒消除活性并非O抗原特异性的,因为通过该技术,大肠杆菌的O149、O45、O8和O138菌株的K88质粒都可以被“消除”。通过凝胶过滤将消除活性与O抗体区分开来,O149抗体在IgM峰中洗脱,而消除活性则在IgG峰中发现。鉴于缺乏O特异性且不存在K88抗体,似乎针对一种常见热稳定抗原决定簇的抗体参与了这一现象。