Cleavinger C M, Kim M F, Wise K S
Department of Molecular Microbiology and Immunology, University of Missouri-Columbia 65212.
J Bacteriol. 1994 Apr;176(8):2463-7. doi: 10.1128/jb.176.8.2463-2467.1994.
The variant surface lipoprotein VlpC of Mycoplasma hyorhinis was shown to be processed by cleavage of a characteristic prokaryotic prolipoprotein signal peptide. In addition, a vlpC::phoA fusion protein expressed and translocated in Escherichia coli was recognized by surface-binding monoclonal antibodies, which identified the characteristic region II of Vlps, containing divergent external sequences proximal to the membrane, as an exposed portion of these surface proteins subject to immune recognition and selection.
猪鼻支原体的可变表面脂蛋白VlpC经一种典型的原核前脂蛋白信号肽切割后进行加工。此外,在大肠杆菌中表达并转运的vlpC::phoA融合蛋白被表面结合单克隆抗体识别,该抗体将Vlp的特征性区域II鉴定为这些表面蛋白的一个暴露部分,该区域含有靠近膜的不同外部序列,易于受到免疫识别和选择。