Behrens A, Heller M, Kirchhoff H, Yogev D, Rosengarten R
Institut für Mikrobiologie und Tierseuchen, Tierärztliche Hochschule Hannover, Germany.
Infect Immun. 1994 Nov;62(11):5075-84. doi: 10.1128/iai.62.11.5075-5084.1994.
A set of strain- and size-variant highly immunogenic membrane surface protein antigens of Mycoplasma bovis, which has been identified by a monoclonal antibody, is shown in this report to make up a family of antigenically and structurally related lipid-modified proteins, designated Vsps (variable surface proteins). By systematic analysis of several isogenic clonal lineages of the type strain PG45, three members of this family have been identified, VspA, VspB, and VspC, each of which was shown to undergo independent high-frequency changes in size as well as noncoordinate phase variation between ON and OFF expression states. The monoclonal antibody-defined epitope common to VspA, VspB, and VspC was accessible on the cell surface in most, but not all, of the clonal populations analyzed and was present on a C-terminal limit tryptic fragment of each Vsp variant that was released from the membrane surface. VspA and VspC were distinguished from VspB by their selective detection with colloidal gold and by their distinctive reaction with a polyclonal antibody against M. bovis D490. VspA, VspB, and VspC were further distinguishable from one another by their characteristic patterns of degradation at carboxypeptidase Y pause sites. While these Vsp-specific structural fingerprints with an irregular periodic spacing were constant for similarly sized variants of a defined Vsp product, they showed distinct differences among variants differing in size. This variability included gain or loss of individual bands within distinct subsets of bands, as well as shifts of the entire banding patterns up- or downwards, indicating that insertions or deletions underlying Vsp size variation can occur at various locations either within the C-terminal domain or within other regions of these proteins. This was similarly confirmed by comparative epitope mapping analysis of tryptic cleavage products generated from different Vsp size variants. The Vsp family of M. bovis described in this study represents a newly discovered system of surface antigenic variation in mycoplasmas displaying features which closely resemble but are also different from the characteristics reported for the Vlp (variable lipoprotein) system of M. hyorhinis. The isogenic lineages established here provide key populations for subsequent analysis of corresponding genes to further elucidate Vsp structure and variation, which may have important relevance for a better understanding of the pathogenicity of this agent.
本报告显示,一组由单克隆抗体鉴定的牛支原体菌株和大小变异的高免疫原性膜表面蛋白抗原,构成了一个抗原性和结构相关的脂质修饰蛋白家族,称为Vsps(可变表面蛋白)。通过对标准菌株PG45的几个同基因克隆谱系进行系统分析,已鉴定出该家族的三个成员,即VspA、VspB和VspC,每个成员在大小上均经历独立的高频变化,并且在ON和OFF表达状态之间存在非协同相变。VspA、VspB和VspC共有的单克隆抗体定义表位在大多数(但不是全部)分析的克隆群体的细胞表面上可及,并且存在于从膜表面释放的每个Vsp变体的C末端限制性胰蛋白酶片段上。VspA和VspC与VspB的区别在于它们能用胶体金选择性检测,以及与抗牛支原体D490的多克隆抗体有独特反应。VspA、VspB和VspC还可通过它们在羧肽酶Y停顿位点的特征性降解模式进一步区分。虽然这些具有不规则周期性间距的Vsp特异性结构指纹对于定义的Vsp产物的相似大小变体是恒定的,但它们在大小不同的变体之间显示出明显差异。这种变异性包括在不同的条带子集中个别条带的增减,以及整个条带模式的向上或向下移动,表明Vsp大小变异背后的插入或缺失可发生在这些蛋白质的C末端结构域内或其他区域的不同位置。这也通过对不同Vsp大小变体产生的胰蛋白酶裂解产物的比较表位图谱分析得到类似证实。本研究中描述的牛支原体Vsp家族代表了支原体中一个新发现的表面抗原变异系统,其显示出的特征与猪鼻支原体的Vlp(可变脂蛋白)系统报道的特征非常相似但也不同。这里建立的同基因谱系为后续分析相应基因以进一步阐明Vsp结构和变异提供了关键群体,这对于更好地理解该病原体的致病性可能具有重要意义。