INHIBITION OF MYCOPLASMA-BOVIS CYTADHERENCE BY A MONOCLONAL-ANTIBODY AND VARIOUS CARBOHYDRATE SUBSTANCES
INHIBITION OF MYCOPLASMA-BOVIS CYTADHERENCE BY A MONOCLONAL-ANTIBODY AND VARIOUS CARBOHYDRATE SUBSTANCES
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DOI：
10.1016/0378-1135(93)90097-q
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发表时间：
1993-09-01
影响因子：
3.3
通讯作者：
HANEL, I
中科院分区：
文献类型：
--
作者：
SACHSE, K;PFUTZNER, H;HANEL, I
研究了牛支原体与永久性胚胎牛肺（EBL）细胞的粘附，以确定参与粘附过程的因素。一种针对M.牛显示出分别使菌株120和454的细胞粘附减少46%和70%。在未抑制试验中，在电泳蛋白图谱中显示出强烈的26 kDa条带的菌株120比相应条带明显较弱的菌株454更强地粘附于EBL细胞单层。结果表明，26 kDa蛋白参与M。牛的附着力。在进一步的抑制实验中，可以证明N-乙酰基-神经氨乳糖、血型糖蛋白和硫酸葡聚糖显著降低粘附的能力。这表明参与唾液酸残基，也可能是硫苷脂基团作为结合受体。这些数据表明了一种复杂的粘附机制，与M。肺炎。
The attachment of Mycoplasma bovis to permanent embryonic bovine lung (EBL) cells was studied in order to identify factors participating in the adhesion process. A monoclonal antibody directed against a 26 kDa protein of M. bovis was shown to reduce cytadherence of strains 120 and 454 by 46% and 70%, respectively. In uninhibited assays, strain 120 which exhibits an intense 26 kDa band in electrophoretic protein patterns adhered more strongly to EBL cell monolayers than strain 454 whose corresponding band is considerably weaker. The findings indicate involvement of the 26 kDa protein in M. bovis adherence. In further inhibition experiments, the ability of N-acetyl-neuraminlactose, glycophorin and dextran sulfate to significantly reduce adherence could be demonstrated. This suggests participation of sialic acid residues and probably also sulfatide groups as binding receptors. The data point to a complex adhesion mechanism with similarities to M. pneumoniae.