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首页> 外文期刊>Infection and immunity >Modulation of invasiveness and catalytic activity of Bordetella pertussis adenylate cyclase by polycations.
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Modulation of invasiveness and catalytic activity of Bordetella pertussis adenylate cyclase by polycations.

机译：聚阳离子调节百日咳博德特氏菌腺苷酸环化酶的侵袭性和催化活性。

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摘要

Penetration of Bordetella pertussis adenylate cyclase into CHO cells was monotonically inhibited by polylysines, with a minimum degree of polymerization of greater than 6 and less than or equal to 9 to 10. Above this level, inhibitory potency per lysyl residue was independent of polymer length; 50% inhibition was obtained with 60 microM lysine monomer. Other polycations were also potent inhibitors. The adenylate cyclase itself showed a biphasic (stimulation-inhibition) response, with a similar independence of polymer length above a certain minimum. Half-maximal inhibitory concentrations for cyclic AMP accumulation corresponded to half-maximal stimulatory concentrations of poly-L-lysine for the cyclase. The inhibitory effect of polylysines on cyclic AMP accumulation was not reversed by washing or enzymatic removal of neuraminic acid. We conclude that charge-charge interactions play an important role in the penetration of B. pertussis adenylate cyclase into host cells.
机译：聚赖氨酸单调抑制了百日咳博德特氏菌腺苷酸环化酶向CHO细胞的渗透，其最低聚合度大于6且小于或等于9至10。高于该水平，每个赖氨酰基残基的抑制能力与聚合物长度无关;用60 microM赖氨酸单体获得50％的抑制作用。其他聚阳离子也是有效的抑制剂。腺苷酸环化酶本身显示出双相（刺激抑制）反应，聚合物长度超过一定最小值时具有类似的独立性。环AMP积累的半数最大抑制浓度对应于环化酶聚L-赖氨酸的半数最大刺激浓度。洗涤或酶去除神经氨酸并不能逆转多赖氨酸对环状AMP积累的抑制作用。我们得出的结论是，电荷-电荷相互作用在百日咳博德特氏菌腺苷酸环化酶向宿主细胞的渗透中起重要作用。

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