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阴道具有足以激活阴道毛滴虫半胱氨酸蛋白酶的还原性环境。

The vagina has reducing environment sufficient for activation of Trichomonas vaginalis cysteine proteinases.

作者信息

Alderete J F, Provenzano D

机构信息

Department of Microbiology, University of Texas Health Science Center, San Antonio, TX 78284-7758, USA.

出版信息

Genitourin Med. 1997 Aug;73(4):291-6. doi: 10.1136/sti.73.4.291.

Abstract

BACKGROUND

Trichomonas vaginalis, a worldwide distributed sexually transmitted protozoan, is remarkable for synthesis of numerous, distinct cysteine proteinases, the significance of which is evidenced by the presence in vivo of soluble proteinases in secretions and antiproteinase antibody in serum of patients with trichomonosis. These proteinases purportedly play a role in host parasitism and immune evasion.

OBJECTIVE

It is known that for cysteine proteinases to be functional, they must be activated by disulphide reducing reagents. Whether or not the host vaginal environment has the reducing environment essential for activation of the trichomonad cysteine proteinases is unknown. Our goal, therefore, was to determine whether or not vaginal secretions had sufficient reducing power to activate the trichomonad proteinases.

METHODS

48 vaginal washes (VWs) from patients were assayed for reducing equivalents and a score in dithiothreitol (DTT) reducing equivalents was assigned to each VW. Activation of trichomonad cysteine proteinases was then tested under the range of reducing equivalents detected from VWs. The possible protective effect of hydrogen peroxide, an oxidising agent produced by some Lactobacillus species, on proteinase activity was also determined.

RESULTS

Nine of 48 VWs (18.7%) possessed < or = 10 microM DTT reducing equivalents, four VWs (8.3%) had from 20 microM DTT to 40 microM DTT reducing equivalents, and most (50%) were between 10 microM to 15 microM. Overall, the range in VWs was from approximately 10 microM to 40 microM reducing equivalents. Importantly, data suggest differential proteinase activation over this in vivo range of reducing level. Only two T vaginalis cysteine proteinase activities were stimulated at 2.5 microM DTT in contrast with all proteinase activities present at 40 microM DTT, albeit quantitatively diminished compared with the activity at 1 mM DTT, the concentration routinely used in vitro. Finally, hydrogen peroxide reversibly neutralised all trichomonad proteinases.

CONCLUSIONS

These results show that the vagina of women has a reducing environment adequate for activation of trichomonad proteinases. The data underscore that the host environment plays a role in the host-parasite interrelation. Finally, hypotheses can now be formulated to help explain resistance and susceptibility to infection commonly reported among women and between men and women with trichomonosis.

摘要

背景

阴道毛滴虫是一种广泛分布的性传播原生动物,以合成多种不同的半胱氨酸蛋白酶而著称,其重要性体现在滴虫病患者分泌物中存在可溶性蛋白酶以及血清中存在抗蛋白酶抗体。这些蛋白酶据称在宿主寄生和免疫逃避中起作用。

目的

已知半胱氨酸蛋白酶要发挥功能,必须被二硫键还原试剂激活。宿主阴道环境是否具有激活滴虫半胱氨酸蛋白酶所需的还原环境尚不清楚。因此,我们的目标是确定阴道分泌物是否具有足够的还原能力来激活滴虫蛋白酶。

方法

对48份来自患者的阴道冲洗液(VW)进行还原当量测定,并为每份VW指定二硫苏糖醇(DTT)还原当量得分。然后在从VW中检测到的还原当量范围内测试滴虫半胱氨酸蛋白酶的激活情况。还确定了过氧化氢(某些乳酸杆菌产生的一种氧化剂)对蛋白酶活性可能的保护作用。

结果

48份VW中有9份(18.7%)的DTT还原当量≤10微摩尔,4份VW(8.3%)的DTT还原当量为20微摩尔至40微摩尔,大多数(50%)在10微摩尔至15微摩尔之间。总体而言,VW中的还原当量范围约为10微摩尔至40微摩尔。重要的是,数据表明在这个体内还原水平范围内蛋白酶激活存在差异。与在40微摩尔DTT时所有蛋白酶活性都存在相比,在2.5微摩尔DTT时仅刺激了两种阴道毛滴虫半胱氨酸蛋白酶活性,尽管与在1毫摩尔DTT(体外常规使用的浓度)时的活性相比在数量上有所减少。最后,过氧化氢可逆地中和了所有滴虫蛋白酶。

结论

这些结果表明女性阴道具有足以激活滴虫蛋白酶的还原环境。数据强调宿主环境在宿主 - 寄生虫相互关系中起作用。最后,现在可以提出假设来帮助解释女性之间以及患有滴虫病的男性和女性之间常见的感染抗性和易感性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/755e/1195862/04a1e1eb60dc/genitmed00004-0059-a.jpg

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