A peroxidase related to the mammalian antimicrobial protein myeloperoxidase in the Euprymna-Vibrio mutualism.
A peroxidase related to the mammalian antimicrobial protein myeloperoxidase in the Euprymna-Vibrio mutualism.
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一种与 Euprymna-Vibrio 互利共生中的哺乳动物抗菌蛋白髓过氧化物酶相关的过氧化物酶。
DOI：
10.1073/pnas.93.24.13683
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发表时间：
1996
影响因子：
11.1
通讯作者：
M. McFall
中科院分区：
文献类型：
--
作者：
V. Weis;A. Small;M. McFall
许多动物-细菌合作协会发生在高度修饰的宿主器官中，这些器官创造了一个独特的环境来容纳和维持共生体。人们一直认为，这些专门的器官通过一个程序的共生特异性或增强的基因表达在一个或两个合作伙伴，但这个过程中一直缺乏一个明确的例子。在这项研究中，我们提供的证据增强生产的酶在共生器官的鱿鱼Euprymna的Euprypopes，其中藏有一个文化的发光细菌费氏弧菌。我们的数据表明，这种酶有一个惊人的生物化学相似性哺乳动物髓过氧化物酶（MPO; EC 1.11.17），抗微生物联茴香胺过氧化物酶发生在中性粒细胞。MPO和鱿鱼过氧化物酶催化相同的反应，具有相似的表观亚基分子量，并且天然人MPO的多克隆抗体特异性地将过氧化物酶样蛋白定位于共生器官的含细菌区域。我们还提供了证据，以前描述的鱿鱼cDNA编码的蛋白质（LO 4），负责观察到的联茴香胺过氧化物酶活性。针对LO 4的片段的抗体从共生器官的提取物中免疫抑制联茴香胺过氧化物酶活性，并在Western印迹分析中针对这些提取物和人MPO反应。这些数据表明，控制细菌数量和生长的相关生化机制在功能上与致病机制和互利共生机制一样多样，并且与软体动物和哺乳动物的遗传距离一样遥远。
Many animal-bacteria cooperative associations occur in highly modified host organs that create a unique environment for housing and maintaining the symbionts. It has been assumed that these specialized organs develop through a program of symbiosis-specific or -enhanced gene expression in one or both partners, but a clear example of this process has been lacking. In this study, we provide evidence for the enhanced production of an enzyme in the symbiotic organ of the squid Euprymna scolopes, which harbors a culture of the luminous bacterium Vibrio fischeri. Our data show that this enzyme has a striking biochemical similarity to mammalian myeloperoxidase (MPO; EC 1.11.17), an antimicrobial dianisidine peroxidase that occurs in neutrophils. MPO and the squid peroxidase catalyze the same reaction, have similar apparent subunit molecular masses, and a polyclonal antibody to native human MPO specifically localized a peroxidase-like protein to the bacteria-containing regions of the symbiotic organ. We also provide evidence that a previously described squid cDNA encodes the protein (LO4) that is responsible for the observed dianisidine peroxidase activity. An antibody made against a fragment of LO4 immunoprecipiated dianisidine peroxidase activity from extracts of the symbiotic organ, and reacted against these extracts and human MPO in Western blot analysis. These data suggest that related biochemical mechanisms for the control of bacterial number and growth operate in associations that are as functionally diverse as pathogenesis and mutualism, and as phylogenetically distant as molluscs and mammals.
受刺激的中性粒细胞发生髓过氧化物酶依赖性荧光素氯化。
DOI：
--
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Hurst,JK;Albrich,JM;Green,TR;Rosen,H;Klebanoff,S
通讯作者：
Klebanoff,S