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首页> 外文期刊>Journal of bacteriology >Glycosylation of the Collagen Adhesin EmaA of Aggregatibacter actinomycetemcomitans Is Dependent upon the Lipopolysaccharide Biosynthetic Pathway
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Glycosylation of the Collagen Adhesin EmaA of Aggregatibacter actinomycetemcomitans Is Dependent upon the Lipopolysaccharide Biosynthetic Pathway

机译：骨集放线菌的胶原粘附蛋白EmaA的糖基化取决于脂多糖的生物合成途径。

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The human oropharyngeal pathogen Aggregatibacter actinomycetemcomitans synthesizes multiple adhesins, including the nonfimbrial extracellular matrix protein adhesin A (EmaA). EmaA monomers trimerize to form antennae-like structures on the surface of the bacterium, which are required for collagen binding. Two forms of the protein have been identified, which are suggested to be linked with the type of O-polysaccharide (O-PS) of the lipopolysaccharide (LPS) synthesized (G. Tang et al., Microbiology 153:2447-2457, 2007). This association was investigated by generating individual mutants for a rhamnose sugar biosynthetic enzyme (rmlC; TDP-4-keto-6-deoxy-d-glucose 3,5-epimerase), the ATP binding cassette (ABC) sugar transport protein (wzt), and the O-antigen ligase (waaL). All three mutants produced reduced amounts of O-PS, and the EmaA monomers in these mutants displayed a change in their electrophoretic mobility and aggregation state, as observed in sodium dodecyl sulfate (SDS)-polyacrylamide gels. The modification of EmaA with O-PS sugars was suggested by lectin blots, using the fucose-specific Lens culinaris agglutinin (LCA). Fucose is one of the glycan components of serotype b O-PS. The rmlC mutant strain expressing the modified EmaA protein demonstrated reduced collagen adhesion using an in vitro rabbit heart valve model, suggesting a role for the glycoconjugant in collagen binding. These data provide experimental evidence for the glycosylation of an oligomeric, coiled-coil adhesin and for the dependence of the posttranslational modification of EmaA on the LPS biosynthetic machinery in A. actinomycetemcomitans.
机译：人类口咽病原体 Agactibacteractinomycetemcomitans 合成多种粘附素，包括非纤维细胞外基质蛋白粘附素A（EmaA）。 EmaA单体三聚形成细菌表面上的触角状结构，这是胶原蛋白结合所必需的。已经鉴定出两种形式的蛋白质，建议与合成的脂多糖（LPS）的O多糖（O-PS）类型相关（G. Tang等，Microbiology 153：2447-2457，2007 ）。通过产生鼠李糖生物合成酶（ rmlC ; TDP-4-keto-6-deoxy-d-glucose 3,5-epimerase），ATP结合盒（ABC）的单个突变体来研究这种关联）糖转运蛋白（ wzt ）和O抗原连接酶（ waaL ）。如在十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶中观察到的，所有三个突变体产生的O-PS量均减少，并且这些突变体中的EmaA单体显示出其电泳迁移率和聚集状态的变化。使用岩藻糖特异性的 Lens culinaris 凝集素（LCA），通过凝集素印迹法提出用O-PS糖修饰EmaA。岩藻糖是b型O-PS血清中的聚糖成分之一。表达 rmlC 突变型EmaA蛋白的突变菌株在体外兔心脏瓣膜模型中显示出降低的胶原蛋白粘附性，表明糖缀合物在胶原蛋白结合中发挥了作用。这些数据为寡聚的卷曲螺旋粘附素的糖基化以及EmaA的翻译后修饰对LPS生物合成机制的依赖性提供了实验证据。放线菌。

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