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Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat
Microbiological Research ( IF 6.7 ) Pub Date : 2018-12-30 , DOI: 10.1016/j.micres.2018.12.007
Chi-Hung Lin , Robyn A. Peterson , Audrey Gueniche , Ségolène Adam de Beaumais , Virginie Hourblin , Lionel Breton , Maria Dalko , Nicolle H. Packer

Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection.

We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium.

Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY).

Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.



中文翻译:

聚糖在表皮葡萄球菌棒状杆菌属的结合中的差异参与。汗流背

汗液是一种分泌液,由于驻留细菌与汗液成分的相互作用,可能是令人不愉快的体味的来源。汗液中糖蛋白的鉴定表明,与蛋白质结合的聚糖可作为细菌的结合表位,如在其他分泌液(如人乳,眼泪和唾液)中发现的那样,有助于保护上皮表面免受感染。

我们对汗液进行了蛋白质组学和糖蛋白分析,以发现大量糖蛋白,主要携带带有或不带有岩藻糖的双天线唾液酸化N-聚糖。使用荧光板测定法确定汗液蛋白上的聚糖是否为产生气味的皮肤表皮葡萄球菌棒状杆菌提供结合表位。发现唾液酸和岩藻糖是表皮葡萄球菌3-22-BD-6的重要结合表位,表皮葡萄球菌3-22-BD-6最近从人类汗液中分离出来,而岩藻糖(但不是唾液酸)促成表皮葡萄球菌ATCC的结合。12228。相反,我们的结果表明汗N-聚糖不提供棒状杆菌的结合表位。

研究了路易斯血型抗原的合成糖模拟物作为表皮葡萄球菌3-22-BD-6与汗液结合的潜在抑制剂。将细菌与LeB,LeX,LeY和sLeX(戊糖)预孵育会导致汗液蛋白粘附力显着降低,这表明末端岩藻糖是关键的结合表位,尤其是与2型链(Galβ1-4GlcNAc)构型连接时(LeY)。

我们的研究结果为进一步研究阐明聚糖在汗液相关恶臭中的作用提供了动力,这可能对化妆品和医学领域产生影响。

更新日期:2018-12-30
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