HYDROPHOBIC SURFACE PROTEIN MASKING BY THE OPPORTUNISTIC FUNGAL PATHOGEN CANDIDA-ALBICANS
HYDROPHOBIC SURFACE PROTEIN MASKING BY THE OPPORTUNISTIC FUNGAL PATHOGEN CANDIDA-ALBICANS
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DOI：
10.1128/iai.60.4.1499-1508.1992
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发表时间：
1992-04-01
影响因子：
3.1
通讯作者：
HAZEN, BW
中科院分区：
文献类型：
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作者：
HAZEN, KC;HAZEN, BW
对白色念珠菌的疏水性和亲水性酵母细胞表面蛋白进行超微结构和生化分析。疏水和亲水酵母细胞分别通过在 23 和 37 摄氏度下生长获得。此外，通过衣霉素和二硫苏糖醇处理，亲水性酵母细胞转化为表面疏水性。当检查冷冻蚀刻的细胞时，温度诱导的亲水性细胞具有长（0.198μm）、紧凑、均匀分布的原纤维，而温度诱导的疏水性细胞具有短（0.085μm）、钝的原纤维。疏水性微球与疏水性细胞的附着发生在短原纤维层的基底和内部。二硫苏糖醇诱导的疏水细胞去除了长原纤维；衣霉素诱导的疏水性细胞保留了一些长原纤维，但与未处理的对照相比，原纤维不太紧凑且更聚集。这些结果表明，长原纤维阻止疏水微球附着到细胞表面的疏水区域。通过评估原纤维密度和排列不同的疏水性酵母细胞群的疏水性亲和力证实了这一点。通过疏水相互作用色谱-高效液相色谱分离后，对来自疏水性和亲水性细胞的 I-125 标记的表面蛋白进行比较，并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和放射自显影进行分析。酵母细胞群具有相似分子量（> 200 kDa）的亲水性蛋白质，但亲水性细胞至少具有两种额外的蛋白质（约63和69至71 kDa）。疏水性表面蛋白似乎是相似的。然而，疏水性细胞的放射性标记疏水性蛋白总量比亲水性细胞高约 10 倍。该结果与超微结构观察一致，超微结构观察表明酵母细胞表面疏水性蛋白质被亲水性高分子质量表面原纤维掩盖。综上所述，数据表明酵母细胞的疏水性不是由表面疏水性蛋白质的差异决定的，而是由亲水性表面原纤维的存在决定的。
Ultrastructural and biochemical analyses of hydrophobic and hydrophilic yeast cell surface proteins of Candida albicans were performed. Hydrophobic and hydrophilic yeast cells were obtained by growth at 23 and 37-degrees-C, respectively. In addition, hydrophilic yeast cells were converted to surface hydrophobicity by treatment with tunicamycin and dithiothreitol. When freeze-etched cells were examined, the temperature-induced hydrophilic cells had long (0.198-mu-m), compact, evenly distributed fibrils while temperature-induced hydrophobic cells had short (0.085-mu-m), blunt fibrils. Hydrophobic microsphere attachment to the hydrophobic cells occurred at the basement of and within the short fibril layer. Dithiothreitol-induced hydrophobic cells had the long fibrils removed; tunicamycin-induced hydrophobic cells retained some of the long fibrils, but the fibrils were less compact and more aggregated than the untreated controls. These results suggest that the long fibrils prevent hydrophobic microsphere attachment to the hydrophobic area of the cell surface. This was confirmed by assessing the hydrophobic avidity of hydrophobic yeast cell populations differing in fibril density and arrangement. I-125-labelled surface proteins from hydrophobic and hydrophilic cells were compared after separation by hydrophobic interaction chromatography-high-performance liquid chromatography and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The yeast cell populations had hydrophilic proteins of similar molecular masses (> 200 kDa), but the hydrophilic cells possessed at least two additional proteins (ca. 63 and 69 to 71 kDa). Hydrophobic surface proteins appeared to be similar. However, the amount of total radiolabelled hydrophobic proteins was approximately 10-fold higher for the hydrophobic cells than for the hydrophilic cells. This result agrees with the ultrastructural observations which showed that yeast cell surface hydrophobic proteins are masked by hydrophilic high-molecular-mass surface fibrils. Taken together, the data indicate that yeast cell hydrophobicity is not determined by differences in surface hydrophobic proteins but by the presence of hydrophilic, surface fibrils.