Byers H L, Tarelli E, Homer K A, Hambley H, Beighton D
Joint Microbiology Research Unit, Faculty of Clinical Dentistry, King's College School of Medicine and Dentistry, London, United Kingdom.
J Dent Res. 1999 Jul;78(7):1370-80. doi: 10.1177/00220345990780071201.
Viridans streptococci have emerged as major opportunistic pathogens. We suggest that for these bacteria to proliferate in vivo and cause disease, they must utilize host tissue components. We have therefore examined the ability of all recognized species of viridans streptococci to liberate and utilize the constituent sugars of the glycans of the extensively sialylated human serum alpha1-acid glycoprotein (AGP) as the sole source of carbohydrate to support in vitro growth. Analysis of residual glycans following bacterial growth was performed by high-pH anion exchange chromatography with pulsed amperometric detection and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Only those species which produced sialidase-namely, Streptococcus oralis, S. intermedius, and S. defectivus--grew on AGP. The extent of degradation of glycans was dependent on the particular glycosidases produced by the bacteria. S. defectivus produced only a sialidase which released the terminal N-acetylneuraminic acid residues of the glycans, and the liberated sugar was utilized. S. intermedius also produced beta-galactosidase and beta-N-acetylglucosaminidase, which removed galactose and N-acetylglucosamine from desialylated glycans, all of which again were utilized by the organism. S. oralis produced beta-galactosidase, beta-N-acetylglucosaminidase, and alpha-fucosidase and novel alpha- and beta-mannosidases which were apparent only from the analysis of the residual sugars of AGP. S. oralis cleaved all the sugars from AGP except for 22% of the N-acetylglucosamine. The residual N-acetylglucosamine residues remaining were those linked to the asparagine of the peptide backbone. All the monosaccharides released by S. oralis from AGP, with the exception of fucose, were utilized. Sialidase production may be a key factor for growth of these species of viridans streptococci on glycoproteins in vivo, since they are commonly associated with extra-oral diseases, with S. oralis emerging as an important pathogen.
草绿色链球菌已成为主要的机会致病菌。我们认为,这些细菌要在体内增殖并引发疾病,就必须利用宿主组织成分。因此,我们检测了所有已知的草绿色链球菌物种释放并利用广泛唾液酸化的人血清α1-酸性糖蛋白(AGP)聚糖中组成糖作为唯一碳水化合物来源以支持体外生长的能力。细菌生长后对残留聚糖的分析通过高pH阴离子交换色谱结合脉冲安培检测以及基质辅助激光解吸电离飞行时间质谱进行。只有那些产生唾液酸酶的物种,即口腔链球菌、中间链球菌和缺陷链球菌,能够在AGP上生长。聚糖的降解程度取决于细菌产生的特定糖苷酶。缺陷链球菌仅产生一种释放聚糖末端N-乙酰神经氨酸残基的唾液酸酶,释放出的糖被利用。中间链球菌还产生β-半乳糖苷酶和β-N-乙酰氨基葡萄糖苷酶,它们从去唾液酸化的聚糖中去除半乳糖和N-乙酰氨基葡萄糖,所有这些糖又被该生物体利用。口腔链球菌产生β-半乳糖苷酶、β-N-乙酰氨基葡萄糖苷酶和α-岩藻糖苷酶以及仅从AGP残留糖分析中才明显的新型α-和β-甘露糖苷酶。口腔链球菌从AGP中裂解出所有的糖,除了22%的N-乙酰氨基葡萄糖。剩余的N-乙酰氨基葡萄糖残基是与肽主链天冬酰胺相连的那些。口腔链球菌从AGP中释放的所有单糖,除了岩藻糖,都被利用。唾液酸酶的产生可能是这些草绿色链球菌物种在体内糖蛋白上生长的关键因素,因为它们通常与口腔外疾病相关,其中口腔链球菌已成为一种重要的病原体。