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Pheromone peptide cOB1 from native Enterococcus faecalis forms amyloid-like structures: A new paradigm for peptide pheromones.
Journal of Peptide Science ( IF 1.8 ) Pub Date : 2019-07-17 , DOI: 10.1002/psc.3178
Shalini Gour 1 , Vijay Kumar 1 , Monika Rana 2 , Jay Kant Yadav 1
Affiliation  

Pheromone peptides are an important component of bacterial quorum‐sensing system. The pheromone peptide cOB1 (VAVLVLGA) of native commensal Enterococcus faecalis has also been identified as an antimicrobial peptide (AMP) and reported to kill the prototype clinical isolate strain of E. faecalis V583. In this study, the pheromone peptide cOB1 has shown to form amyloid‐like structures, a characteristic which is never reported for a pheromone peptide so far. With in silico analysis, the peptide was predicted to be highly amyloidogenic. Further, under experimental conditions, cOB1 formed aggregates displaying characteristics of amyloid structures such as bathochromic shift in Congo red absorbance, enhancement in thioflavin T fluorescence, and fibrillar morphology under transmission electron microscopy. This novel property of pheromone peptide cOB1 may have some direct effects on the binding of the pheromone to the receptor cells and subsequent conjugative transfer, making this observation more important for the therapeutics, dealing with the generation of virulent and multidrug‐resistant pathogenic strains.

中文翻译:

来自天然粪肠球菌的信息素肽cOB1形成淀粉样结构:肽信息素的新范式。

信息素肽是细菌群体感应系统的重要组成部分。天然共生肠球菌肠球菌的信息素肽cOB1(VAVLVLGA)也已被鉴定为抗菌肽(AMP),据报道杀死了粪肠球菌V583的原型临床分离株。在这项研究中,信息素肽cOB1已显示出形成淀粉样结构,到目前为止,尚未对信息素肽进行报道。与计算机经分析,该肽被预测为高度淀粉样蛋白。此外,在实验条件下,cOB1形成聚集体,显示出淀粉样结构的特征,如刚果红吸收的红移,硫黄素T荧光增强和透射电子显微镜下的原纤维形态。信息素肽cOB1的这一新特性可能对信息素与受体细胞的结合以及随后的共轭转移具有某些直接影响,这使得该观察结果对于治疗具有毒性和多重耐药性的病原体菌株的治疗更为重要。
更新日期:2019-07-17
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