Lucchese A, Guida A, Capone G, Donnarumma G, Laino L, Petruzzi M, Serpico R, Silvestre F, Gargari M
Multidisciplinary Department of Medical-Surgical and Odontostomatological Specialties, Second University of Naples SUN, Naples, Italy.
Postgraduate School in Oral Surgery, Department of Neurosciences, Reproductive and Odontostomatological Sciences, University of Naples "Federico II", Naples, Italy.
Oral Implantol (Rome). 2016 Nov 13;9(2):83-88. doi: 10.11138/orl/2016.9.2.083. eCollection 2016 Apr-Jun.
To identify potential antigenic targets for Porphyromonas gingivalis vaccine development.
In the present study, we analyzed the Porphyromonas gingivalis, fimA type II primary amino acid sequence and characterized the similarity to the human proteome at the pentapeptide level.
We found that exact peptide-peptide profiling of the fimbrial antigen the human proteome shows that only 19 out of 344 fimA type II pentapeptides are uniquely owned by the bacterial protein.
The concept that protein immunogenicity is allocated in rare peptide sequences and the search the Porphyromonas gingivalis fimA type II sequence for peptides unique to the bacterial protein and absent in the human host, might be used in new therapeutical approaches as a significant adjunct to current periodontal therapies.
确定牙龈卟啉单胞菌疫苗开发的潜在抗原靶点。
在本研究中，我们分析了牙龈卟啉单胞菌fimA II型的一级氨基酸序列，并在五肽水平上对其与人类蛋白质组的相似性进行了表征。
我们发现，菌毛抗原与人类蛋白质组的精确肽段分析表明，344个fimA II型五肽中只有19个为该细菌蛋白所特有。
蛋白质免疫原性存在于稀有肽序列中的概念，以及在牙龈卟啉单胞菌fimA II型序列中寻找细菌蛋白特有的、人类宿主中不存在的肽段，可能作为当前牙周治疗的重要辅助手段用于新的治疗方法中。
