Role of multifunctional protein, GAPDH, associated with bacteria and human cells in infection by periodontopathic bacteria

本研究表明口腔链球菌ATCC 9811 GAPDH的166 ~ 183个氨基酸残基中可能存在牙龈卟啉菌菌毛的结合结构域。与S. oral alis ATCC 9811 GAPDH氨基酸残基166 ~ 183对应的肽（pep166-183）抑制了几种不同类型FimA的口腔链球菌和牙龈卟啉卟啉菌的菌间生物膜形成。pep166-183具有较强的抑制牙龈假单胞菌与几种口腔细菌间生物膜形成的活性，表现出较强的细胞表面相关GAPDH活性。此外，我们发现人类细胞GAPDH中牙龈假单胞菌菌毛的结合域可能与口腔假单胞菌GAPDH存在相同的结合域。

This study showed that a binding domain for P. gingivalis fimbriae may exist within amino acid residues 166 to 183 of S. oralis ATCC 9811 GAPDH. The peptide corresponding to amino acid residues 166 to 183 of S. oralis ATCC 9811 GAPDH (pep166-183) inhibited the interbacterial biofilm formation by several oral streptococci and P. gingivalis strains with different types of FimA. pep166-183 strongly inhibited biofilm formation between P. gingivalis and several oral bacteria which showed relatively strong cell surface-associated GAPDH activity. Moreover, we found that the binding domain for P. gingivalis fimbriae in human cell GAPDH may exist within the same domain as in S. oralis GAPDH.