Analysis of a unique interaction between the complement regulatory protein factor H and the periodontal pathogen Treponema denticola.
Analysis of a unique interaction between the complement regulatory protein factor H and the periodontal pathogen Treponema denticola.
复制标题
补体调节蛋白 H 因子与牙周病原体齿垢密螺旋体之间独特相互作用的分析。
DOI：
10.1128/iai.01544-08
复制
发表时间：
2009
影响因子：
3.1
通讯作者：
Marconi,RichardT
中科院分区：
文献类型：
--
作者：
McDowell,JohnV;Huang,Bernice;Fenno,JChristopher;Marconi,RichardT
Treponema denticola, a spirochete associated with periodontitis, is abundant at the leading edge of subgingival plaque, where it interacts with gingival epithelia.T. denticolaproduces a number of virulence factors, including dentilisin, a protease which is cytopathic to host cells, and FhbB, a uniqueT. denticolalipoprotein that binds complement regulatory proteins. Earlier analyses suggested that FhbB specifically bound to factor H (FH)-like protein 1 (FHL-1). However, by using dentilisin-deficient mutants ofT. denticola, we found thatT. denticolapreferentially binds FH and not FHL-1, and that FH is then cleaved by dentilisin to yield an FH subfragment of ∼50 kDa. FH bound to dentilisin-deficient mutants but was not cleaved and retained its ability to serve as a cofactor for factor I in the cleavage of C3b. To assess the molecular basis of the interaction of FhbB with FH, mutational analyses were conducted. Replacement of specific residues in widely separated domains of FhbB and disruption of a central alpha helix with coiled-coil formation probability attenuated or eliminated FH binding. The data presented here are the first to demonstrate the retention at the cell surface of a proteolytic cleavage product of FH. The precise role of this FH fragment in the host-pathogen interaction remains to be determined.
