Open AccessAdpC Is a Prevotella intermedia 17 Leucine-Rich Repeat Internalin-Like Protein
Author(s) -
Divya Iyer,
Cecilia Anaya-Bergman,
Kathryn Jones,
Sai S. Yanamandra,
Dipanwita Sengupta,
Hiroshi Miyazaki,
Janina P. Lewis
Publication year - 2010
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.00510-09
Subject(s) - biology , prevotella intermedia , microbiology and biotechnology , escherichia coli , porphyromonas gingivalis , gene , bacteria , biochemistry , genetics
The oral bacteriumPrevotella intermedia attaches to and invades gingival epithelial cells, fibroblasts, and endothelial cells. Several genes encoding proteins that mediate both the adhesion and invasion processes are carried on the genome of this bacterium. Here, we characterized one such protein, AdpC, belonging to the leucine-rich repeat (LRR) protein family. Bioinformatics analysis revealed that this protein shares similarity with theTreponema pallidum LRR (LRRTP ) family of proteins and contains six LRRs. Despite the absence of a signal peptide, this protein is localized on the bacterial outer membrane, indicating that it is transported through an atypical secretion mechanism. The recombinant form of this protein (rAdpC) was shown to bind fibrinogen. In addition, the heterologous host strainEscherichia coli BL21 expressing rAdpC (V2846) invaded fibroblast NIH 3T3 cells at a 40-fold-higher frequency than controlE. coli BL21 cells expressing a shamP. intermedia 17 protein. Although similar results were obtained by using human umbilical vein endothelial cells (HUVECs), only a 3-fold-increased invasion of V2846 into oral epithelial HN4 cells was observed. Thus, AdpC-mediated invasion is cell specific. This work demonstrated that AdpC is an important invasin protein ofP. intermedia 17.