title: Recombinant Treponema pallidum protein Tp0965 activates endothelial cells and increases the permeability of endothelial cell monolayer.
abstract: The recombinant Treponema pallidum protein Tp0965 (rTp0965), one of the many proteins derived from the genome of T. pallidum subsp. pallidum, shows strong immunogenicity and immunoreactivity. In this study, we investigated the effects of rTp0965 on the endothelial barrier. Treatment of human umbilical vein endothelial cells (HUVECs) with rTp0965 resulted in increased levels of ICAM-1, E-selectin, and MCP-1 mRNA and protein expression. These increases contributed to the adhesion and chemataxis of monocytes (THP-1 cells) to HUVECs preincubated with rTp0965. In addition, rTp0965 induced reorganization of F-actin and decreased expression of claudin-1 in HUVECs. Interestingly, inhibition of the RhoA/ROCK signal pathway protected against rTp0965-induced higher endothelial permeability as well as transendothelial migration of monocytes. These data indicate that Tp0965 protein may play an important role in the immunopathogenesis of syphilis.
authors.affiliation: Department of Dermatology, Wuxi Second Affiliated Hospital of Nanjing Medical University, Wuxi, Jiangsu Province, China.
authors.forename: Rui-Li
authors.initials: RL
authors.lastname: Zhang
authors.affiliation: Institute of Dermatology, Chinese Academy of Medical Sciences & Peking Union Medical College, & National Center for STD Control, China Centers for Diseases Control and Prevention, Nanjing, Jiangsu Province, China.
authors.forename: Jing-Ping
authors.initials: JP
authors.lastname: Zhang
authors.affiliation: Institute of Dermatology, Chinese Academy of Medical Sciences & Peking Union Medical College, & National Center for STD Control, China Centers for Diseases Control and Prevention, Nanjing, Jiangsu Province, China.
authors.forename: Qian-Qiu
authors.initials: QQ
authors.lastname: Wang
mesh_terms: D000199:Actins / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology; D002463:Cell Membrane Permeability / Q000502:physiology*; D002478:Cells, Cultured; D018932:Chemokine CCL2 / Q000096:biosynthesis / Q000235:genetics; D002633:Chemotaxis / Q000502:physiology; D062445:Claudin-1 / Q000096:biosynthesis; D019040:E-Selectin / Q000096:biosynthesis / Q000235:genetics; D061307:Human Umbilical Vein Endothelial Cells / Q000378:metabolism*; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000096:biosynthesis / Q000235:genetics; D050576:Membrane Fusion Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D009000:Monocytes / Q000502:physiology; D012333:RNA, Messenger / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000494:pharmacology; D015398:Signal Transduction; D013587:Syphilis / Q000473:pathology; D019108:Tight Junctions / Q000378:metabolism; D014210:Treponema pallidum / Q000472:pathogenicity*; D020742:rhoA GTP-Binding Protein / Q000037:antagonists & inhibitors
chemical_list: D000199:Actins; D001426:Bacterial Proteins; C111835:CCL2 protein, human; D018932:Chemokine CCL2; D062445:Claudin-1; D019040:E-Selectin; D050576:Membrane Fusion Proteins; D012333:RNA, Messenger; D011994:Recombinant Proteins; C066737:RHOA protein, human; D018799:Intercellular Adhesion Molecule-1; D020742:rhoA GTP-Binding Protein