Evaluation of the recombinant protein Tp0965 of Treponema pallidum as candidate antigen for serological diagnosis of syphilis

Runina, A. V.; Старовойтова, А. С.; Deryabin, D. G.; Kubanov, Alexey А.

doi:10.15690/vramn653

Cited by 8 publications

(3 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tp0965 is a putative membrane fusion protein and belongs to efflux transporter resistance‐nodulation‐division family MFP subunit . Our and other previous study suggested that recombinant protein Tp0965 showed excellent antigenicity and immunoreactivity …”

Section: Introductionmentioning

confidence: 59%

“…7 Our and other previous study suggested that recombinant protein Tp0965 showed excellent antigenicity and immunoreactivity. 10,11 Endothelial dysfunction plays key roles in vascular intimal inflammation by initiating the formation of atherosclerotic plaques and thrombosis. 12 It is also the key step of systemic dissemination and pathophysiological basic of syphilis.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chemerin induced by Treponema pallidum predicted membrane protein Tp0965 mediates the activation of endothelial cell via MAPK signaling pathway

Zhang

Wang²,

Yang

2019

J of Cellular Biochemistry

View full text Add to dashboard Cite

Chemerin, a chemoattractant protein, is involved in endothelial dysfunction and vascular inflammation in pathological conditions. In a recent study, we observed the upregulation of chemerin in endothelial cells following in vitro treatment with Treponema pallidum. Here, we investigated the role of chemerin in endothelial cells activation induced by the T. pallidum predicted membrane protein Tp0965. Following stimulation of human umbilical vein endothelial cells (HUVECs) with Tp0965, chemerin and its receptor chemerin receptor 23 (ChemR23) were upregulated, companied with elevated expression of Toll-like receptor 2. Furthermore, chemerin from HUVECs activated endothelial cells via chemerin/ChemR23 signaling in an autocrine/paracrine manner, characterized by upregulated expression of intercellular adhesion molecule 1, E-selectin, and matrix metalloproteinase-2. Activation of endothelial cells depended on the mitogen-activated protein kinase signaling pathway. In addition, Tp0965induced chemerin promoted THP-1-derived macrophages migration to endothelial cells, also via the chemerin/ChemR23 pathway. The RhoA/ROCK signaling pathway was also involved in THP-1-derived macrophages migration in response to chemerin/ChemR23. Our results highlight the role of Tp0965induced chemerin in endothelial cells dysfunction, which contributes to the immunopathogenesis of vascular inflammation of syphilis. K E Y W O R D S chemerin, endothelial cell, membrane protein, syphilis, Treponema pallidum

show abstract

Section: Introductionmentioning

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Chemerin induced by Treponema pallidum predicted membrane protein Tp0965 mediates the activation of endothelial cell via MAPK signaling pathway

Zhang

Wang²,

Yang

2019

J of Cellular Biochemistry

View full text Add to dashboard Cite

show abstract

“…Tp0965 is a putative membrane fusion protein and belongs to efflux transporter RND family MFP subunit [7]. Our and others previous study suggested that recombinant protein Tp0965 showed excellent antigenicity and immunoreactivity [10-11].…”

Section: Introductionmentioning

confidence: 99%

Chemerin Induced byTreponema pallidumPredicted Membrane Protein Tp0965 Mediates Endothelial Dysfunction via Activating MAPK Signaling Pathway

Zhang

Yang

Wang

2018

Preprint

View full text Add to dashboard Cite

24Chemerin, a chemoattractant protein, is involved in endothelial dysfunction and 25 vascular inflammation in pathological conditions. In a recent study, we observed the 26 upregulation of chemerin in endothelial cells following in vitro treatment with T. 27 pallidum. Here, we investigated the role of chemerin in endothelial cells dysfunction 28 induced by the T. pallidum predicted membrane protein Tp0965. Following 29 stimulation of human umbilical vein endothelial cells (HUVECs) with Tp0965, 30 chemerin and its ChemR23 receptor were up-regulated, companied with elevated 31 expression of TLR2. Furthermore, chemerin from HUVECs activated endothelial cells 32 via chemerin/ChemR23 signaling in an autocrine/paracrine manner, characterized by 33 upregulated expression of ICAM-1, E-selectin and MMP-2. Activation of endothelial 34 cells depended on the MAPK signaling pathway. In addition, Tp0965-induced 35 chemerin promoted monocytes migration to endothelial cells, also via 36 chemerin/ChemR23 pathway. The RhoA/ROCK signaling pathway was also involved 37 in monocytes migration in response to chemerin/ChemR23. Our results highlight the 38 role of Tp0965-induced chemerin in endothelial cells dysfunction, which contributes to 39 the immunopathogenesis of vascular inflammation of syphilis.40 Author summary 41 Treponema pallidum is the spirochete of syphilis, which causes a chronic system 42 inflammation. Endothelium damage caused by this bacterium is the key step in the 43 systemic dissemination and pathophysiology of syphilis, particularly cardiovascular 44 syphilis and neurosyphilis. In this study, we show a novel molecular mechanism of 3 45 endothelium damage induce by Treponema pallidum predicted membrane protein 46 Tp0965. Chemerin is a recently identified adipocytokine and chemoattractant protein 47 with a crucial role in endothelial dysfunction and vascular inflammation in pathological 48 conditions. Our data show that Tp0965 up-regulated the expression of chemerin and its 49 ChemR23 receptor by endothelial cells in vitro. Furthermore, chemerin from HUVECs 50 activated endothelial cells via chemerin/ChemR23 signaling in an autocrine/paracrine 51 manner and depended on the MAPK signaling pathway. In addition, Tp0965-induced 52 chemerin promoted monocytes migration to endothelial cells, also via 53 chemerin/ChemR23 pathway. The RhoA/ROCK signaling pathway was also involved 54 in monocytes migration in response to chemerin/ChemR23. These findings contribute 55 to the immunopathogenesis of vascular inflammation of syphilis. 56 57 Introduction 58 Treponema pallidum subsp. pallidum (T. pallidum) is the spirochete of syphilis, a 59 sexually transmitted infection that remains an important public health problem around 60 the world [1]. Infection by this bacterium causes a chronic system inflammation, and if 61 untreated can seriously and irreversibly damage the nervous and cardiovascular system.62 Cardiovascular syphilis is associated with multiple clinical syndromes, of which aortic 63 aneurysms, aortic insufficiency,...

show abstract

Immunochip for Syphilis Serodiagnostics with the Use of Extended Array of Treponema pallidum Recombinant Antigens

et al. 2018

View full text Add to dashboard Cite

Evaluation of the recombinant protein Tp0965 of Treponema pallidum as candidate antigen for serological diagnosis of syphilis

Cited by 8 publications

References 8 publications

Chemerin induced by Treponema pallidum predicted membrane protein Tp0965 mediates the activation of endothelial cell via MAPK signaling pathway

Chemerin induced by Treponema pallidum predicted membrane protein Tp0965 mediates the activation of endothelial cell via MAPK signaling pathway

Chemerin Induced byTreponema pallidumPredicted Membrane Protein Tp0965 Mediates Endothelial Dysfunction via Activating MAPK Signaling Pathway

Immunochip for Syphilis Serodiagnostics with the Use of Extended Array of Treponema pallidum Recombinant Antigens

Contact Info

Product

Resources

About