Isoforskolin and Cucurbitacin IIa promote the expression of anti-inflammatory regulatory factor SIGIRR in human macrophages stimulated with Borrelia burgdorferi basic membrane protein A

2020 ◽  
Vol 88 ◽  
pp. 106914
Author(s):  
Yun Peng ◽  
Taigui Chen ◽  
Lisha Luo ◽  
Lianbao Li ◽  
Wenjing Cao ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Borrelia Burgdorferi ◽  
Protein A ◽  
Regulatory Factor ◽  
Human Macrophages ◽  
Anti Inflammatory

Borrelia burgdorferi basic membrane protein A could induce chemokine production in murine microglia cell line BV2

2017 ◽  
Vol 111 ◽  
pp. 174-181 ◽  
Author(s):  
Hua Zhao ◽  
Aihua Liu ◽  
Yuhui Cui ◽  
Zhang Liang ◽  
Bingxue Li ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Borrelia Burgdorferi ◽  
Cell Line ◽  
Protein A ◽  
Chemokine Production ◽  
Microglia Cell ◽  
Murine Microglia

Borrelia Burgdorferi Basic Membrane Protein a Initiates Arthritis in the Tree Shrew

2021 ◽  
Author(s):  
Bingxue Li ◽  
Peng Yue ◽  
Jiaru Yang ◽  
Su-Yi Luo ◽  
Guozhong Zhou ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Borrelia Burgdorferi ◽  
Tree Shrew ◽  
Protein A

scholarly journals Borrelia burgdorferi basic membrane protein A stimulates murine macrophage to secrete specific chemokines

2018 ◽  
Vol 15 (13) ◽  
pp. 1473-1479
Author(s):  
Yun Peng ◽  
Zhang Liang ◽  
Aihua Liu ◽  
Erhua Li ◽  
Xiting Dai ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Borrelia Burgdorferi ◽  
Protein A ◽  
Murine Macrophage

scholarly journals Cutting Edge: Outer Membrane Protein A (OmpA) Binds to and Activates Human Macrophages

2000 ◽  
Vol 165 (5) ◽  
pp. 2335-2340 ◽  
Author(s):  
Caroline Soulas ◽  
Thierry Baussant ◽  
Jean-Pierre Aubry ◽  
Yves Delneste ◽  
Nicolas Barillat ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Cutting Edge ◽  
Human Macrophages ◽  
Outer Membrane Protein A

scholarly journals Interleukin-10 Anti-Inflammatory Response to Borrelia burgdorferi, the Agent of Lyme Disease: a Possible Role for Suppressors of Cytokine Signaling 1 and 3

2006 ◽  
Vol 74 (10) ◽  
pp. 5780-5789 ◽  
Author(s):  
Vida A. Dennis ◽  
Ayanna Jefferson ◽  
Shree R. Singh ◽  
Frédéric Ganapamo ◽  
Mario T. Philipp
Keyword(s):  
Borrelia Burgdorferi ◽  
Inflammatory Cytokines ◽  
Protein A ◽  
Surface Protein ◽  
Interleukin 10 ◽  
Cytokine Signaling ◽  
Socs3 Expression ◽  
Suppressors Of Cytokine Signaling ◽  
Anti Inflammatory ◽  
Factor Α

ABSTRACT It has been established that interleukin-10 (IL-10) inhibits inflammatory cytokines produced by macrophages in response to Borrelia burgdorferi or its lipoproteins. The mechanism by which IL-10 exerts this anti-inflammatory effect is still unknown. Recent findings indicate that suppressors of cytokine signaling (SOCS) proteins are induced by cytokines and Toll-like receptor (TLR)-mediated stimuli, and in turn they can down-regulate cytokine and TLR signaling in macrophages. Because it is known that SOCS are induced by IL-10 and that B. burgdorferi and its lipoproteins most likely interact via TLR2 or the heterodimers TLR2/1 and/or TLR2/6, we hypothesized that SOCS are induced by IL-10 and B. burgdorferi and its lipoproteins in macrophages and that SOCS may mediate the inhibition by IL-10 of concomitantly elicited cytokines. We report here that mouse J774 macrophages incubated with IL-10 and added B. burgdorferi spirochetes (freeze-thawed, live, or sonicated) or lipidated outer surface protein A (L-OspA) augmented their SOCS1/SOCS3 mRNA and protein expression, with SOCS3 being more abundant. Pam3Cys, a synthetic lipopeptide, also induced SOCS1/SOCS3 expression under these conditions, but unlipidated OspA was ineffective. Neither endogenous IL-10 nor the translation inhibitor cycloheximide blocked SOCS1/SOCS3 induction by B. burgdorferi and its lipoproteins, indicating that the expression of other genes is not required. This temporally correlated with the IL-10-mediated inhibition of the inflammatory cytokines IL-1β, IL-6, IL-12p40, IL-18, and tumor necrosis factor α. Our data are evidence to suggest that expression of SOCS is part of the mechanism of IL-10-mediated inhibition of inflammatory cytokines elicited by B. burgdorferi and its lipoproteins.

Overexpression of Outer Membrane Protein A Is a Risk Factor for Mortality in Escherichia coli Bloodstream Infections

2019 ◽  
Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Risk Factor ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Bloodstream Infections ◽  
Outer Membrane Protein A

scholarly journals Anaplasma phagocytophilum Outer Membrane Protein A Interacts with Sialylated Glycoproteins To Promote Infection of Mammalian Host Cells

2012 ◽  
Vol 80 (11) ◽  
pp. 3748-3760 ◽  
Author(s):  
Nore Ojogun ◽  
Amandeep Kahlon ◽  
Stephanie A. Ragland ◽  
Matthew J. Troese ◽  
Juliana E. Mastronunzio ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Anaplasma Phagocytophilum ◽  
Protein A ◽  
Host Cells ◽  
Mammalian Host ◽  
Content Type ◽  
Outer Membrane Protein A ◽  
Sialylated Glycoproteins

ABSTRACTAnaplasma phagocytophilumis the tick-transmitted obligate intracellular bacterium that causes human granulocytic anaplasmosis (HGA).A. phagocytophilumbinding to sialyl Lewis x (sLex) and other sialylated glycans that decorate P selectin glycoprotein 1 (PSGL-1) and other glycoproteins is critical for infection of mammalian host cells. Here, we demonstrate the importance ofA. phagocytophilumouter membrane protein A (OmpA) APH_0338 in infection of mammalian host cells. OmpA is transcriptionally induced during transmission feeding ofA. phagocytophilum-infected ticks on mice and is upregulated during invasion of HL-60 cells. OmpA is presented on the pathogen's surface. Sera from HGA patients and experimentally infected mice recognize recombinant OmpA. Pretreatment ofA. phagocytophilumorganisms with OmpA antiserum reduces their abilities to infect HL-60 cells. The OmpA N-terminal region is predicted to contain the protein's extracellular domain. GlutathioneS-transferase (GST)-tagged versions of OmpA and OmpA amino acids 19 to 74 (OmpA19-74) but not OmpA75-205bind to, and competitively inhibitA. phagocytophiluminfection of, host cells. Pretreatment of host cells with sialidase or trypsin reduces or nearly eliminates, respectively, GST-OmpA adhesion. Therefore, OmpA interacts with sialylated glycoproteins. This study identifies the firstA. phagocytophilumadhesin-receptor pair and delineates the region of OmpA that is critical for infection.

Sign in / Sign up

Export Citation Format

Share Document