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

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

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

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.

scholarly journals Increasing the Interaction of Borrelia burgdorferi with Decorin Significantly Reduces the 50 Percent Infectious Dose and Severely Impairs Dissemination

2007 ◽  
Vol 75 (9) ◽  
pp. 4272-4281 ◽  
Author(s):  
Qilong Xu ◽  
Sunita V. Seemanaplli ◽  
Kristy McShan ◽  
Fang Ting Liang
Keyword(s):  
Borrelia Burgdorferi ◽  
Severe Combined Immunodeficiency ◽  
Protein A ◽  
Antigen Expression ◽  
In Vitro Assays ◽  
Infectious Dose ◽  
Surface Antigen Expression ◽  
Immunocompetent Mice ◽  
Surface Adhesins

ABSTRACT Tight regulation of surface antigenic expression is crucial for the pathogenic strategy of the Lyme disease spirochete, Borrelia burgdorferi. Here, we report the influence of increasing expression of decorin-binding protein A (DbpA), one of the most investigated spirochetal surface adhesins, on the 50% infectious dose (ID50), dissemination, tissue colonization, pathogenicity, and persistence of B. burgdorferi in the murine host. Our in vitro assays showed that increasing DbpA expression dramatically increased the interaction of B. burgdorferi with decorin and sensitivity to growth inhibition/killing by anti-DbpA antibodies; however, this increased interaction did not affect spirochetal growth and replication in the presence of decorin. Increasing DbpA expression significantly reduced ID50 values and severely impaired dissemination in severe combined immunodeficiency (SCID) and immunocompetent mice. During infection of SCID mice, B. burgdorferi with increased DbpA expression was able to effectively colonize heart and skin tissues, but not joint tissues, completely abrogating arthritis virulence. Although increasing DbpA expression did not affect spirochetal persistence in the skin, it diminished the ability of B. burgdorferi to persist in the heart and joint tissues during chronic infection of immunocompetent mice. Taken together, the study highlights the importance of controlling surface antigen expression in the infectivity, dissemination, tissue colonization, pathogenicity, and persistence of B. burgdorferi during mammalian infection.

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