Outer membrane protein A (OmpA) is a potential virulence factor of Vibrio alginolyticus strains isolated from diseased fish

2019 ◽  
Vol 43 (2) ◽  
pp. 275-284 ◽  
Author(s):  
Supansa Bunpa ◽  
Nattarika Chaichana ◽  
Jade L. L. Teng ◽  
Hwei Huih Lee ◽  
Patrick C. Y. Woo ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Virulence Factor ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Vibrio Alginolyticus ◽  
Potential Virulence Factor ◽  
Diseased Fish ◽  
Outer Membrane Protein A

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 Recombinant outer membrane protein A fragments protect against Escherichia coli meningitis

2016 ◽  
Vol 49 (3) ◽  
pp. 329-334 ◽  
Author(s):  
Wen-Shyang Hsieh ◽  
Yi-Yuan Yang ◽  
Hsin-Yi Yang ◽  
Yu-Shan Huang ◽  
Hsueh-Hsia Wu
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Outer Membrane Protein A

scholarly journals The Interaction ofN-Glycans in Fcγ Receptor I α-Chain withEscherichia coliK1 Outer Membrane Protein A for Entry into Macrophages

2014 ◽  
Vol 289 (45) ◽  
pp. 30937-30949 ◽  
Author(s):  
Subramanian Krishnan ◽  
Fan Liu ◽  
Ravinder Abrol ◽  
Jacqueline Hodges ◽  
William A. Goddard ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Fcγ Receptor ◽  
Outer Membrane Protein A ◽  
Α Chain
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