ArticleInfection and immunity2012
Anaplasma phagocytophilum outer membrane protein A interacts with sialylated glycoproteins to promote infection of mammalian host cells.
Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Article
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- Distinct modes of cell division drivemBio · 2025Article
- Genomic characters ofEmerging microbes & infections · 2024Article
- Identification ofInfection and immunity · 2024Article
- Aptamer selection against cell extracts containing the zoonotic obligate intracellular bacterium, Anaplasma phagocytophilum.Scientific reports · 2024Article
- A glimpse into the world of microRNAs and their putative roles in hard ticks.Frontiers in cell and developmental biology · 2024Review
- Current vaccines, experimental immunization trials, and new perspectives to control selected vector borne blood parasites of veterinary importance.Frontiers in veterinary science · 2024Review
- Article
- Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection.Infection and immunity · 2022Article
- Review
- Epidemiology, Diagnosis, and Control of Canine Infectious Cyclic Thrombocytopenia and Granulocytic Anaplasmosis: Emerging Diseases of Veterinary and Public Health Significance.Veterinary sciences · 2021Review
- Immunization against Anaplasma phagocytophilum Adhesin Binding Domains Confers Protection against Infection in the Mouse Model.Infection and immunity · 2020Article
- Article
- Epidemiology of Nucleus-Dwelling Holospora: Infection, Transmission, Adaptation, and Interaction with Paramecium.Results and problems in cell differentiation · 2020Review
- Ehrlichia chaffeensis EplA Interaction With Host Cell Protein Disulfide Isomerase Promotes Infection.Frontiers in cellular and infection microbiology · 2020Article
- Global Transcription Profiles ofFrontiers in veterinary science · 2020Article
- Counterattacking the tick bite: towards a rational design of anti-tick vaccines targeting pathogen transmission.Parasites & vectors · 2019Review
- Proteome Analysis Revealed Changes in Protein Expression Patterns Caused by Mutations inFrontiers in cellular and infection microbiology · 2019Article
- Article
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Abstract
Anaplasma phagocytophilum is the tick-transmitted obligate intracellular bacterium that causes human granulocytic anaplasmosis (HGA). A. phagocytophilum binding to sialyl Lewis x (sLe(x)) 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 of A. phagocytophilum outer membrane protein A (OmpA) APH_0338 in infection of mammalian host cells. OmpA is transcriptionally induced during transmission feeding of A. 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 of A. phagocytophilum organisms 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. Glutathione S-transferase (GST)-tagged versions of OmpA and OmpA amino acids 19 to 74 (OmpA(19-74)) but not OmpA(75-205) bind to, and competitively inhibit A. phagocytophilum infection 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 first A. phagocytophilum adhesin-receptor pair and delineates the region of OmpA that is critical for infection.
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