ArticleInfection and immunity2006
Two monoclonal antibodies with defined epitopes of P44 major surface proteins neutralize Anaplasma phagocytophilum by distinct mechanisms.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Generation of Population-Level Diversity inPathogens (Basel, Switzerland) · 2025Article
- Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023Review
- Beyond binding: antibody effector functions in infectious diseases.Nature reviews. Immunology · 2018Review
- Functions of Antibodies.Microbiology spectrum · 2014Article
- Breaking in and grabbing a meal: Anaplasma phagocytophilum cellular invasion, nutrient acquisition, and promising tools for their study.Microbes and infection · 2013Review
- An emerging tick-borne disease of humans is caused by a subset of strains with conserved genome structure.Pathogens (Basel, Switzerland) · 2013Article
- Ehrlichia chaffeensis uses its surface protein EtpE to bind GPI-anchored protein DNase X and trigger entry into mammalian cells.PLoS pathogens · 2013Article
- Anaplasma phagocytophilum--a widespread multi-host pathogen with highly adaptive strategies.Frontiers in cellular and infection microbiology · 2013Review
- Mechanisms of obligatory intracellular infection with Anaplasma phagocytophilum.Clinical microbiology reviews · 2011Review
- Proteomic analysis of Neorickettsia sennetsu surface-exposed proteins and porin activity of the major surface protein P51.Journal of bacteriology · 2010Article
- Cyclic di-GMP signaling regulates invasion by Ehrlichia chaffeensis of human monocytes.Journal of bacteriology · 2010Article
- Anaplasma phagocytophilum and Ehrlichia chaffeensis: subversive manipulators of host cells.Nature reviews. Microbiology · 2010Review
- Molecular events involved in cellular invasion by Ehrlichia chaffeensis and Anaplasma phagocytophilum.Veterinary parasitology · 2010Review
- Differential expression and glycosylation of anaplasma phagocytophilum major surface protein 2 paralogs during cultivation in sialyl Lewis x-deficient host cells.Infection and immunity · 2009Article
- The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection.Journal of bacteriology · 2009Article
- Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells.Infection and immunity · 2008Article
- Anaplasma phagocytophilum p44 mRNA expression is differentially regulated in mammalian and tick host cells: involvement of the DNA binding protein ApxR.Journal of bacteriology · 2007Article
- Identification of novel surface proteins of Anaplasma phagocytophilum by affinity purification and proteomics.Journal of bacteriology · 2007Article
- Surface-exposed proteins of Ehrlichia chaffeensis.Infection and immunity · 2007Article
- Porin activity of Anaplasma phagocytophilum outer membrane fraction and purified P44.Journal of bacteriology · 2007Article
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3 authors.
Funding
Abstract
Anaplasma phagocytophilum is an obligatory intracellular bacterium that causes human granulocytic anaplasmosis. The polymorphic 44-kDa major outer membrane proteins of A. phagocytophilum are dominant antigens recognized by patients and infected animals. However, the ability of anti-P44 antibody to neutralize the infection has been unclear due to a mixture of P44 proteins with diverse hypervariable region amino acid sequences expressed by a given bacterial population and lack of epitope-defined antibodies. Monoclonal antibodies (MAbs) 5C11 and 3E65 are directed to different domains of P44 proteins, the N-terminal conserved region and P44-18 central hypervariable region, respectively. Passive immunization with either MAb 5C11 or 3E65 partially protects mice from infection with A. phagocytophilum. In the present study, we demonstrated that the two monoclonal antibodies recognize bacterial surface-exposed epitopes of naturally folded P44 proteins and mapped these epitopes to specific peptide sequences. The two MAbs almost completely blocked the infection of the A. phagocytophilum population that predominantly expressed P44-18 in HL-60 cells by distinct mechanisms: MAb 5C11 blocked the binding, but MAb 3E65 did not block binding or internalization. Instead, MAb 3E65 inhibited internalized A. phagocytophilum to develop into microcolonies called morulae. Some plasma from experimentally infected horses and mice reacted with these two epitopes. Taken together, these data indicate the presence of at least two distinct bacterial surface-exposed neutralization epitopes in P44 proteins. The results indicate that antibodies directed to certain epitopes of P44 proteins have a critical role in inhibiting A. phagocytophilum infection of host cells.
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