ArticleInfection and immunity2007
Ehrlichia canis gp200 contains dominant species-specific antibody epitopes in terminal acidic domains.
Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
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- Antibody reactive immunomes ofFrontiers in cellular and infection microbiology · 2023Article
- Type 1 secretion system and effectors in Rickettsiales.Frontiers in cellular and infection microbiology · 2023Review
- Immunoreactive Protein Repertoires of Ehrlichia chaffeensis and E. canis Reveal the Dominance of Hypothetical Proteins and Conformation-Dependent Antibody Epitopes.Infection and immunity · 2021Article
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- Recombinant Ehrlichia P29 protein induces a protective immune response in a mouse model of ehrlichiosis.Vaccine · 2013Article
- Ehrlichia moonlighting effectors and interkingdom interactions with the mononuclear phagocyte.Microbes and infection · 2013Review
- Tyrosine-phosphorylated Ehrlichia chaffeensis and Ehrlichia canis tandem repeat orthologs contain a major continuous cross-reactive antibody epitope in lysine-rich repeats.Infection and immunity · 2011Article
- Molecular and cellular pathobiology of Ehrlichia infection: targets for new therapeutics and immunomodulation strategies.Expert reviews in molecular medicine · 2011Review
- Ehrlichia chaffeensis tandem repeat proteins and Ank200 are type 1 secretion system substrates related to the repeats-in-toxin exoprotein family.Frontiers in cellular and infection microbiology · 2011Article
- Sequence and phylogenetic analysis of the gp200 protein of Ehrlichia canis from dogs in Taiwan.Journal of veterinary science · 2010Article
- Progress and obstacles in vaccine development for the ehrlichioses.Expert review of vaccines · 2010Review
- New insights into molecular Ehrlichia chaffeensis-host interactions.Microbes and infection · 2010Review
- Molecular characterization of antibody epitopes of Ehrlichia chaffeensis ankyrin protein 200 and tandem repeat protein 47 and evaluation of synthetic immunodeterminants for serodiagnosis of human monocytotropic ehrlichiosis.Clinical and vaccine immunology : CVI · 2010Article
- Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements.Infection and immunity · 2009Article
- Major species-specific antibody epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 orthologs in surface-exposed tandem repeat regions.Clinical and vaccine immunology : CVI · 2009Article
- An Ehrlichia chaffeensis tandem repeat protein interacts with multiple host targets involved in cell signaling, transcriptional regulation, and vesicle trafficking.Infection and immunity · 2009Article
- Defining the immune response to Ehrlichia species using murine models.Veterinary parasitology · 2008Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Species-specific antibody epitopes within several major immunoreactive protein orthologs of Ehrlichia species have recently been identified and molecularly characterized. In this study, dominant B-cell epitopes within the acidic (pI 5.35) ankyrin repeat-containing 200-kDa major immunoreactive protein (gp200) of Ehrlichia canis were defined. The E. canis gp200 gene (4,263 bp; 1,421 amino acids) was cloned and expressed as four (N-terminal, 1,107 bp; N-internal, 910 bp; C-internal, 1,000 bp; and C-terminal, 1,280 bp) overlapping recombinant proteins. The N-terminal, C-internal, and C-terminal polypeptides (369, 332, and 426 amino acids, respectively) were strongly recognized by antibody, and the major epitope(s) in these polypeptides was mapped to four polypeptide regions (40 to 70 amino acids). Smaller overlapping recombinant polypeptides (14 to 15 amino acids) spanning these regions identified five strongly immunoreactive species-specific epitopes that exhibited conformational dependence. The majority of the epitopes (four) were located in two strongly acidic (pI 4 to 4.9) domains in the distal N- and C-terminal regions of the protein flanking the centralized ankyrin domain-containing region. The amino acid content of the epitope-containing domains included a high proportion of strongly acidic amino acids (glutamate and aspartate), and these domains appear to have important biophysical properties that influence the antibody response to gp200.
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