title: Structure-based vaccines provide protection in a mouse model of ehrlichiosis.
abstract: BACKGROUND
  Recent advances in bioinformatics have made it possible to predict the B cell and T cell epitopes of antigenic proteins. This has led to design of peptide based vaccines that are more specific, safe, and easy to produce. The obligately intracellular gram negative bacteria Ehrlichia cause ehrlichioses in humans and animals. As yet there are no vaccines to protect against Ehrlichia infection.
  
  
  RESULTS
  We applied the principle of structural vaccinology to design peptides to the epitopes of Ehrlichia muris outer membrane P28-19 (OMP-1/P28) and Ehrlichia Heat shock protein 60 (Hsp60/GroEL) antigenic proteins. Both P28-19 and Ehrlichia Hsp60 peptides reacted with polyclonal antibodies against E. canis and E. chaffeensis and could be used as a diagnostic tool for ehrlichiosis. In addition, we demonstrated that mice vaccinated with Ehrlichia P28-19 and Hsp60 peptides and later challenged with E. muris were protected against the pathogen.
  
  
  CONCLUSIONS
  Our results demonstrate the power of structural vaccines and could be a new strategy in the development of vaccines to provide protection against pathogenic microorganisms.
authors: Department of Pathology, University of Texas Medical Branch, Galveston, Texas, United States of America. suntom2@gmail.com
authors: Sunil
authors: S
authors: Thomas
authors: Nagaraja R
authors: NR
authors: Thirumalapura
authors: Patricia A
authors: PA
authors: Crocquet-Valdes
authors: Bruce A
authors: BA
authors: Luxon
authors: David H
authors: DH
authors: Walker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000907:Antibodies, Bacterial / Q000097:blood / Q000276:immunology; D000942:Antigens, Bacterial / Q000235:genetics / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D001428:Bacterial Vaccines / Q000737:chemistry* / Q000627:therapeutic use*; D015496:CD4-Positive T-Lymphocytes / Q000276:immunology; D018834:Chaperonin 60 / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D004536:Ehrlichia / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D016873:Ehrlichiosis / Q000276:immunology / Q000382:microbiology / Q000517:prevention & control*; D005260:Female; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology / Q000378:metabolism; D011487:Protein Conformation; D018417:Th1 Cells / Q000276:immunology
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D018834:Chaperonin 60; D010446:Peptide Fragments; C449088:p28 protein, Ehrlichia ewingii