Enhancement of immune response towards non-lipidized Borrelia burgdorferi recombinant OspC antigen by binding onto the surface of metallochelating nanoliposomes with entrapped lipophilic derivatives of norAbuMDP
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22387453
DOI
10.1016/j.jconrel.2012.02.017
PII: S0168-3659(12)00141-1
Knihovny.cz E-resources
- MeSH
- Acetylmuramyl-Alanyl-Isoglutamine chemistry toxicity MeSH
- Antigens, Bacterial immunology MeSH
- Borrelia burgdorferi immunology MeSH
- Chelating Agents chemistry toxicity MeSH
- Calorimetry, Differential Scanning MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Liposomes MeSH
- Mice, Inbred BALB C MeSH
- Mice MeSH
- Nanoparticles chemistry toxicity MeSH
- Drug Carriers chemistry toxicity MeSH
- Bacterial Outer Membrane Proteins immunology MeSH
- Antibodies, Bacterial blood MeSH
- Scattering, Radiation MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Light MeSH
- Microscopy, Electron, Transmission MeSH
- Lyme Disease Vaccines administration & dosage immunology MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Acetylmuramyl-Alanyl-Isoglutamine MeSH
- Antigens, Bacterial MeSH
- Chelating Agents MeSH
- Liposomes MeSH
- Drug Carriers MeSH
- OspC protein MeSH Browser
- Bacterial Outer Membrane Proteins MeSH
- Antibodies, Bacterial MeSH
- Lyme Disease Vaccines MeSH
Lyme disease caused by spirochete Borrelia burgdorferi sensu lato, is a tick-born illness. If the infection is not eliminated by the host immune system and/or antibiotics, it may further disseminate and cause severe chronic complications. The immune response to Borrelia is mediated by phagocytic cells and by Borrelia-specific complement-activating antibodies associated with Th1 cell activation. A new experimental vaccine was constructed using non-lipidized form of recombinant B. burgdorferi s.s. OspC protein was anchored by metallochelating bond onto the surface of nanoliposomes containing novel nonpyrogenic lipophilized norAbuMDP analogues denoted MT05 and MT06. After i.d. immunization, the experimental vaccines surpassed Alum with respect to OspC-specific titers of IgG2a, IgG2b isotypes when MT06 was used and IgG3, IgM isotypes when MT05 was used. Both adjuvants exerted a high adjuvant effect comparable or better than MDP and proved themselves as nonpyrogenic.
References provided by Crossref.org
Targeting Human Thrombus by Liposomes Modified with Anti-Fibrin Protein Binders