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Status: Bibliographieeintrag

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Verfasst von:Skamel, Claudia [VerfasserIn]   i
 Ploss, Martin [VerfasserIn]   i
 Böttcher, Bettina [VerfasserIn]   i
 Stehle, Thomas [VerfasserIn]   i
 Wallich, Reinhard [VerfasserIn]   i
 Simon, Markus M. [VerfasserIn]   i
 Nassal, Michael [VerfasserIn]   i
Titel:Hepatitis B virus capsid-like particles can display the complete, dimeric outer surface protein C and stimulate production of protective antibody responses against Borrelia burgdorferi infection
Verf.angabe:Claudia Skamel, Martin Ploss, Bettina Böttcher, Thomas Stehle, Reinhard Wallich, Markus M. Simon, and Michael Nassal
E-Jahr:2006
Jahr:June 23, 2006
Umfang:8 S.
Teil:volume:281
 year:2006
 number:25
 pages:17474-17481
 extent:8
Fussnoten:Gesehen am 04.06.2021
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : ASBMB Publications, 1905
Jahr Quelle:2006
Band/Heft Quelle:281(2006), 25, Seite 17474-17481
ISSN Quelle:1083-351X
Abstract:Hepatitis B virus capsid-like particles (CLPs), icosahedral assemblies formed by 90 or 120 core protein dimers, hold promise as immune-enhancing vaccine carriers for heterologous antigens. Insertions into the immunodominant c/e1 B cell epitope, a surface-exposed loop, are especially immunogenic. However, display of whole proteins, desirable to induce multispecific and possibly neutralizing antibody responses, can be restrained by an unsuitable structure of the foreign protein and by its propensity to undergo homomeric interactions. Here we analyzed CLP formation by core fusions with two distinct variants of the dimeric outer surface lipoprotein C (OspC) of the Lyme disease agent Borrelia burgdorferi. Although the topology of the termini in the OspC dimer does not match that of the insertion sites in the carrier dimer, both fusions, coreOspCa and coreOspCb, efficiently formed stable CLPs. Electron cryomicroscopy clearly revealed the surface disposition of the OspC domains, possibly with OspC dimerization occurring across different core protein dimers. In mice, both CLP preparations induced high-titered antibody responses against the homologous OspC variant, but with substantial cross-reactivity against the other variant. Importantly, both conferred protection to mice challenged with B. burgdorferi. These data show the principal applicability of hepatitis B virus CLPs for the display of dimeric proteins, demonstrate the presence in OspC of hitherto uncharacterized epitopes, and suggest that OspC, despite its genetic variability, may be a valid vaccine candidate.
DOI:doi:10.1074/jbc.M513571200
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://dx.doi.org/10.1074/jbc.M513571200
 DOI: https://doi.org/10.1074/jbc.M513571200
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Animals
 Antigens, Bacterial
 Bacterial Outer Membrane Proteins
 Bacterial Vaccines
 Borrelia burgdorferi
 Dimerization
 Epitopes, B-Lymphocyte
 Genetic Variation
 Mice
 Mice, Inbred BALB C
 Mice, SCID
 Models, Molecular
 Nucleocapsid Proteins
 Plasmids
 Protein Conformation
 Protein Structure, Tertiary
K10plus-PPN:175980326X
Verknüpfungen:→ Zeitschrift

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