2016
The Position of His-Tag in Recombinant OspC and Application of Various Adjuvants Affects the Intensity and Quality of Specific Antibody Response after Immunization of Experimental Mice
KRUPKA, Michal; Josef MASEK; Lucia BARKOCZIOVA; Pavlina Turanek KNOTIGOVA; Pavel KULICH et. al.Základní údaje
Originální název
The Position of His-Tag in Recombinant OspC and Application of Various Adjuvants Affects the Intensity and Quality of Specific Antibody Response after Immunization of Experimental Mice
Autoři
KRUPKA, Michal; Josef MASEK; Lucia BARKOCZIOVA; Pavlina Turanek KNOTIGOVA; Pavel KULICH; Jana PLOCKOVA; Robert LUKAC; Eliska BARTHELDYOVA; Stepan KOUDELKA; Radka CHALOUPKOVÁ; Marek SEBELA; Daniel ZYKA; Ladislav DROZ; Roman EFFENBERG; Miroslav LEDVINA; Andrew D. MILLER; Jaroslav TURANEK a Milan RASKA
Vydání
Plos one, San Francisco, Public Library of Science, 2016, 1932-6203
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 2.806
Kód RIV
RIV/00216224:14310/16:00089986
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000369554000110
EID Scopus
2-s2.0-84959386730
Klíčová slova anglicky
OUTER SURFACE PROTEIN; LYME-DISEASE VACCINE; BORRELIA-BURGDORFERI OSPA; LIPOPHILIC DERIVATIVES; MOLECULAR ANALYSIS; IMMUNE-RESPONSE; GENE-TRANSFER; EPITOPE; EXPRESSION; ANTIGEN
Změněno: 14. 4. 2017 15:10, Ing. Andrea Mikešková
Anotace
V originále
Lyme disease, Borrelia burgdorferi-caused infection, if not recognized and appropriately treated by antibiotics, may lead to chronic complications, thus stressing the need for protective vaccine development. The immune protection is mediated by phagocytic cells and by Borrelia-specific complement-activating antibodies, associated with the Th1 immune response. Surface antigen OspC is involved in Borrelia spreading through the host body. Previously we reported that recombinant histidine tagged (His-tag) OspC (rOspC) could be attached onto liposome surfaces by metallochelation. Here we report that levels of OspC-specific antibodies vary substantially depending upon whether rOspC possesses an N' or C' terminal His-tag. This is the case in mice immunized: (a) with rOspC proteoliposomes containing adjuvants MPLA or non-pyrogenic MDP analogue MT06; (b) with free rOspC and Montanide PET GEL A; (c) with free rOspC and alum; or (d) with adjuvant-free rOspC. Stronger responses are noted with all N'-terminal His-tag rOspC formulations. OspC-specific Th1-type antibodies predominate post-immunization with rOspC proteoliposomes formulated with MPLA or MT06 adjuvants. Further analyses confirmed that the structural features of soluble N' and C' terminal His-tag rOspC and respective rOspC proteoliposomes are similar including their thermal stabilities at physiological temperatures. On the other hand, a change in the position of the rOspC His-tag from N' to C' terminal appears to affect substantially the immunogenicity of rOspC arguably due to steric hindrance of OspC epitopes by the C' terminal His-tag itself and not due to differences in overall conformations induced by changes in the His-tag position in rOspC variants.
Návaznosti
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| LO1214, projekt VaV |
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