期刊
VACCINE
卷 30, 期 5, 页码 948-958出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.vaccine.2011.11.059
关键词
Malaria; CTB; Delivery system; Subunit vaccine
资金
- Grants-in-Aid for Scientific Research [21390132, 23590490] Funding Source: KAKEN
Methylotrophic yeast (Pichia pastoris) secreted cholera toxin B subunit (CUB) predominantly as a biologically active pentamer (PpCTB) with identical ganglioside binding affinity profiles to that of choleragenoid. Unlike choleragenoid, however, the PpCTB did not induce a footpad edema response in mice. Of the two potential glycosylation sites (NIT4-6 and NICT90-92) for this protein, a N-linked oligosaccharide was identified at Asn4. The oligosaccharide, presumed to extend from the lateral circumference of the CUB pentamer ring structure, was exploited as a site-specific anchoring scaffold for the C-terminal 19-kDa merozoite surface protein-1 (MSP1-19) of the rodent malaria parasite, Plasmodium yoelii. Conjugation of MSP1-19 to PpCTB via its oligosaccharide moiety induced higher protective efficacy against lethal parasite infection than conjugation directly to the PpCTB protein body in both intranasal and subcutaneous immunization regimes. Such increased protection was potentially due to the higher antigen loading capacity of CUB achieved when the antigen was linked to the extended branches of the oligosaccharide. This might have allowed the antigen to reside in more spacious molecular environment with less steric hindrance between the constituent molecules of the fusion complex. (C) 2011 Elsevier Ltd. All rights reserved.
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