Abstract
Subunit antigens are attractive candidates for vaccine development, as they are safe, cost-effective, and rapidly produced. Nevertheless, subunit antigens often need to be adjuvanted and/or formulated to produce products with acceptable potency and efficacy. Here, we describe a simple method for improving the potency and efficacy of a recombinant subunit antigen by its immobilization on nickel-chelating nanolipoprotein particles (NiNLPs). NiNLPs are membrane mimetic nanoparticles that provide a delivery and presentation platform amenable to binding any recombinant subunit immunogens featuring a polyhistidine tag. A His-tagged, soluble truncated form of the West Nile virus (WNV) envelope protein (trE-His) was immobilized on NiNLPs. Single inoculations of the NiNLP-trE-His produced superior anti-WNV immune responses and provided significantly improved protection against a live WNV challenge compared to mice inoculated with trE-His alone. These results have broad implications in vaccine development and optimization, as NiNLP technology is well-suited to many types of vaccines, providing a universal platform for enhancing the potency and efficacy of recombinant subunit immunogens.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1018-1022 |
| Number of pages | 5 |
| Journal | Bioconjugate Chemistry |
| Volume | 21 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 16 2010 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Organic Chemistry
- Pharmaceutical Science
- Biomedical Engineering
- Pharmacology
Cite this
Conjugation to nickel-chelating nanolipoprotein particles increases the potency and efficacy of subunit vaccines to prevent west nile encephalitis. / Fischer, Nicholas O; Infante, Ernesto; Ishikawa, Tomohiro; Blanchette, Craig D.; Bourne, Nigel; Hoeprich, Paul D.; Mason, Peter W.
In: Bioconjugate Chemistry, Vol. 21, No. 6, 16.06.2010, p. 1018-1022.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Conjugation to nickel-chelating nanolipoprotein particles increases the potency and efficacy of subunit vaccines to prevent west nile encephalitis
AU - Fischer, Nicholas O
AU - Infante, Ernesto
AU - Ishikawa, Tomohiro
AU - Blanchette, Craig D.
AU - Bourne, Nigel
AU - Hoeprich, Paul D.
AU - Mason, Peter W.
PY - 2010/6/16
Y1 - 2010/6/16
N2 - Subunit antigens are attractive candidates for vaccine development, as they are safe, cost-effective, and rapidly produced. Nevertheless, subunit antigens often need to be adjuvanted and/or formulated to produce products with acceptable potency and efficacy. Here, we describe a simple method for improving the potency and efficacy of a recombinant subunit antigen by its immobilization on nickel-chelating nanolipoprotein particles (NiNLPs). NiNLPs are membrane mimetic nanoparticles that provide a delivery and presentation platform amenable to binding any recombinant subunit immunogens featuring a polyhistidine tag. A His-tagged, soluble truncated form of the West Nile virus (WNV) envelope protein (trE-His) was immobilized on NiNLPs. Single inoculations of the NiNLP-trE-His produced superior anti-WNV immune responses and provided significantly improved protection against a live WNV challenge compared to mice inoculated with trE-His alone. These results have broad implications in vaccine development and optimization, as NiNLP technology is well-suited to many types of vaccines, providing a universal platform for enhancing the potency and efficacy of recombinant subunit immunogens.
AB - Subunit antigens are attractive candidates for vaccine development, as they are safe, cost-effective, and rapidly produced. Nevertheless, subunit antigens often need to be adjuvanted and/or formulated to produce products with acceptable potency and efficacy. Here, we describe a simple method for improving the potency and efficacy of a recombinant subunit antigen by its immobilization on nickel-chelating nanolipoprotein particles (NiNLPs). NiNLPs are membrane mimetic nanoparticles that provide a delivery and presentation platform amenable to binding any recombinant subunit immunogens featuring a polyhistidine tag. A His-tagged, soluble truncated form of the West Nile virus (WNV) envelope protein (trE-His) was immobilized on NiNLPs. Single inoculations of the NiNLP-trE-His produced superior anti-WNV immune responses and provided significantly improved protection against a live WNV challenge compared to mice inoculated with trE-His alone. These results have broad implications in vaccine development and optimization, as NiNLP technology is well-suited to many types of vaccines, providing a universal platform for enhancing the potency and efficacy of recombinant subunit immunogens.
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U2 - 10.1021/bc100083d
DO - 10.1021/bc100083d
M3 - Article
C2 - 20509624
AN - SCOPUS:77953630897
VL - 21
SP - 1018
EP - 1022
JO - Bioconjugate Chemistry
JF - Bioconjugate Chemistry
SN - 1043-1802
IS - 6
ER -