DMCA
Immunogenicity of Self-Associated Aggregates and Chemically Cross-Linked Conjugates of the 42 kDa
BibTeX
@MISC{Merozoite_immunogenicityof,
author = {Plasmodium Merozoite and Surface Protein and Feng Qian and Karine Reiter and Yanling Zhang and Richard L. Shimp and Vu Nguyen and Joan A. Aebig and Kelly M. Rausch and Daming Zhu and Lynn Lambert and Gregory E. D. Mullen and Laura B. Martin and Carole A. Long and Louis H. Miller and David L. Narum},
title = {Immunogenicity of Self-Associated Aggregates and Chemically Cross-Linked Conjugates of the 42 kDa},
year = {}
}
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Abstract
Self-associated protein aggregates or cross-linked protein conjugates are, in general, more immunogenic than oligomeric or monomeric forms. In particular, the immunogenicity in mice of a recombinant malaria transmission blocking vaccine candidate, the ookinete specific Plasmodium falciparum 25 kDa protein (Pfs25), was increased more than 1000-fold when evaluated as a chemical cross-linked protein-protein conjugate as compared to a formulated monomer. Whether alternative approaches using protein complexes improve the immunogenicity of other recombinant malaria vaccine candidates is worth assessing. In this work, the immunogenicity of the recombinant 42 kDa processed form of the P. falciparum merozoite surface protein 1 (MSP142) was evaluated as a self-associated, non-covalent aggregate and as a chemical cross-linked protein-protein conjugate to ExoProtein A, which is a recombinant detoxified form of Pseudomonas aeruginosa exotoxin A. MSP142 conjugates were prepared and characterized biochemically and biophysically to determine their molar mass in solution and stoichiometry, when relevant. The immunogenicity of the MSP142 self-associated aggregates, cross-linked chemical conjugates and monomers were compared in BALB/c mice after adsorption to aluminum hydroxide adjuvant, and in one instance in association with the TLR9 agonist CPG7909 with an aluminum hydroxide formulation.
