Picture of blood cells

Open Access research which pushes advances in bionanotechnology

Strathprints makes available scholarly Open Access content by researchers in the Strathclyde Institute of Pharmacy & Biomedical Sciences (SIPBS) , based within the Faculty of Science.

SIPBS is a major research centre in Scotland focusing on 'new medicines', 'better medicines' and 'better use of medicines'. This includes the exploration of nanoparticles and nanomedicines within the wider research agenda of bionanotechnology, in which the tools of nanotechnology are applied to solve biological problems. At SIPBS multidisciplinary approaches are also pursued to improve bioscience understanding of novel therapeutic targets with the aim of developing therapeutic interventions and the investigation, development and manufacture of drug substances and products.

Explore the Open Access research of SIPBS. Or explore all of Strathclyde's Open Access research...

Lack of immunological cross-reactivity between parasite-derived and recombinant forms of es-62, a secreted protein of acanthocheilonema viteae

Egan, C.A. and Houston, K.M. and Alcocer, M.J.C. and Solovyova, A. and Tate, R. and Lochnit, G. and McInnes, I.B. and Harnett, M.M. (2006) Lack of immunological cross-reactivity between parasite-derived and recombinant forms of es-62, a secreted protein of acanthocheilonema viteae. Parasitology, 132 (2). pp. 263-274. ISSN 0031-1820

Full text not available in this repository.Request a copy from the Strathclyde author

Abstract

The longevity of filarial nematodes is dependent on secreted immunomodulatory products. Previous investigation of one such product, ES-62, has suggested a critical role for post-translationally attached phosphorylcholine (PC) moieties. In order to further investigate this, ES-62 lacking PC was produced, using the Pichia pastoris recombinant gene expression system. Unlike parasite-derived ES-62, which is tetrameric the recombinant material was found to consist of a mixture of apparently stable tetramers, dimers and monomers. Nevertheless, the recombinant protein was considered to be an adequate PC-free ES-62 as it was recognized by existing antisera against the parasite-derived protein. However, subsequent to this, recognition of parasite-derived ES-62 by antibodies produced against the recombinant protein was found to be absent. In an attempt to explain this, recombinant ES-62 was subjected to structural analysis and was found to (i) contain 3 changes in amino acid composition; (ii) demonstrate significant alterations in glycosylation; (iii) show major differences in protein secondary structure. The effects of these alterations in relation to the observed change in immunogenicity were investigated and are discussed. The data presented clearly show that recognition by existing antibodies is insufficient proof that recombinant proteins can be used to mimic parasite-derived material in studies on nematode immunology and vaccination.