Comparative assessment of a DNA and protein Leishmania donovani gamma glutamyl cysteine synthetase vaccine to cross-protect against murine cutaneous leishmaniasis caused by L. major or L. mexicana infection (2011)
Journal Article
Campbell, S., Campbell, S. A., Alawa, J., Doro, B., Henriquez, F., Roberts, C., Nok, A., Alawa, C., Alsaadi, M., Mullen, A., & Carter, K. (2012). Comparative assessment of a DNA and protein Leishmania donovani gamma glutamyl cysteine synthetase vaccine to cross-protect against murine cutaneous leishmaniasis caused by L. major or L. mexicana infection. Vaccine, 30(7), 1357-1363. https://doi.org/10.1016/j.vaccine.2011.12.067

Leishmaniasis is a major health problem and it is estimated that 12 million people are currently infected. A vaccine which could cross-protect people against different Leishmania spp. would facilitate control of this disease as more than one species... Read More about Comparative assessment of a DNA and protein Leishmania donovani gamma glutamyl cysteine synthetase vaccine to cross-protect against murine cutaneous leishmaniasis caused by L. major or L. mexicana infection.

Vaccination with Recombinant Leishmania donovani Gamma-Glutamylcysteine Synthetase Fusion Protein Protects Against L. donovani Infection (2010)
Journal Article
Campbell, S. A., Henriquez, F. L., Campbell, S. A., Roberts, C. W., Mullen, A. B., Burchmore, R., & Carter, K. C. (2010). Vaccination with Recombinant Leishmania donovani Gamma-Glutamylcysteine Synthetase Fusion Protein Protects Against L. donovani Infection. Journal of Parasitology, 96(5), 929-936. https://doi.org/10.1645/ge-2360.1

Visceral leishmaniasis presents a serious health threat in many parts of the world. There is, therefore, an urgent need for an approved vaccine for clinical use to protect against infection. In this study, the ability of recombinant Leishmania donova... Read More about Vaccination with Recombinant Leishmania donovani Gamma-Glutamylcysteine Synthetase Fusion Protein Protects Against L. donovani Infection.

Type I and type II fatty acid biosynthesis in Eimeria tenella: enoyl reductase activity and structure (2007)
Journal Article
CAMPBELL, S., LU, J., MUENCH, S., ALLARY, M., Campbell, S. A., ROBERTS, C., MUI, E., McLEOD, R., RICE, D., & PRIGGE, S. (2007). Type I and type II fatty acid biosynthesis in Eimeria tenella: enoyl reductase activity and structure. Parasitology, 134(14), 1949-1962. https://doi.org/10.1017/s0031182007003319

Apicomplexan parasites of the genus Eimeria are the major causative agent of avian coccidiosis, leading to high economic losses in the poultry industry. Recent results show that Eimeria tenella harbours an apicoplast organelle, and that a key biosynt... Read More about Type I and type II fatty acid biosynthesis in Eimeria tenella: enoyl reductase activity and structure.

DNA vaccination against the parasite enzyme gamma-glutamylcysteine synthetase confers protection against Leishmania donovani infection (2007)
Journal Article
Campbell, S., Carter, K., Henriquez, F., Campbell, S. A., Roberts, C., Nok, A., Mullen, A., & McFarlane, E. (2007). DNA vaccination against the parasite enzyme gamma-glutamylcysteine synthetase confers protection against Leishmania donovani infection. Vaccine, 25(22), 4502-4509. https://doi.org/10.1016/j.vaccine.2007.03.014

Enzymes of type II fatty acid synthesis and apicoplast differentiation and division in Eimeria tenella (2006)
Journal Article
Ferguson, D., Campbell, S. A., Henriquez, F., Phan, L., Mui, E., Richards, T., Muench, S., Allary, M., Lu, J., Prigge, S., Tomley, F., Shirley, M., Rice, D., McLeod, R., & Roberts, C. (2007). Enzymes of type II fatty acid synthesis and apicoplast differentiation and division in Eimeria tenella. International Journal for Parasitology, 37(1), 33-51. https://doi.org/10.1016/j.ijpara.2006.10.003

Apicomplexan parasites, Eimeria tenella, Plasmodium spp. and Toxoplasma gondii, possess a homologous plastid-like organelle termed the apicoplast, derived from the endosymbiotic enslavement of a photosynthetic alga. However, currently no eimerian nuc... Read More about Enzymes of type II fatty acid synthesis and apicoplast differentiation and division in Eimeria tenella.

Evolutionary Origins of the Eukaryotic Shikimate Pathway: Gene Fusions, Horizontal Gene Transfer, and Endosymbiotic Replacements (2006)
Journal Article
Richards, T. A., Dacks, J. B., Campbell, S. A., Blanchard, J. L., Foster, P. G., McLeod, R., Roberts, C. W., Richards, T. A., Dacks, J. B., Campbell, S. A., Blanchard, J. L., Foster, P. G., McLeod, R., & Roberts, C. W. (2006). Evolutionary Origins of the Eukaryotic Shikimate Pathway: Gene Fusions, Horizontal Gene Transfer, and Endosymbiotic Replacements. Eukaryotic Cell, 5(9), 1517-1531. https://doi.org/10.1128/ec.00106-06

Currently the shikimate pathway is reported as a metabolic feature of prokaryotes, ascomycete fungi, apicomplexans, and plants. The plant shikimate pathway enzymes have similarities to prokaryote homologues and are largely active in chloroplasts, sug... Read More about Evolutionary Origins of the Eukaryotic Shikimate Pathway: Gene Fusions, Horizontal Gene Transfer, and Endosymbiotic Replacements.

A complete shikimate pathway in Toxoplasma gondii: an ancient eukaryotic innovation (2003)
Journal Article
Campbell, S., Campbell, S. A., Richards, T., Mui, E., Samuel, B., Coggins, J., McLeod, R., & Roberts, C. (2004). A complete shikimate pathway in Toxoplasma gondii: an ancient eukaryotic innovation. International Journal for Parasitology, 34(1), 5-13. https://doi.org/10.1016/j.ijpara.2003.10.006

The shikimate pathway is essential for survival of the apicomplexan parasites Plasmodium falciparum, Toxoplasma gondii and Cryptosporidium parvum. As it is absent in mammals it is a promising therapeutic target. Herein, we describe the genes encoding... Read More about A complete shikimate pathway in Toxoplasma gondii: an ancient eukaryotic innovation.

Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli (2000)
Journal Article
Maclean, J., Campbell, S. A., Pollock, K., Chackrewarthy, S., Coggins, J. R., & Lapthorn, A. J. (2000). Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli. Acta crystallographica. Section D, Biological crystallography, 56(4), 512-515. https://doi.org/10.1107/s0907444900002377

Shikimate dehydrogenase from Escherichia coli has been crystallized by the vapour-diffusion method using ammonium sulfate as a precipitant. Mass spectrometry confirmed the purity of the enzyme and dynamic light scattering was used to find the appropr... Read More about Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli.