Ivan Campeotto

Contact

• workRoom C03 Bioenergy and Brewery
  Sutton Bonington Campus
  Sutton Bonington
  Leicestershire
  LE12 5RD
  UK
• Ivan.Campeotto@nottingham.ac.uk

Biography

Career summary:

• Senior Lecturer in Biochemistry at Nottingham Trent University
• Wellcome Trust ISSF - Early Career Research Fellow at the Leicester Institute of Structural and Chemical Biology.
• BTP Research Fellow at Pembroke College, University of Oxford.
• Research Associate at the University of Oxford.
• Research Associate at Imperial College London.
• Research Associate at King's College London.
• PhD in protein crystallography at the Astbury Centre for Structural Molecular Biology, University of Leeds.
• Degree in Industrial Biotechnology at the University of Padua (Italy).

Other roles:

Member of the CCP4 WG1 and WG2, Honorary Fellow at LISCB (University of Leicester), Visiting Lecturer (NTU), Editor Board Member of Scientific Reports and Frontiers in Microbiology

Expertise Summary

My group currently focuses on structure-based drug design and structure-guided vaccine development in the fields of Neglected Tropical Diseases (NTDs) and of emerging viruses, with main focus on Chagas disease.

To achieve this, we use protein crystallography as the main research tool in combination with cryo-EM, 2D NMR, HDX-MS and complementary biophysical techniques (ITC, BLI, SPR, DSF, DSC, CD etc.). My group has access to the Diamond Light Source (DLS) MX beamlines, Research Complex at Harwell and other synchrotrons in France (Soleil) and Germany (Petra and DESY). I am also involved in methods development for in situ serial crystallography, to trap intermediates of enzymes from human pathogens in collaboration with the VMXi team at DLS.

We use several expression systems for recombinant protein production: Escherichia coli, Vibrio natrigens, HEK293F cells, sf9 cells, Leishmania tarantulae and more recently Tobacco plants.

Teaching Summary

I am module leader for the UG course on "Fundamental in Immunology" (BIOS2010) which will start in October 2023 and will have particular focus on host-pathogen interactions and vaccines.

I am also module leader for the PG module "Research skills in Microbia Biotehcnology" (BIOS4125).

Research Summary

My main research stream lies in the design and production of immunogens from human and animal pathogens, for the generation of monoclonal antibodies, which we test for diagnostic and therapeutic… read more

Recent Publications

• 2024. Preclinical Development of a Stabilized RH5 Virus-Like Particle Vaccine that Induces Improved Anti-Malarial Antibodies bioRXiv.
• 2024. Rational structure-guided design of a blood stage malaria vaccine immunogen presenting a single epitope from PfRH5: bioRxiv bioRXiv.
• 2024. Open and closed conformations of a sub-80 kDa Chagas vaccine candidate defined by a cryo-EM led integrative approach bioRxiv.
• MIKOLAJEK, H., SANCHEZ-WEATHERBY, J., SANDY, J., GILDEA, R. J., CAMPEOTTO, I., CHERUVARA, H., CLARKE, J. D., FOSTER, T., FUJII, S., PAULSEN, I. T., SHAH, B. S. and HOUGH, M. A., 2023. Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi: IUCrJ IUCrJ. 10(Pt 4), 420-429

• View all publications

Current Research

My main research stream lies in the design and production of immunogens from human and animal pathogens, for the generation of monoclonal antibodies, which we test for diagnostic and therapeutic applications. After this initial step, we proceed with the determination of antigen-antibody complexes, which are used to guide the design and development of vaccine prototypes via epitopes conjugation to engineered Virus-Like-Particles (VLPs), upon "a la carte" computational epitope crafting.

I was successful in this approach and designed, produced and characterized a heat stable variant of the leading protein candidate for a blood-stage malaria vaccine, called RH5, which lead to a patent with myself as co-inventor (PCT/GB2017/052608), when I was at the University of Oxford, which has been licensed to the Serum Institute of India in 2022, for human trials in children in Gambia and Burkina Faso (trial NCT05357560).

Current Lab members: Sagar Batra (PhD student), Oliver Boakye (PhD student), Sam Skinner (PhD student), Christopher Waugh (Senior Research Technician)

Alumni :

• Master student Iqra Kaleem (Oxford Expression Technologies)
• Master student Sadia Purba (Freelance Medical writer)
• Master student Ahmad Jazuli
• Master student Hirak Naitik Tailor (PhD student at Center of Molecular Medicine Cologne, Germany)
• Master student Raizel Fernandes (NHS)
• Master student Agata Kowalska (R&D at Reckitt)
• Master student Maria Morra (Wellcome Sanger Institute, Cambridge)
• BSc student Camilla Huemert (PhD student, Imperial College London)

• 2024. Preclinical Development of a Stabilized RH5 Virus-Like Particle Vaccine that Induces Improved Anti-Malarial Antibodies bioRXiv.
• 2024. Rational structure-guided design of a blood stage malaria vaccine immunogen presenting a single epitope from PfRH5: bioRxiv bioRXiv.
• 2024. Open and closed conformations of a sub-80 kDa Chagas vaccine candidate defined by a cryo-EM led integrative approach bioRxiv.
• MIKOLAJEK, H., SANCHEZ-WEATHERBY, J., SANDY, J., GILDEA, R. J., CAMPEOTTO, I., CHERUVARA, H., CLARKE, J. D., FOSTER, T., FUJII, S., PAULSEN, I. T., SHAH, B. S. and HOUGH, M. A., 2023. Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi: IUCrJ IUCrJ. 10(Pt 4), 420-429
• CAMPEOTTO, I., GALAWAY, F., MEHMOOD, S., BARFOD, L. K., QUINKERT, D., KOTRAIAH, V., PHARES, T. W., WRIGHT, K. E., SNIJDERS, A. P., DRAPER, S. J., HIGGINS, M. K. and WRIGHT, G. J., 2020. The Structure of the Cysteine-Rich Domain of Plasmodium falciparum P113 Identifies the Location of the RH5 Binding Site: mBio mBio. 11(5),
• WARSZAWSKI, S., DEKEL, E., CAMPEOTTO, I., MARSHALL, J. M., WRIGHT, K. E., LYTH, O., KNOP, O., REGEV-RUDZKI, N., HIGGINS, M. K., DRAPER, S. J., BAUM, J. and FLEISHMAN, S. J., 2020. Design of a basigin-mimicking inhibitor targeting the malaria invasion protein RH5: Proteins Proteins. 88(1), 187-195
• CAMPEOTTO, I., LEBEDEV, A., SCHREURS, A. M. M., KROON-BATENBURG, L. M. J., LOWE, E., PHILLIPS, S. E. V., MURSHUDOV, G. N. and PEARSON, A. R., 2018. Pathological macromolecular crystallographic data affected by twinning, partial-disorder and exhibiting multiple lattices for testing of data processing and refinement tools: Sci Rep Sci Rep. 8(1), 14876
• CAMPEOTTO, I., GOLDENZWEIG, A., DAVEY, J., BARFOD, L., MARSHALL, J. M., SILK, S. E., WRIGHT, K. E., DRAPER, S. J., HIGGINS, M. K. and FLEISHMAN, S. J., 2017. One-step design of a stable variant of the malaria invasion protein RH5 for use as a vaccine immunogen: Proc Natl Acad Sci U S A Proc Natl Acad Sci U S A. 114(5), 998-1002
• SCHUSTER, C. F., BELLOWS, L. E., TOSI, T., CAMPEOTTO, I., CORRIGAN, R. M., FREEMONT, P. and GRUNDLING, A., 2016. The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus: Sci Signal Sci Signal. 9(441), ra81
• CAMPEOTTO, I., ZHANG, Y., MLADENOV, M. G., FREEMONT, P. S. and GRUNDLING, A., 2015. Complex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family: J Biol Chem J Biol Chem. 290(5), 2888-901
• CAMPEOTTO, I., PERCY, M. G., MACDONALD, J. T., FORSTER, A., FREEMONT, P. S. and GRUNDLING, A., 2014. Structural and mechanistic insight into the Listeria monocytogenes two-enzyme lipoteichoic acid synthesis system: J Biol Chem J Biol Chem. 289(41), 28054-69
• DANIELS, A. D., CAMPEOTTO, I., VAN DER KAMP, M. W., BOLT, A. H., TRINH, C. H., PHILLIPS, S. E., PEARSON, A. R., NELSON, A., MULHOLLAND, A. J. and BERRY, A., 2014. Reaction mechanism of N-acetylneuraminic acid lyase revealed by a combination of crystallography, QM/MM simulation, and mutagenesis: ACS Chem Biol ACS Chem Biol. 9(4), 1025-32
• THWAITES, T., NOGUEIRA, A. T., CAMPEOTTO, I., SILVA, A. P., GRIESHABER, S. S. and CARABEO, R. A., 2014. The Chlamydia effector TarP mimics the mammalian leucine-aspartic acid motif of paxillin to subvert the focal adhesion kinase during invasion: J Biol Chem J Biol Chem. 289(44), 30426-30442
• CORRIGAN, R. M., CAMPEOTTO, I., JEGANATHAN, T., ROELOFS, K. G., LEE, V. T. and GRUNDLING, A., 2013. Systematic identification of conserved bacterial c-di-AMP receptor proteins: Proc Natl Acad Sci U S A Proc Natl Acad Sci U S A. 110(22), 9084-9
• CAMPEOTTO, I. and ACEVEDO-ROCHA, C. G., 2013. Hijacking nature--new approaches to unravel enzyme mechanisms and engineer improved biocatalysts: EMBO Rep EMBO Rep. 14(4), 299-301
• CAMPEOTTO, I., BOLT, A. H., HARMAN, T. A., DENNIS, C., TRINH, C. H., PHILLIPS, S. E., NELSON, A., PEARSON, A. R. and BERRY, A., 2010. Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution: J Mol Biol J Mol Biol. 404(1), 56-69
• CAMPEOTTO, I., CARR, S. B., TRINH, C. H., NELSON, A. S., BERRY, A., PHILLIPS, S. E. and PEARSON, A. R., 2009. Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution: Acta Crystallogr Sect F Struct Biol Cryst Commun Acta Crystallogr Sect F Struct Biol Cryst Commun. 65(Pt 11), 1088-90
• Rational structure-guided design of a blood stage malaria vaccine immunogen presenting a single epitope from PfRH5 bioRXiv.
• Rational structure-guided design of a blood stage malaria vaccine immunogen presenting a single epitope from PfRH5 bioRXiv.