Professor Richard J. Pleass

Chair in Parasite Immunology

Areas of interest

Structure and function of antibodies and their Fc-receptors in immunity to parasites. 


Richard Pleass graduated in Zoology from King’s College London in 1990.  After an MSc in Medical Parasitology from the London School of Hygiene and Tropical Medicine he obtained his PhD in Parasite Immunology from Imperial College London in 1994. He moved to the University of Dundee to work on IgA, and as a Wellcome Trust Advanced Training Fellow developed recombinant human antibodies targeting the malaria parasite. He became a lecturer at the Institute of Genetics, University of Nottingham in 2003. With 5 yr MRC and EU career development awards he became Associate Professor in 2007 before joining the Liverpool School of Tropical Medicine in 2010. In 2013 his work was recognized with the Universal Biotech Prize in Paris



Immunoglobulins, also called antibodies, are an important arm of the immune response helping to both eliminate parasites and stop them causing disease. They are flexible adaptor molecules found in blood and are produced by B-cells. While one part of the antibody molecule binds to the pathogen, the other part (the Fc portion) interacts with cells of the immune system via Fc-receptors (FcR). FcR have been described for all five classes of antibody (IgG, IgA, IgM, IgE, and IgD). The structural diversity of the Fc receptor family and their broad distribution on different cells of the immune system enables them to mediate a plethora of biological functions as diverse as antigen presentation, phagocytosis, cytotoxicity, induction of inflammatory cascades and modulation of immune responses. Parasites, in order to survive in the immune competent host, have devised ingenious methods to subvert this important aspect of the immune response. Using a number of approaches, including human FcR transgenic and knockout models, we are dissecting the roles of FcR receptors in immunity to parasites and utilizing this information to drive forward the development of novel self-adjuvantizing vaccines for the neglected tropical diseases.


Selected publications

  • Selected publications

    Czajkowsky DM, Salanti A, Ditlev SB, Shao Z, Ghumra A, Rowe JA, Pleass RJ. (2010). IgM, FcmRs, and malarial immune evasion. J Immunol. 184: 4597-603.

    Lazarou M, Guevara Patiño JM, Jennings RM, McIntosh RS, Shi J, Howell S, Cullen E, Jones T, Adame-Gallegos J, Chappel JA, McBride JS, Blackman MJ, Holder AA, Pleass RJ. (2009). Inhibition of erythrocyte invasion andPlasmodium falciparum Merozoite Surface Protein 1 processing requires intact IgG binding to the carboxy-terminal region of the protein: construction and properties of chimeric human IgG1 and IgG3 antibodies that retain function.Infect. Immun. 77: 5659-67.

    Ghumra A, Shi J, McIntosh RS, Rasmussen R, Braathen R, Johansen F-E, Sandlie I, Mongini P, Areschoug T, Lindahl G, Lewis MJ, Woof JM and Pleass RJ (2009). Structural requirements for the interaction of human IgM and IgA with the human Fca/m receptor (hFca/mR). Eur. J Immunol . 39: 1147-56.

    Ghumra A, Semblat J-P, McIntosh RS, Raza A, Rasmussen R, Johansen F-E, Sandlie I, Mongini P, Rowe JA andPleass RJ (2008). Indentification of residues in the Cm4 domain of polymeric IgM essential for interaction with P. falciparum erythrocyte membrane 1 (PfEMP1). J. Immunol. 181: 1988-2000.

    McIntosh RS, Shi J, Jennings RM, Chappel JC, de Koning-Ward TF, Smith T, Green J, van Egmond M, Leusen JH, Lazarou M, van de Winkel J, Jones TS, Crabb BS, Holder AA, Pleass RJ. (2007). Novel fully human anti-Plasmodium falciparum MSP119 antibodies highlight the importance of human FcgRI in mediating protection to malaria. PLoS Pathogens 18;3(5):e72.

    Aslam A, McIntosh RS, Quinn P, Shi J, Ghumra A, McKerrow JH, Bunting KA, Dunne DW, Doenhoff M, Morrison SL, Zhang Ke, Pleass RJ. (2007). Proteases from Schistosoma mansoni cercariae cleave IgE at solvent exposed interdomain regions. Mol. Immunol. 45: 567-574.

    Pleass, RJ and Holder, AA (2005). Antibody-based therapies for malaria. Nat. Rev. Microbiol. 3: 893-899.