John McCafferty

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John McCafferty is a British scientist, one of the founders of Cambridge Antibody Technology, well known as one of the inventors of scFv antibody fragment phage display,[1] a technology that revolutionised the monoclonal antibody drug discovery. Later improvements of antibody phage display technology enables the display of millions of different antibody fragments on the surface of filamentous phage (better known as antibody phage library) and subsequent selection of highly specific recombinant antibodies to any given target. This technology is widely exploited in pharmaceutical industry for the discovery and development of therapeutic monoclonal antibodies to treat mainly cancer, inflammatory and infectious diseases. One of the most successful was HUMIRA (adalimumab), discovered by Cambridge Antibody Technology as D2E7 and developed and marketed by Abbott Laboratories. HUMIRA, an antibody to TNF alpha, was the world's first phage display derived fully human antibody,[2] which achieved annual sales exceeding $1bn [3] therefore achieving blockbuster status.

In 2002, after 12 years in Cambridge Antibody Technology(now MedImmune, a fully owned subsidiary of pharmaceutical giant Astrazenaca)McCafferty set up a group at the Sanger Institute developing and utilising methods for protein generation and recombinant antibody isolation in high throughput for proteomic applications.McCafferty has been involved in developing large human antibody repertoires both at CAT and at the Sanger Institute from which antibodies of high affinity and specificity to any antigen can be derived. He ran a laboratory at the Biochemistry Dept at University of Cambridge capitalising on the above technologies with a focus on the study of protein:protein interactions driving direct cell:cell communication[4][5][6][7][8][9] and has recently founded a new therapeutic antibody discovery biotechnology company, IONTAS Ltd.


  1. ^ McCafferty J; Griffiths A.D; Winter G; Chiswell D.J (1990). "Phage antibodies: filamentous phage displaying antibody variable domains". Nature. 348 (63017): 552–554. Bibcode:1990Natur.348..552M. PMID 2247164. doi:10.1038/348552a0. 
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  6. ^ Schofield DJ, Pope A, Clementel V, Buckell J, Chapple SDJ,, Clarke KF, Conquer JS, Crofts AM, Crowther SRE, Dyson MR, Flack G, Griffin GJ, Hooks Y, Howat WJ, Kolb-Kokocinski A,, Kunze S, Martin CD, Maslen GL,, Mitchell JM, OÕSullivan M, Perera RL, Roake W, Shadbolt SP, Vincent KJ, Warford A, Wilson WE, Xie J, Young JL, McCafferty J (2007) Application of phage display to high throughput antibody generation and characterisation. Genome Biology. 8 (11) R254
  7. ^ Dyson MR, Perera RL, Shadbolt SP, Biderman L, Bromek K, Murzina NV, McCafferty J (2008) Identification of soluble protein fragments by gene fragmentation and genetic selection. Nucl Acid Research 36 e51
  8. ^ Teng MS, Shadbolt P, Fraser AG, Jansen G, and McCafferty J. (2008) Control of feeding behaviour in C. elegans by human G protein coupled receptors permits screening for agonist-expressing bacteria. Proc Natl Acad Sci, 105 (39) 14826-14831
  9. ^ Chapple SDJ, Crofts AM, Shadbolt SP, McCafferty J, Dyson MR (2006) Multiplexed expression and screening for recombinant protein production in mammalian cells. BMC Biotechnology 6:49