yALE JOu RNAL OF BIOLOGy AND MEDICINE 85 (2012), pp.285-292. Copyright © 2012. Sy MPOSIu M From Structure to Solutions: The Role of Basic Research in Developing Anthrax Countermeasures Microbiology Graduate Program Seminar: Anthrax Toxin Camille A. Hardiman PhD Candidate, Section for Microbial Pathogenesis, Yale School of Medicine, New Haven, Connecticut Dr. John Collier traced the discoveries that elucidated the structure and function of the an- thrax toxin in his talk “Anthrax Toxin,” which was part of the Microbiology Graduate Program Seminar Series at yale School of Medicine on February 23, 2012. Dr. Collier, Professor of Microbiology and Immunobiology at Harvard u niversity, began by noting the advantages to studying anthrax pathogenesis in a biosafety level-1 lab. This designation does not merely facilitate his research, but also reflects a larger trend of basic research being leveraged to develop translational applications. Basic research on toxin structure has led to the devel- opment of a vaccine by Dr. Collier’s group. Next-generation prophylactics also may stem from recent discoveries uncovering a role for cellular cofactors that mediate toxin function. Finally, basic research into the toxin substructure has facilitated efforts to change the re- ceptor tropism to target dysregulated cells for therapeutic purposes. The urgency around biodefense agents makes the choice of research priorities a salient issue. As such, this au- thor submits that basic research occupies a unique and lucrative niche driving clinical ap- plications. To whom all correspondence should be addressed: Camille A. Hardiman, Boyer Center for Molecular Medicine, 295 Congress Ave., PO Box 0812, New Haven, CT 06536-0812; Tele: 203-737-2409; Fax: 203-737-2630; Email: camille.hardiman@yale.edu. †Abbreviations: AT, anthrax toxin; AVA, anthrax vaccine absorbed; BSL, biosafety level; cAMP, cyclic AMP; CopI, coatomer protein I; DTA, Diphtheria Toxin fragment A; EF, edema factor; EGF, epidermal growth factor; EGFR, epidermal growth factor receptor; IL- 2, interleukin-2; LF, lethal factor; LFn, LF N-terminal domain; MAPK-K, mitogen-activated protein kinase-kinase; NIAID, National Institute for Allergy and Infectious Disease; NIH, National Institutes of Health; PA, protective antigen; PA63, protective antigen 63-kDa frag- ment; rPA, recombinant PA. Keywords: John Collier, anthrax toxin, protective antigen, vaccine, translational research 285