Photo of Simon Daefler

Simon Daefler

  • ASSISTANT PROFESSOR Medicine, Infectious Diseases
Print ProfilePrint Profile

Education

  • Ph.D., University of Cologne

  • National Institutes of Health

  • New York University

  • Harvard Medical School

  • The Rockefeller University

  • M.D., University of Cologne

Research

Dr. Daifler??s research interests are focused on two intracellular pathogens, salmonella and francisella. His work with these pathogens dissects out intracellular host pathogen interactions that allow survival of the organism within key target cells including the macrophage and heptocate. These pathogens are important subjects of study both because of their impact on world health and their potential use as a tool for bioterrorism. Dr. Daefler is Executive Director of the Biosafety Laboratory Level 3+ (BSL3+) at Mount Sinai School of Medicine. He also has extensive experience as an educator and mentor.

Publications

Daefler S, Klotman ME, Wong-Staal F. Trans-activating rev protein of the human immunodeficiency virus 1 interacts directly and specifically with its target RNA. Proc Natl Acad Sci U S A 1990 June; 87(12): 4571-4575.

Goldblum N, Daefler S, Llana T, Ablashi D, Josephs S, Salahuddin Z. Susceptibility to HIV-1 infection of a human B-lymphoblastoid cell line, DG75, transfected with subgenomic DNA fragments of Epstein-Barr virus. Dev Biol Stand 1990; 72: 309-313.

Bonnekoh B, Daefler S, Krueger GR, Mahrle G. Keratinocyte lipid fluidity under the influence of cholesterols, Keratinocyte lipid fluidity under the influence of cholesterols,Keratinocyte lipid fluidity under the influence of cholesterols,hydrocortisones, . In Vivo 1991 May-June; 5(3): 227-232.

Li G, Lisziewicz J, Sun D, Zon G, Daefler S, Wong-Staal F, Gallo RC, Klotman ME. Inhibition of Rev activity and human immunodeficiency virus type 1 replication by antisense oligodeoxynucleotide phosphorothioate analogs directed against the Rev-responsive element. J Virol 1993 November; 67(11): 6882-6888.

Navarre WW, Daefler S, Scneewind O. Cell wall sorting of lipoproteins in Staphylococcus aureus. J Bacteriol 1996 January; 178(2): 441-446.

Daefler S, Guilvout I, Hardie KR, Pugsley AP, Russel M. The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function . Mol Microbiol 1997 May; 24(3): 465-475.

Daefler S, Russel M, Model P. Module swaps between related translocator proteins pIV(f1), pIV(IKe) and PulD: identification of a specificity domain. J Mol Biol 1997 March; 266(5): 978-992.

Daefler S, Russel M. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol Microbiol 1998 June; 28(6): 1367-1380.

Daefler S. Type III secretion by Salmonella typhimurium does not require contact with a eukaryotic host. Mol Microbiol 1999 January; 31(1): 45-51.

Lee AH, Zareei MP, Daefler S. Identification of a NIPSNAP homologue as host cell target for Salmonella virulence protein SpiC. Cell Microbiol 2002 November; 4(11): 739-750.

Industry Relationships

Physicians and scientists on the faculty of the Icahn School of Medicine at Mount Sinai often interact with pharmaceutical, device and biotechnology companies to improve patient care, develop new therapies and achieve scientific breakthroughs. In order to promote an ethical and transparent environment for conducting research, providing clinical care and teaching, Mount Sinai requires that salaried faculty inform the School of their relationships with such companies.

Dr. Daefler has not yet completed reporting of Industry relationships.

Mount Sinai's faculty policies relating to faculty collaboration with industry are posted on our website at http://icahn.mssm.edu/about-us/services-and-resources/faculty-resources/handbooks-and-policies/faculty-handbook. Patients may wish to ask their physician about the activities they perform for companies.

Edit profile in Sinai Central

Address

Annenberg Building Floor 23, Room 09
1468 Madison Avenue
New York, NY 10029

Tel: 212-241-4690
Fax: 646-607-1011