Amal Amer MD, PhD

Assistant Professor

Biological Research Tower

460W 12th Ave

Room 1014

Columbus, Ohio 43210,

Email: Amal.Amer@osumc.edu

Tel: (614) 247-1566

Fax: (614) 292-9616

Center for Microbial Interface Biology
http://cmib.osu.edu/

Education

Postdoctoral fellowship: University of Michigan, 2001-2006

Ph.D.: University of Western Ontario, London, Ontario, Canada. 2002

M.D.: Faculty of Medicine, Cairo University, Cairo, Egypt. 1986

Research interests

     Legionella pneumophila and Burkholderia cepacia are pulmonary pathogens that can cause lung infections in immunocompromised individuals.

     Legionella pneumophila is an intracellular bacterium which causes an acute form of pneumonia called Legionnaires’s disease. Our previous work showed that mouse macrophages lacking the NOD-LRR protein Ipaf or its downstream effector caspase-1 are permissive to intracellular Legionella replication.  We also demonstrated that cytosolic exposure of bacterial flagellin was sufficient for the induction of caspase-1 activation through host Ipaf, but not TLR5.  Interestingly, our results revealed that Ipaf and caspase-1 restrict Legionella replication through the regulation of phagosome maturation in response to flagellin, providing a novel function for NOD-LRR family proteins in host defense against an intracellular bacterium. 

     Recently we became interested in Burkholderia cepacia, an opportunistic pathogen that can cause severe lung infections in cystic fibrosis patients.

     Our laboratory will examine the host inflammatory responses to Legionella pneumophila and Burkholderia cepacia in macrophages and in mice models of infections.

 Publications:
1.  Lamkanfi M, Amer A, Kanneganti TD, Munoz-Planillo R, Chen G, Vandenabeele P, Fortier A, Gros P, & G Nunez  (2007).The NLR family member Naip5/Birc1e restricts Legionella pneumophila growth independent
of caspase-1 activation. Journal of Immunology. 178 (12), 8022-8027.
2.  Amer A, Franchi L, Kanneganti TD, Body-Malapel M, Özören N, Brady G, Gewitz A, Akira S & Núñez.(2006). Regulation of Legionella phagosome maturation and infection through flagellin and host Ipaf.  Journal of Biological Chemistry. 281 (46), 35217-35223.
3.  Franchi L, Amer A (equal first authorship), Mathilde Body-Malapel, Nesrin Ozoren, Kanneganti TD, Bertin J, Coyle A, Grant EP & Núñez. (2006). Cytosolic flagellin requires Ipaf to activate caspase-1 and interleukin-1b in Salmonella infected macrophages. Nature Immunology. 7 (6), 576-582.
4.  Kanneganti TD, Body-Malapel M, Amer A, Park JH, Whitfield J, Taraporewala ZF, Miller D, Patton JT, Inohara N & Núñez. (2006). Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double –stranded RNA. Journal of Biological Chemistry. 281 (48), 36560-36568.
5.  Kanneganti TD, Özören N, Body-Malapel M, Amer A, Park JH, Franchi L, Whitfield J, Barchet W, Colonna M, Vandenabeele P, Bertin J, Coyle A, Grant EP, Akira S & Núñez. (2006). Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3.  Nature. 440, 233-236.
6.  Amer, A. O. and M. S. Swanson. 2005. Autophagy is an immediate macrophage response to Legionella pneumophila. Cellular Microbiology. 7:765-78.
7.  Amer, A. O., B. B. Byrne and M. S. Swanson. 2005. Macrophages rapidly transfer pathogens from cholesterol-rich vacuoles to autophagosomes. Autophagy. 1:53-58.
8.  Amer, A. O. and M. S. Swanson. 2002. A phagosome of one's own: A microbial guide to life in the macrophage. Current Opinion in Microbiology 5:56-61.
9.  Amer, A. O. and M. A. Valvano. 2002. Conserved aspartic acids are essential for the enzymatic activity of the WecA protein initiating  the biosynthesis of O-specific lipopolysaccharide and enterobacterial  common antigen in Escherichia coli. Microbiology 148: 571-582.
10.  Amer, A. O. and M. A. Valvano. 2001. Conserved amino acid residues found in a predicted cytosolic domain of WecA (UDP-N-acetyl glucosamine:undecaprenol- phosphate N-acetylglucosamine-1- phosphate transferase) are implicated in the recognition of UDP-N- acetylglucosamine. Microbiology 147:3015-3025.
11.  Amer, A. O. and M. A. Valvano. 2000. The N-terminal region of the Escherichia coli WecA (Rfe) protein (N-acetylglucosamine bactoprenyl transferase) is required for function but not for membrane insertion. Journal of Bacteriology, 182: 498-503.