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Faculty Detail    
Name MICHAEL E. NIEDERWEIS
 
Campus Address BBRB 609 Zip 2170
Phone
E-mail  mnieder@uab.edu
Other websites PubMed Listing
     


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Microbiology  Microbiology Professor
Center  Center for AIDS Research  Center for AIDS Research Professor
Center  Center for Biophysical Sciences/Engineering  Center for Biophysical Sciences/Engineering Professor

Graduate Biomedical Sciences Affiliations
Biochemistry and Structural Biology 
Cellular and Molecular Biology Program 
Immunology 
Medical Scientist Training Program 
Microbiology 

Biographical Sketch 
Michael Niederweis (b. 1964), Professor of Microbiology, received a diploma in chemistry from the Saarland University, Germany, in 1989, and a Ph.D. in microbiology from the University of Erlangen-Nuernberg, Germany, in 1993. His graduate studies were with Dr. Wolfgang Hillen on the structural analysis of protein-DNA interactions. From 1994-1996, Dr. Niederweis did postdoctoral studies with Dr. Donald Crothers at the Yale University, New Haven, Dr. Lee W. Riley at the Cornell University, Medical College, New York, and Dr. Roland Benz, University of Wuerzburg. In 1997, he established his laboratory in the Microbiology Department of the University of Erlangen-Nuernberg, Germany, to study mycobacterial porins. He obtained multiple young investigator awards. Dr. Niederweis joined the UAB faculty in 2004. In 2017 Dr. Niederweis was appointed as the inaugural holder of the endowed professorship in Bacteriology at UAB. In 2018, he was elected as a member of the American Academy of Microbiology.



Research/Clinical Interest
Title
Novel proteins in the outer membrane of mycobacteria: Functions, structures, role in tuberculosis and applications
Description
One of the most prominent features of M. tuberculosis is its unusual outer membrane that plays a crucial role in the intrinsic drug resistance and in survival of M. tuberculosis in vivo. This membrane is functionalized by intriguing proteins which provide essential functions such as nutrient uptake, have new structures and likely function by novel mechanisms. We discovered the first outer membrane channel protein in mycobacteria, obtained the first crystal structure of a mycobacterial outer membrane protein and demonstrated that mycobacteria indeed have two membranes. Our goal is to identify and characterize outer membrane proteins of M. tuberculosis. One of those proteins, CpnT, enables the secretion of the major exotoxin of M. tuberculosis, a NAD+ glycohydrolase which triggers necroptosis in infected macrophages. We use state-of-the art genetic, biochemical, biophysical and structural biology approaches to achieve our aims.

Selected Publications 
Publication PUBMEDID
NAD(+) depletion triggers macrophage necroptosis, a cell death pathway exploited by Mycobacterium tuberculosis  29996103 
PPE surface proteins are required for heme utilization by Mycobacterium tuberculosis  28119467 
The Tuberculosis Necrotizing Toxin kills macrophages by hydrolyzing NAD  26237511 
Surface sphingomyelin hydrolysis by the outer membrane protein Rv0888 supports replication of Mycobacterium tuberculosis in macrophages  26036301 
The Mycobacterium tuberculosis outer membrane channel protein CpnT confers susceptibility to toxic molecules  25645841 
An outer membrane channel protein of Mycobacterium tuberculosis with exotoxin activity  24753609 
Self-poisoning of Mycobacterium tuberculosis by interrupting siderophore recycling  24497493 
Discovery of a siderophore export system essential for virulence of Mycobacterium tuberculosis  23431276 
MspA nanopores from subunit dimers  22719928 
Reading DNA at single-nucleotide resolution with a mutant MspA nanopore and phi29 DNA polymerase  22446694 
Copper resistance is essential for virulence of Mycobacterium tuberculosis  21205886 
Nanopore DNA sequencing with MspA  20798343 
Mycobacterial outer membranes: in search of proteins  20060722 
Single-molecule DNA detection with an engineered MspA protein nanopore  19098105 
The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients  16238622 
Multidrug resistance of a porin deletion mutant of Mycobacterium smegmatis  15504836 
The structure of a mycobacterial outer-membrane channel  14976314 
Mycobacterial porins--new channel proteins in unique outer membranes  12940978 
Porins in the cell wall of Mycobacterium tuberculosis  10515949 

Keywords
tuberculosis, virulence, antibiotic resistance, membrane, proteins, transport, nanotechnology