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Faculty Detail    
Name MICHAEL E. NIEDERWEIS
 
Campus Address BBRB 609 Zip 2170
Phone 205-975-4390
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.

Research/Clinical Interest
Title
Novel proteins in the outer membrane of mycobacteria: Functions, structures, role in tuberculosis and applications
Description
Tuberculosis is caused by Mycobacterium tuberculosis and kills approximately two million people each year, more than any other bacterial pathogen. Yet, M. tuberculosis is one of the least understood bacterial pathogens. Virulence of M. tuberculosis is mainly associated with its ability to survive within macrophages. The outer membrane is an efficient permeability barrier for toxic molecules and plays a key role in protecting M. tuberculosis from the host immune system. To date, the molecular basis for the transport of most solutes across the outer membrane is unknown for M. tuberculosis. The aim of our research is to identify and characterize the outer membrane proteome of M. tuberculosis. The identification of proteins that enable transport of solutes across the outer membrane would represent a major breakthrough in our understanding of the physiology and drug resistance of M. tuberculosis. The proteins which functionalize the outer membrane of M. tuberculosis are fascinating for several reasons: (i) They fulfill essential biological functions. (ii) The outer membrane proteins reside in a highly unusual lipid membrane. Therefore, their structures will be novel as we have already shown for MspA. This makes it likely that they also function by novel mechanisms. iii) Some outer membrane proteins are likely to represent attractive drug targets because inhibitors do not have to cross the notoriously impermeable outer membrane, which is a major determinant of the intrinsic drug resistance of M. tuberculosis. (iv) Many outer membrane proteins of pathogenic Gram-negative bacteria are involved in interactions with host cells. We assume that this will also be the case for M. tuberculosis.

Selected Publications 
Publication PUBMEDID
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