Gram-negative pathogens have increasingly developed resistance to antibiotics in the last decade. Using Structural Biology, I study the structure of bacterial virulence factors and membrane secretion systems to understand the mechanisms of infection and propose new targets for antimicrobial development.
Assistant Professor Noha Elshamy
| Campus | Katahira campus |
|---|---|
| Laboratory |
Applied Biological Molecular Science
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| Tel | +81-22-217-6206 |
| elshamy.noha.c1＠tohoku.ac.jp |
| Career |
May 2026 – current Assistant Professor, Graduate School of Life Sciences, Tohoku University |
|---|---|
| Selected Publications |
Note: selected papers have been published under the academic name Elhosseiny.
|
Recent Activities
Bacterial secretion systems:
I have recently focused on sequence and structural variability in the outer membrane component of the Type II Secretion System (T2SS) in Gram-negative bacterial. My current goal is to understand the correlation between domain sequence length and structural organization, with substrate recruitment and the secretion mechanism. I use techniques such as genomic mutagenesis, functional assays and cryo-EM single particle analysis to understand how the outer membrane component of the T2SS enables the secretion of virulence protein.
I have recently focused on sequence and structural variability in the outer membrane component of the Type II Secretion System (T2SS) in Gram-negative bacterial. My current goal is to understand the correlation between domain sequence length and structural organization, with substrate recruitment and the secretion mechanism. I use techniques such as genomic mutagenesis, functional assays and cryo-EM single particle analysis to understand how the outer membrane component of the T2SS enables the secretion of virulence protein.
Lipoprotein membrane localization:
The lipoprotein outer membrane localization machinery plays an important role in the processing and transport of lipoproteins that are important for membrane structure, as well as displaying virulence-related proteins on the surface of the cell, where it engages with host receptors. Since this machinery is vital for the life of the microbial cell, it represents a good target for antimicrobial development. Using X-ray crystallography, I determine the structure of the components of the lipoprotein localization system and employ computational drug design to test for lead compounds for antimicrobial development.
The lipoprotein outer membrane localization machinery plays an important role in the processing and transport of lipoproteins that are important for membrane structure, as well as displaying virulence-related proteins on the surface of the cell, where it engages with host receptors. Since this machinery is vital for the life of the microbial cell, it represents a good target for antimicrobial development. Using X-ray crystallography, I determine the structure of the components of the lipoprotein localization system and employ computational drug design to test for lead compounds for antimicrobial development.