Research
Faculty Members
Biophysical Chemistry（Chemistry）
Kawahara KazukiAssistant professor
He received his Ph. D from Osaka University in 2009. After working as JSPS research fellow at Osaka University, he became a specially appointed assistant professor at Nara Women’s University in 2010. He returned to Osaka University in 2013 as a specially appointed assistant professor and was appointed to current position from 2017. His current research focus is on the structural biology of infectious diseases.
Research theme
Structural biology of bacterial virulence factors
Bacterial pathogens use a wide variety of virulence factors to cause human infection. These factors include bacterial toxins, effectors, adhesins, and specialized secretion systems. By using structural biology methods, we are investigating the molecular mechanisms of action of these virulence factors during human infection.
Development of anti-adhesion agents as novel therapeutics for multi-drug resistant bacteria
The emergence of new multi-drug resistant bacteria is currently a serious concern. Therefore, the development of non-antibiotic based drugs as an alternative therapeutic option for bacterial infectious diseases is now urgently needed. For such purposes, we focus on the process of bacterial adhesion, which is most crucial step in bacterial infection, and try to develop anti-adhesive agents that specifically interfere with the type IV pili-mediated host-pathogen interactions of enteric pathogens such as enterotoxigenic Escherichia coli. and Vibrio cholerae.
Development of methods for characterizing protein-protein interactions (PPIs)
Protein-protein interactions (PPIs) play outstanding roles in almost all of the biological processes, and the knowledge of three-dimensional structures of proteins and their complexes are crucial to understand PPIs. We utilize an integrated approach spanning biophysics, biochemistry, chemical biology and structural biology with the aim of understanding and characterizing the PPIs of disease associated proteins.
Representative achievements
Nakamura S., Kawahara K., Oki H., Yoshida T., Ohkubo T., Kobayashi Y., Maruno T., Motooka D., Matsuda S., Kodama T., Iida T., Tsujino Y., Fukakusa S. (2019) Peptide inhibiting colonization by pathogenic bacteria, and including colonization inhibitor same. US Patent Application No.16/097, 219 Publication date Sep.19.
Oki H.,* Kawahara K.,* Maruno T., Imai T., Muroga Y., Fukakusa S., Iwashita T., Kobayashi Y., Matsuda S., Kodama T., Iida T., Yoshida T., Ohkubo T., Nakamura S. (2018) Interplay of a secreted protein with type IVb pilus for efficient enterotoxigenic Escherichia coli colonization. Proc. Natl. Acad. Sci. USA 115, 7422-7427.
Kawahara K., Yonogi S., Munetomo R., Oki H., Yoshida T., Kumeda Y., Matsuda S., Kodama T., Ohkubo T., Iida T., Nakamura S. (2016) Crystal structure of the ADP-ribosylating component of BEC, the binary enterotoxin of Clostridium perfringens. Biochem. Biophys. Res. Commun. 480, 261-267.
Kawahara K., Oki H., Fukakusa S., Yoshida T., Imai T., Maruno T., Kobayashi Y., Motooka D., Iida T., Ohkubo T., Nakamura S. (2016) Homo-trimeric Structure of the Type IVb Minor Pilin CofB Suggests Mechanism of CFA/III Pilus Assembly in Human Enterotoxigenic Escherichia coli. J Mol Biol. 428, 1209-1226.
Kawahara K., Yoshida T., Maruno T., Oki H., Ohkubo T., Koide T., Kobayashi Y. (2020) Spatiotemporal regulation of PEDF signaling by type I collagen remodeling. Proc. Natl. Acad. Sci. USA 117 11450-11458.
Kawahara K., Nemoto N., Motooka D., Nishi Y., Doi M., Uchiyama S., Nakazawa T., Nishiuchi Y., Yoshida T., Ohkubo T., Kobayashi Y. (2012) Polymorphism of collagen triple helix revealed by 19F NMR of model peptide [Pro-4(R)-hydroxyprolyl-Gly]3-[Pro-4(R)-fluoroprolyl-Gly]-[Pro-4(R)-hydroxyprolyl-Gly]3. J. Phys. Chem. B. 116, 6908-6915.
Kawahara K., Nishi Y., Nakamura S., Uchiyama S., Nishiuchi Y., Nakazawa T., Ohkubo T., and Kobayashi Y. (2005) Effect of Hydration on the Stability of the Collagen-like Triple-Helical Structure of [4(R)-Hydroxyprolyl-4(R)-hydroxyprolylglycine]10. Biochemistry 44, 15812-15822.
