Inspection of mechanism for recognition of host by phage
Project/Area Number |
23570211
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Molecular biology
|
Research Institution | Osaka University |
Principal Investigator |
YONESAKI Tetsuro 大阪大学, 理学(系)研究科(研究院), 教授 (90115965)
|
Co-Investigator(Kenkyū-buntansha) |
OTSUKA Yuichi 大阪大学, 大学院理学研究科, 助教 (10548861)
|
Project Period (FY) |
2011-04-28 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | T4ファージ / 大腸菌 / OmpC / LPS / 吸着 / 尾部繊維先端部位 / T4ファージ / ファージ / 宿主認識 / ポリン / 尾線維 / 尾部基盤スパイク |
Outline of Final Research Achievements |
T4 adsorption to E. coli K12 strain depends on the presence of OmpC, but T4 can adsorb to B strain independently of OmpC. Using K12 mutants defective in various genes required for LPS synthesis, we systematically analyzed the adsorption of T4 phage to these mutants dependent on or independent of OmpC. Furthermore, we isolated T4 mutants which can adsorb to B strain but not to K12 strain or vice versa. These results strongly suggest that T4 has two different mechanisms for adsorption to host cells. In addition, present study identified specific structures in OmpC and the distal tip of T4 long tail fiber, required for the recognition of OmpC by T4.
|
Report
(5 results)
Research Products
(25 results)
-
[Journal Article] AbpA and AbpB provide anti-phage activity in <i>Escherichia coli</i>2014
Author(s)
1.Yasui, R., Washizaki, A., Furihata, Y., Yonesaki, T., and Otsuka, Y.
-
Journal Title
Genes & Genetic Systems
Volume: 89
Issue: 2
Pages: 51-60
DOI
NAID
ISSN
1341-7568, 1880-5779
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
-
-
[Journal Article] Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance.2013
Author(s)
Wei, Y., Gao, Z., Otsuka, Y., Naka, K., Yonesaki, T., Zhang, H., and Dong, Y.
-
Journal Title
Mol. Microbiol.
Volume: 90
Issue: 5
Pages: 956-965
DOI
Related Report
Peer Reviewed
-
-
-
-
-
-
-
-
[Presentation] T4 Alt modifies E. coli MazF2014
Author(s)
Abdulraheem Alawneh, Tetsuro Yonesaki, Yuichi Otsuka
Organizer
EMBO Conference on Viruses of Microbes III
Place of Presentation
Zurich, Switzerland
Year and Date
2014-07-08
Related Report
-
-
-
-
-
-
-
-
-
-
-
-
-
-