Crucial role of the lipid part of lipopolysaccharide for conformational change of minor spike H protein of bacteriophage phiX174.
The contribution of the lipid part of lipopolysaccharide (LPS) to recognition by minor spike H protein of bacteriophage phiX174 was investigated by comparing the interactions of H protein with LPS and its deacylated derivatives. The fluorescence and circular dichroism (CD) spectra of H protein increased upon binding to intact LPS and a partially deacylated derivative. In contrast, completely deacylated derivatives showed lower affinities and almost no fluorescence or CD changes of H protein. These results demonstrate that the lipid part of LPS is responsible for the conformational change of minor spike H protein, which would function as a trigger for phage DNA ejection for infection of the host cell.
Inagaki
Minoru
M
Department of Lifescience, Faculty of Bioresources, Mie University, 1577 Kurima-machiya, Tsu, Mie 514-8507, Japan. inagaki@bio.mie-u.ac.jp
Wakashima
Hirohito
H
Kato
Muneharu
M
Kaitani
Koji
K
Nishikawa
Shiro
S
D010584:Bacteriophage phi X 174 / Q000737:chemistry*; D001665:Binding Sites; D002942:Circular Dichroism; D008055:Lipids / Q000737:chemistry / Q000494:pharmacology*; D008070:Lipopolysaccharides / Q000494:pharmacology*; D017433:Protein Structure, Secondary / Q000187:drug effects*; D015678:Viral Structural Proteins / Q000737:chemistry*
D008055:Lipids; D008070:Lipopolysaccharides; D015678:Viral Structural Proteins