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Recognition of receptor lipopolysaccharides by spike G protein of bacteriophage phiX174.

Authors
  • Kawaura, T
  • Inagaki, M
  • Karita, S
  • Kato, M
  • Nishikawa, S
  • Kashimura, N
Type
Published Article
Journal
Bioscience, biotechnology, and biochemistry
Publication Date
Sep 01, 2000
Volume
64
Issue
9
Pages
1993–1997
Identifiers
PMID: 11055411
Source
Medline
License
Unknown

Abstract

The spike G protein of bacteriophage phiX174 was prepared as a hexa histidine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound specifically to lipopolysaccharides (LPSs) of the phiX174-sensitive strains, and did not bind to LPSs of the phiX174-insensitive strains. The truncated G protein obtained after trypsin digestion of HisG had the similar affinity to the LPSs to HisG, indicating that eight amino acid residues from the N-terminus are not essential to the binding with the LPSs.

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