Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174

Tomoko KAWAURA; Minoru INAGAKI; Shuichi KARITA; Muneharu KATO; Shiro NISHIKAWA; Naoki KASHIMURA

doi:10.1271/bbb.64.1993

Biochemistry & Molecular Biology Notes

Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174

Tomoko KAWAURA, Minoru INAGAKI, Shuichi KARITA, Muneharu KATO, Shiro NISHIKAWA, Naoki KASHIMURA

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Keywords: spike G protein, φX174, lipopolysaccharide, enzyme-linked assay, phage receptor

JOURNAL FREE ACCESS

2000 Volume 64 Issue 9 Pages 1993-1997

DOI https://doi.org/10.1271/bbb.64.1993

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Abstract

The spike G protein of bacteriophage φX174 was prepared as a hexa histidine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound specifically to lipopolysaccharides (LPSs) of the φX174-sensitive strains, and did not bind to LPSs of the φX174-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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