Lipopolysaccharides of Escherichia coli K12 Strains That Express Cloned Genes for the Ogawa and Inaba Antigens of Vibrio cholerae O1: Identification of O-Antigenic Factors
スポンサーリンク
概要
- 論文の詳細を見る
Structural and serological studies were performed with the lipopolysaccharide (LPS) expressed by Escherichia coli K12 strains No. 30 and No. 64, into which cosmid clones derived from Vibrio cholerae O1 NIH 41 (Ogawa) and NIH 35A3 (Inaba) had been introduced, respectively. The two recombinant strains, No. 30 (Ogawa) and No. 64 (Inaba), produced LPS that included, in common, the O-polysaccharide chain composed of an α(1→2)-linked N-(3-deoxy-L-glycero-tetronyl)-D-perosamine (4-amino-4, 6-dideoxy-D-manno-pyranose) homopolymer attached to the core oligosaccharide of the LPS of E. coli K12. Structural analysis revealed the presence of N-(3-deoxy-L-glycero-tetronyl)-2-O-methyl-D-perosamine at the non-reducing terminus of the O-polysaccharide chain of LPS from No. 30 (Ogawa) but not from No. 64 (Inaba). Serological analysis revealed that No. 30 (Ogawa) and No. 64 (Inaba) LPS were found to share the group antigen factor A of V. cholerae O1. They were distinguished by presence of the Ogawa antigen factor B [co-existing with relatively small amounts of the Inaba antigen factor (c)] in the former LPS and the Inaba antigen factor C in the latter LPS. It appears, therefore, that No. 30 (Ogawa) and No. 64 (Inaba) have O-antigenic structures that are fully consistent with the AB(c) structure for the Ogawa and the AC structure for the Inaba O-forms of V. cholerae O1, respectively. Thus, the present study clearly confirmed our previous finding that the Ogawa antigenic factor B is substantially related to the 2-O-methyl group at the non-reducing terminus of the α(1→2)-linked N-(3-deoxy-L-glycero-tetronyl)-D-perosamine homopolymer that forms the O-polysaccharide chain of LPS of V. cholerae O1 (Ogawa).
- 微生物学・免疫学学会連合の論文
微生物学・免疫学学会連合 | 論文
- The Structural Proteins of Newcastle Disease Virus
- The Pathogenicity of Newcastle Disease Virus Isolated from Migrating and Domestic Ducks and the Susceptibility of the Viral Glycoproteins to Proteolytic Cleavage
- Analysis of Nuclear Accumulation of Influenza Nucleoprotein Antigen Using a Temperature-Sensitive Mutant
- Enhancement of fusion from within by Antiviral Antibody in Cells Infected with Newcastle Disease Virus
- Analysis of Nuclear Accumulation of Influenza Nucleoprotein Antigen in the Presence of p-Fluorophenylalanine