1996•Infection and ImmunityOpen access

Purification and characterization of a pilus of a Vibrio cholerae strain: a possible colonization factor

Tetsu Yamashiro, Masaaki Iwanaga

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Abstract

A new flexible type of pilus was purified from Vibrio cholerae non-O1, non-0139 strain NAGV14 and characterized. The molecular mass of the pilin was estimated to be 20 kDa, and the antigenicity differed from that of known pili such as toxin-coregulated pili, mannose-sensitive hemagglutinating pili, V10 pili, and Al-1841 pili. The NAGV14 pilus was regarded as a colonization factor because the purified pili adhered to rabbit intestine and adhesion was inhibited by treating the organisms with the Fab fraction of an antipilus antibody. An intestinal receptor blockade using purified pili failed to inhibit adhesion of the organisms. The NAGV14 pili adhered to the surface of live V. cholerae. An antigen cross-reacting with the NAGV14 pili was widely and specifically distributed among V. cholerae strains irrespective of serotype and biotype. The amino acid sequence of the pilin was homologous with that of MshA. The NAGV14 pili did not agglutinate human and rabbit erythrocytes.

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A new flexible type of pilus was purified from Vibrio cholerae non-O1, non-0139 strain NAGV14 and characterized. The molecular mass of the pilin was estimated to be 20 kDa, and the antigenicity differed from that of known pili such as toxin-coregulated pili, mannose-sensitive hemagglutinating pili, V10 pili, and Al-1841 pili. The NAGV14 pilus was regarded as a colonization factor because the purified pili adhered to rabbit intestine and adhesion was inhibited by treating the organisms with the Fab fraction of an antipilus antibody. An intestinal receptor blockade using purified pili failed to inhibit adhesion of the organisms. The NAGV14 pili adhered to the surface of live V. cholerae. An antigen cross-reacting with the NAGV14 pili was widely and specifically distributed among V. cholerae strains irrespective of serotype and biotype. The amino acid sequence of the pilin was homologous with that of MshA. The NAGV14 pili did not agglutinate human and rabbit erythrocytes.

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Available abstract

A new flexible type of pilus was purified from Vibrio cholerae non-O1, non-0139 strain NAGV14 and characterized. The molecular mass of the pilin was estimated to be 20 kDa, and the antigenicity differed from that of known pili such as toxin-coregulated pili, mannose-sensitive hemagglutinating pili, V10 pili, and Al-1841 pili. The NAGV14 pilus was regarded as a colonization factor because the purified pili adhered to rabbit intestine and adhesion was inhibited by treating the organisms with the Fab fraction of an antipilus antibody. An intestinal receptor blockade using purified pili failed to inhibit adhesion of the organisms. The NAGV14 pili adhered to the surface of live V. cholerae. An antigen cross-reacting with the NAGV14 pili was widely and specifically distributed among V. cholerae strains irrespective of serotype and biotype. The amino acid sequence of the pilin was homologous with that of MshA. The NAGV14 pili did not agglutinate human and rabbit erythrocytes.

Key concepts: Pilus, Pilin, Vibrio cholerae, Microbiology, Biology, Bacterial adhesin, Antigenicity, Fimbria

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