Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin

Kanto, Sachiko; Okino, Hiroshi; Aizawa, Shin‐Ichi; Yamaguchi, Shigeru

doi:10.1016/0022-2836(91)90187-b

Cited by 113 publications

(99 citation statements)

References 27 publications

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“…Little is known about the distribution of methylated flagellins among salmonellae, except for a limited study of the distribution of the methylase gene (formerly designated nml for lysine N-methy lase) by phage transduction experiments (Stocker et al, 1961). The available evidence suggests that all lysine residues which are surfaceexposed in the native flagellum are methylated (Kanto et al, 1991). With respect to recent efforts to express foreign antigens as part of the mature flagellum with the aim of producing live recombinant vaccines (Newton et al, 1989(Newton et al, , 1995Verma et al, 1995), we note that methylation could affect the antigenicity of these foreign epitopes, modifying or abolishing immune responses directed against them.…”

Section: Discussionmentioning

confidence: 99%

The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200 element in Salmonella typhimurium

et al. 1997

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The cloning and molecular genetic analysis of a locus mapping within the flagellar gene (fli) complex of Salmonella typhimurium is reported. A copy of the insertion element IS200 was located in a noncoding stretch of DNA upstream of the fliA gene. Comparative nucleotide sequence analysis showed that this copy of IS200 was 711 bp long and that its flanking regions contained no features common to other characterized insertion sites of this element. The element was located 37 bp downstream of an ORF whose product was shown by interspecific transfer and amino acid analysis to carry out N-methylation of selected lysine residues in Salmonella flagellin. The sequence and phenotype of this ORF identified it as fliB, encoding the only prokaryotic N-methylase acting on amino groups to have been characterized to date. It was found to be conserved among all clinically significant serovars of Salmonella. The IS200 insertion site is of particular interest since it was conserved in all but two rare evolutionary lines of 5. typhimurium, and was absent from 85 Salmonella strains belonging to 37 other serovars. It is thus a phylogenetically significant marker at the serovar level.

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Section: Discussionmentioning

confidence: 99%

The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200 element in Salmonella typhimurium

et al. 1997

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“…On the other hand, both strains undergo a similar level of change (about 6 %) when the salt concentration is halved to 85 mM. Flagellin structure may be affected by amino acid substitutions Kanto et al (1991) identified key mutations in strains of S. typhimurium compared to the wild-type SJW1103 that were responsible for changes in flagellar shape in that The schematic diagram (c) illustrates how the shape of the FlaA flagellum was observed to change with respect to FlaAB at pH 5?8 and in 425 mM NaCl, and thus how this change affects amplitude and wavelength. The amplitude is reduced in FlaA (A1) with respect to FlaAB (A2), while the wavelength (B1) increases compared to FlaAB (B2).…”

Section: + Cells Are Motile In Viscous Mediummentioning

confidence: 97%

Enhanced motility of a Proteus mirabilis strain expressing hybrid FlaAB flagella

2004

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Proteus mirabilis has two tandemly arranged flagellin-encoding genes, flaA and flaB. flaA is transcribed from a s 28 promoter, while flaB is silent. flaA and flaB can undergo reversible rearrangement to produce a set of hybrid genes referred to as flaAB. Flagellins composed of FlaAB protein have a different amino acid sequence and are antigenically distinct from flagellin composed of FlaA, implicating flagellin gene conversion as a putative virulence mechanism for P. mirabilis. The change in amino acid sequence is also hypothesized to alter the filament helix and, hence, affect the motility of FlaAB-expressing strains. To test this hypothesis, the motility of wild-type P. mirabilis was compared with that of a strain, DF1003, locked into the FlaAB + hybrid phase, under conditions of altered ionic strength, pH and viscosity. Cell motion tracking analysis showed that DF1003 has wild-type swimming velocity at physiological conditions, but moves significantly faster and travels further compared to the wild-type at NaCl concentrations greater than 170 mM. DF1003 is also significantly faster than the wild-type at pH 5?2, 5?8 and 8?2, and at 5 and 10 % polyvinylpyrrolidone. Measurements of amplitude and wavelength for isolated flagella subjected to pH 5?8 or 425 mM NaCl showed a loss of helical structure in FlaA flagella compared to FlaAB filaments, a feature that could significantly affect motility under these conditions. These results support a hypothesis that FlaAB flagellin imparts a motile advantage to P. mirabilis in conditions that otherwise may impede bacterial movement. In a broader context, flagellar antigenic variation, commonly thought to serve as means to avoid host defences, may also enhance motility in other bacterial species, thus aiding in the adaptation and survival of the cells.

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“…Heat-killed S. typhimurium (HKST) 3 (3) was prepared from an overnight culture of SL1344 that was washed twice in PBS before incubation at 65°C for 1 h. Other heat-killed Salmonella or Shigella were prepared in a similar manner, and each strain was assessed for motility in soft agar to confirm flagella expression before the preparation of heat-killed bacteria. FliC was prepared from phase-fixed bacterial strains BC115 and BC116 using both shearing and differential centrifugation as previously described (19,20). FliC was further purified using a Sephadex G-200 column, collecting fractions that contained a single band of the relevant m.w.…”

Section: Bacterial Strains Infection and Ag Preparationmentioning

confidence: 99%

Characterization of CD4+ T Cell Responses During Natural Infection with Salmonella typhimurium

McSorley

Cookson

Jenkins

2000

The Journal of Immunology

221

217

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CD4+ T cells are important for resistance to infection with Salmonella typhimurium. However, the Ag specificity of this T cell response is unknown. Here, we demonstrate that a significant fraction of Salmonella-specific CD4+ T cells respond to the flagellar filament protein, FliC, and that this Ag has the capacity to protect naive mice from lethal Salmonella infection. To characterize this Ag-specific response further, we generated FliC-specific CD4+ T cell clones from mice that had resolved infection with an attenuated strain of Salmonella. These clones were found to respond to an epitope from a constant region of FliC, enabling them to cross-react with flagellar proteins expressed by a number of distinct Salmonella serovars.

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Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin

Cited by 113 publications

References 27 publications

The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200 element in Salmonella typhimurium

The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200 element in Salmonella typhimurium

Enhanced motility of a Proteus mirabilis strain expressing hybrid FlaAB flagella

Characterization of CD4+ T Cell Responses During Natural Infection with Salmonella typhimurium

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