dependent manner: Relatively large beads (0.5–1 μm in diameter) move fast relative to the cell body, whereas, small beads
(0.1–0.2 μm) do not move on the cell body, i.e., staying at one
position on the cell body. The phenomena suggest that LPS can
freely move on the outer membrane and that the observed
beads’ movements are caused by drag force exerted on beads.
In other words, beads are retarded from the swimming cell by
viscous drag [2].
References
1. Cox PJ, Twigg GI (1974) Leptospiral motility.
Nature 250:260–261
2. Tahara H, Takabe K, Sasaki Y et al (2018) The
mechanism of two-phase motility in the spirochete Leptospira: swimming and crawling. Sci
Adv 4:eaar7975
3. Goldstein SF, Charon NW (1990) Multipleexposure photographic analysis of a motile spirochete. Proc Natl Acad Sci U S A
87:4895–4899
4. Nakamura S, Leshansky A, Magariyama Y,
Namba K, Kudo S (2014) Direct measurement
of helical cell motion of the spirochete Leptospira. Biophys J 106:47–54
5. Josenhans C, Suerbaum S (2002) The role of
motility as a virulence factor in bacteria. Int J
Med Microbiol 291:605–614
6. Lertsethtakarn P, Ottemann KM, Hendrixson
DR (2011) Motility and chemotaxis in Campylobacter and Helicobacter. Ann Rev Microbiol
65:389–410
7. Lambert A, Picardeau M, Haake DA et al
(2012) FlaA proteins in Leptospira interrogans
are essential for motility and virulence but are
not required for formation of the flagellum
sheath. Infect Immun 80:2019–2025
8. Wunder EA, Figueira CP, Benaroudj N et al
(2016) A novel flagellar sheath protein, FcpA,
determines filament coiling, translational
motility and virulence for the Leptospira spirochete. Mol Microbiol 101:457–470
9. Bromley DB, Charon NW (1979) Axial filament involvement in the motility of Leptospira
interrogans. J Bacteriol 137:1406–1412
10. Picardeau M, Brenot A, Saint Girons I (2001)
First evidence for gene replacement in Leptospira spp. inactivation of L. biflexa flaB results in
non-motile mutants deficient in endoflagella.
Mol Microbiol 40:189–199
11. Sasaki Y, Kawamoto A, Tahara H et al (2018)
Leptospiral flagellar sheath protein FcpA interacts with FlaA2 and FlaB1 in Leptospira biflexa.
PLoS One 13:e0194923
12. Wunder EA, Slamti L, Suwondo DN et al
(2018) FcpB is a surface filament protein of
the endoflagellum required for the motility of
the spirochete Leptospira. Front Cell Infect
Microbiol 8:130
13. Islam MS, Takabe K, Kudo S, Nakamura S
(2014) Analysis of the chemotactic behaviour
of Leptospira using microscopic agar-drop
assay. FEMS Microbiol Lett 356:39–44
14. Affroze S, Islam MS, Takabe K, Kudo S, Nakamura S (2016) Characterization of leptospiral
chemoreceptors using a microscopic agar drop
assay. Curr Microbiol 73:202–205
15. Takabe K, Tahara H, Islam MS, Affroze S,
Kudo S, Nakamura S (2017) Viscositydependent variations in the cell shape and
swimming manner of Leptospira. Microbiology
163:153–160
16. Takabe K, Kawamoto A, Tahara H, Kudo S,
Nakamura S (2017) Implications of coordinated cell-body rotations for Leptospira motility. Biochem Biophys Res Commun
491:1040–1046
17. Berg HC, Turner L (1979) Movement of
microorganisms in viscous environments.
Nature 278:349–351
18. Takabe K, Nakamura S, Ashihara M, Kudo S
(2013) Effect of osmolarity and viscosity on the
motility of pathogenic and saprophytic Leptospira. Microbiol Immunol 57:236–239
19. Magariyama Y, Kudo S (2002) A mathematical
explanation of an increase in bacterial swimming speed with viscosity in linear-polymer
solutions. Biophys J 83:733–739
20. Nakamura S, Adachi Y, Goto T, Magariyama Y
(2006) Improvement in motion efficiency of
the spirochete Brachyspira pilosicoli in viscous
environments. Biophys J 90:3019–3026
21. Naresh R, Hampson DJ (2010) Attraction of
Brachyspira pilosicoli to mucin. Microbiology
156:191–197
148
Shuichi Nakamura
(0.1–0.2 μm) do not move on the cell body, i.e., staying at one
position on the cell body. The phenomena suggest that LPS can
freely move on the outer membrane and that the observed
beads’ movements are caused by drag force exerted on beads.
In other words, beads are retarded from the swimming cell by
viscous drag [2].
References
1. Cox PJ, Twigg GI (1974) Leptospiral motility.
Nature 250:260–261
2. Tahara H, Takabe K, Sasaki Y et al (2018) The
mechanism of two-phase motility in the spirochete Leptospira: swimming and crawling. Sci
Adv 4:eaar7975
3. Goldstein SF, Charon NW (1990) Multipleexposure photographic analysis of a motile spirochete. Proc Natl Acad Sci U S A
87:4895–4899
4. Nakamura S, Leshansky A, Magariyama Y,
Namba K, Kudo S (2014) Direct measurement
of helical cell motion of the spirochete Leptospira. Biophys J 106:47–54
5. Josenhans C, Suerbaum S (2002) The role of
motility as a virulence factor in bacteria. Int J
Med Microbiol 291:605–614
6. Lertsethtakarn P, Ottemann KM, Hendrixson
DR (2011) Motility and chemotaxis in Campylobacter and Helicobacter. Ann Rev Microbiol
65:389–410
7. Lambert A, Picardeau M, Haake DA et al
(2012) FlaA proteins in Leptospira interrogans
are essential for motility and virulence but are
not required for formation of the flagellum
sheath. Infect Immun 80:2019–2025
8. Wunder EA, Figueira CP, Benaroudj N et al
(2016) A novel flagellar sheath protein, FcpA,
determines filament coiling, translational
motility and virulence for the Leptospira spirochete. Mol Microbiol 101:457–470
9. Bromley DB, Charon NW (1979) Axial filament involvement in the motility of Leptospira
interrogans. J Bacteriol 137:1406–1412
10. Picardeau M, Brenot A, Saint Girons I (2001)
First evidence for gene replacement in Leptospira spp. inactivation of L. biflexa flaB results in
non-motile mutants deficient in endoflagella.
Mol Microbiol 40:189–199
11. Sasaki Y, Kawamoto A, Tahara H et al (2018)
Leptospiral flagellar sheath protein FcpA interacts with FlaA2 and FlaB1 in Leptospira biflexa.
PLoS One 13:e0194923
12. Wunder EA, Slamti L, Suwondo DN et al
(2018) FcpB is a surface filament protein of
the endoflagellum required for the motility of
the spirochete Leptospira. Front Cell Infect
Microbiol 8:130
13. Islam MS, Takabe K, Kudo S, Nakamura S
(2014) Analysis of the chemotactic behaviour
of Leptospira using microscopic agar-drop
assay. FEMS Microbiol Lett 356:39–44
14. Affroze S, Islam MS, Takabe K, Kudo S, Nakamura S (2016) Characterization of leptospiral
chemoreceptors using a microscopic agar drop
assay. Curr Microbiol 73:202–205
15. Takabe K, Tahara H, Islam MS, Affroze S,
Kudo S, Nakamura S (2017) Viscositydependent variations in the cell shape and
swimming manner of Leptospira. Microbiology
163:153–160
16. Takabe K, Kawamoto A, Tahara H, Kudo S,
Nakamura S (2017) Implications of coordinated cell-body rotations for Leptospira motility. Biochem Biophys Res Commun
491:1040–1046
17. Berg HC, Turner L (1979) Movement of
microorganisms in viscous environments.
Nature 278:349–351
18. Takabe K, Nakamura S, Ashihara M, Kudo S
(2013) Effect of osmolarity and viscosity on the
motility of pathogenic and saprophytic Leptospira. Microbiol Immunol 57:236–239
19. Magariyama Y, Kudo S (2002) A mathematical
explanation of an increase in bacterial swimming speed with viscosity in linear-polymer
solutions. Biophys J 83:733–739
20. Nakamura S, Adachi Y, Goto T, Magariyama Y
(2006) Improvement in motion efficiency of
the spirochete Brachyspira pilosicoli in viscous
environments. Biophys J 90:3019–3026
21. Naresh R, Hampson DJ (2010) Attraction of
Brachyspira pilosicoli to mucin. Microbiology
156:191–197
148
Shuichi Nakamura