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TitleAsymmetric sheath coordination controls flagellar architecture and function in Leptospira spirochete.
Journal, issue, pagesEmbo J., Vol. 45, Page 2882-2904, Year 2026
Publish dateOct 18, 2025
AuthorsAkihiro Kawamoto / Toshiki Kuribayashi / Masatomo Morita / Shuichi Nakamura / Nobuo Koizumi /
PubMed AbstractBacterial flagella are essential for motility, but their structure and how they generate movement vary greatly. Most motile bacteria use external helical flagella, whereas spirochetes have ...Bacterial flagella are essential for motility, but their structure and how they generate movement vary greatly. Most motile bacteria use external helical flagella, whereas spirochetes have periplasmic flagella (PFs) that distort the cell body to drive forward movement. Here, we generated sheath protein knockout mutants and used high-resolution cryo-electron microscopy to elucidate the mechanisms underlying PF assembly, curvature, and rigidity in Leptospira biflexa. The PF consists of a FlaB1-based core filament surrounded asymmetrically by sheath proteins. Weak but essential binding of FlaA2 to the core enables asymmetric localization of the coiling protein FcpA. FcpA alone can induce curvature, whereas FcpB acts as a structural wedge that reinforces PF rigidity and enables efficient swimming in liquid. Specific glycosylation of FlaB1 mediates sheath-core interactions and may guide the assembly of sheath components. We propose that sheath proteins interact transiently with the core and may be anchored to the outer membrane, allowing core rotation beneath a static sheath. These findings reveal how cooperative interactions among sheath components confer structural and mechanical specialization to spirochete flagella.
External linksEmbo J. / PubMed:41844841 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.3 - 4.35 Å
Structure data

63347

9lry

EMDB-63347, PDB-9lry:
Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa
Method: EM (helical sym.) / Resolution: 2.3 Å

63348

9lrz

EMDB-63348, PDB-9lrz:
Core filament of the spirochete periplasmic flagella of Leptospira biflexa
Method: EM (helical sym.) / Resolution: 2.4 Å

63349

9ls0

EMDB-63349, PDB-9ls0:
Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa deleted fcpB strain
Method: EM (helical sym.) / Resolution: 2.4 Å

63350

9ls1

EMDB-63350, PDB-9ls1:
core filament of the spirochete periplasmic flagella of Leptospira biflexa deleted fcpB strain
Method: EM (helical sym.) / Resolution: 2.4 Å

66641

9x7k

EMDB-66641, PDB-9x7k:
core filament of the spirochete periplasmic flagella of Leptospira biflexa wild type
Method: EM (single particle) / Resolution: 4.35 Å

66642

9x7l

EMDB-66642, PDB-9x7l:
core filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain
Method: EM (single particle) / Resolution: 3.32 Å

66643

9x7m

EMDB-66643, PDB-9x7m:
core filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain
Method: EM (single particle) / Resolution: 3.2 Å

66646

9x7s

EMDB-66646, PDB-9x7s:
sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain
Method: EM (single particle) / Resolution: 2.83 Å

66647

9x7v

EMDB-66647, PDB-9x7v:
Sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain
Method: EM (single particle) / Resolution: 2.7 Å

66649

9x80

EMDB-66649, PDB-9x80:
sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type
Method: EM (single particle) / Resolution: 3.24 Å

Source
  • leptospira biflexa (bacteria)
KeywordsMOTOR PROTEIN / Filament / Flagellar motor

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