SpoIVA contributes to efficient engulfment through a cytoskeletal-like mechanism during Bacillus subtilis sporulation
Abstract
During endospore (spore) development in bacteria, polar cell division generates two transcriptionally distinct cellular compartments, the mother cell and future spore (forespore).
Signalling between these cells leads to sequential and compartmentalized transcription, along with key morphogenetics events, including the phagocytic-like process of engulfment and the recruitment of coat proteins to the engulfing membrane. The SpoIVA ATPase is an essential sporulation protein that assembles into static filaments at the forespore surface during engulfment, where it functions as the basement layer for coat assembly. Here, using Bacillus subtilis, we reveal an additional role for SpoIVA during engulfment. Cytological analysis of a spoIVA null mutant (ΔspoIVA) revealed engulfment defects such as septal membrane bulges and asymmetric membrane migration, similar to those typically associated with impaired peptidoglycan remodelling during engulfment. Engulfment defects were exacerbated when ΔspoIVA was combined mutants known to impact engulfment progression and efficiency. Importantly, a spoIVA mutant (K30A) impaired for ATP hydrolysis and filament formation in vitro but partially functional for coat assembly in vivo, closely phenocopies the spoIVA null mutant engulfment defects. Based on these data, we propose a model whereby SpoIVA polymerisation at the spore surface, independently of coat assembly, plays a mechanical and structural role during engulfment, akin to the cytoskeletal proteins that drive phagocytosis in eukaryotic cells.
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BibTeX
@misc{fekade2026spoiva,
title = {{SpoIVA contributes to efficient engulfment through a cytoskeletal-like mechanism during Bacillus subtilis sporulation}},
author = {Betty Fekade and Siham Gabow and Kaitlyn Coleman and Saskia Bakker and Chris L B Graham and Cécile Morlot and Christopher D A Rodrigues},
howpublished = {HAL},
year = {2026},
month = jul,
doi = {10.64898/2026.07.08.736982},
url = {https://univ-grenoble-alpes.hal.science/hal-05798938v1},
note = {CC BY 4.0},
}
RIS
TY - UNPB
TI - SpoIVA contributes to efficient engulfment through a cytoskeletal-like mechanism during Bacillus subtilis sporulation
AU - Betty Fekade
AU - Siham Gabow
AU - Kaitlyn Coleman
AU - Saskia Bakker
AU - Chris L B Graham
AU - Cécile Morlot
AU - Christopher D A Rodrigues
PY - 2026
DA - 2026/07/08
PB - HAL
DO - 10.64898/2026.07.08.736982
UR - https://univ-grenoble-alpes.hal.science/hal-05798938v1
AB - During endospore (spore) development in bacteria, polar cell division generates two transcriptionally distinct cellular compartments, the mother cell and future spore (forespore). Signalling between these cells leads to sequential and compartmentalized transcription, along with key morphogenetics events, including the phagocytic-like process of engulfment and the recruitment of coat proteins to the engulfing membrane. The SpoIVA ATPase is an essential sporulation protein that assembles into static filaments at the forespore surface during engulfment, where it functions as the basement layer for coat assembly. Here, using Bacillus subtilis, we reveal an additional role for SpoIVA during engulfment. Cytological analysis of a spoIVA null mutant (ΔspoIVA) revealed engulfment defects such as septal membrane bulges and asymmetric membrane migration, similar to those typically associated with impaired peptidoglycan remodelling during engulfment. Engulfment defects were exacerbated when ΔspoIVA was combined mutants known to impact engulfment progression and efficiency. Importantly, a spoIVA mutant (K30A) impaired for ATP hydrolysis and filament formation in vitro but partially functional for coat assembly in vivo, closely phenocopies the spoIVA null mutant engulfment defects. Based on these data, we propose a model whereby SpoIVA polymerisation at the spore surface, independently of coat assembly, plays a mechanical and structural role during engulfment, akin to the cytoskeletal proteins that drive phagocytosis in eukaryotic cells.
ER -