Reconstitution of a biofilm adhesin system from a sulfate- reducing bacterium in Pseudomonas fluorescens
成果类型:
Article
署名作者:
Karbelkar, Amruta A.; Font, Maria; Smith, T. Jarrod; Sondermann, Holger; O'Toole, George A.
署名单位:
Dartmouth College; Helmholtz Association; Deutsches Elektronen-Synchrotron (DESY)
刊物名称:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN/ISSBN:
0027-9338
DOI:
10.1073/pnas.2320410121
发表日期:
2024-03-26
关键词:
desulfovibrio-vulgaris
protein
lapg
pf0-1
摘要:
Biofilms of sulfate- reducing bacterium (SRB) like Desulfovibrio vulgaris Hildenborough (DvH) can facilitate metal corrosion in various industrial and environmental settings leading to substantial economic losses. Although the mechanisms of biofilm formation by DvH are not yet well understood, recent studies indicate the large adhesin, DvhA, is a key determinant of biofilm formation. The dvhA gene neighborhood resembles the biofilm- regulating Lap system of Pseudomonas fluorescens but is curiously missing the c- di-GMP- binding regulator LapD. Instead, DvH encodes an evolutionarily unrelated c-di-GMP- binding protein (DVU1020) that we hypothesized is functionally analogous to LapD. To study this unusual Lap system and overcome experimental limitations with the slow- growing anaerobe DvH, we reconstituted its predicted SRB Lap system in a P. fluorescens strain lacking its native Lap regulatory components (Delta lapG Delta lapD). Our data support the model that DvhA is a cell surface-associated LapA-like adhesin with a N- terminal retention module and that DvhA is released from the cell surface upon cleavage by the LapG-like protease DvhG. Further, we demonstrate DVU1020 (named here DvhD) represents a distinct class of c- di- GMP- binding, biofilm- regulating proteins that regulates DvhG activity in response to intracellular levels of this second messenger. This study provides insight into the key players responsible for biofilm formation by DvH, thereby expanding our understanding of Lap - like systems.
来源URL: