Journal Article PUBDB-2026-01363

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Structural analyses uncover protease-adhesin interactions and c-di-GMP receptor regulation in sulfate-reducing bacteria

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2026
Springer Nature [London]

Nature Communications 17(1), 3564 () [10.1038/s41467-026-71936-5]
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Abstract: Desulfovibrio vulgaris is a sulfate-reducing organism with biofim-forming capacity relevant for bioremediation and microbe-induced corrosion. Biofilm formation of D. vulgaris depends on two large adhesins that are regulated by proteins encoded in the Dvh operon, which resembles the gammaproteobacterial Lap system in composition but differs in the sequence and domain organization of its regulatory proteins, DvhG and DvhD. We show that DvhG is a calcium-dependent protease that targets the periplasmic domains of both adhesins via extensive interactions. Additionally, structures of DvhD establish this HD-GYP domain-containing protein as a c-di-GMP-dependent switch with a periplasmic dCache domain. Our data support a model in which DvhD controls DvhG activity through a c-di-GMP-dependent mechanism that is molecularly distinct, but functionally analogous to LapD. Together, our results reveal how conserved regulatory logic can be implemented through distinct molecular architectures, highlighting the evolutionary flexibility of c-di-GMP signaling networks in controlling surface attachment across diverse bacterial lineages.

Classification:

Contributing Institute(s):
  1. Strukturelle Mikrobiologie CSSB (CSSB-DESY-HS)
Research Program(s):
  1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)
  2. DFG project G:(GEPRIS)564279481 - Die Typ-VI-Sekretionssysteme von Bacteroides und dessen spezifischen Mechanismen für den Transmembrantransport von Effektorproteinen mit unbekannter Funktion (564279481) (564279481)
Experiment(s):
  1. PETRA Beamline P11 (PETRA III)

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 Record created 2026-04-27, last modified 2026-04-28


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