Publications by authors named "Andree M Hubber"

Article Synopsis
  • Intracellular pathogens, like Legionella pneumophila, use effector proteins to manipulate host cell functions for infection.
  • These effectors are regulated in their function and are involved in the host's ubiquitin-proteasome system, which breaks down proteins.
  • The study focuses on how the effector LubX mimics a host protein to ensure the degradation of another effector, SidH, and describes methods to detect this process of polyubiquitination in both laboratory and living systems.*
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Tethering proteins play a key role in vesicular transport, ensuring that cargo arrives at a specific destination. The bacterial effector protein SidC and its paralog SdcA have been described as tethering factors encoded by the intracellular pathogen Legionella pneumophila. Here, we demonstrate that SidC proteins are important for early events unique to maturation of vacuoles containing Legionella and discover monoubiquitination of Rab1 as a new SidC-dependent activity.

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Rhizobial surface polysaccharides are required for nodule formation on the roots of at least some legumes but the mechanisms by which they act are yet to be determined. As a first step to investigate the function of exopolysaccharide (EPS) in the formation of determinate nodules, we isolated Mesorhizobium loti mutants affected in various steps of EPS biosynthesis and characterized their symbiotic phenotypes on two Lotus spp. The wild-type M.

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The Mesorhizobium loti R7A symbiosis island contains genes encoding a VirB/D4 type IV secretion system (T4SS) similar to that of Agrobacterium tumefaciens. This system has host-dependent effects on symbiosis that probably are due to translocation of two effector proteins, Msi059 and Msi061, into host cells. Here we report that, as in A.

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