Publications by authors named "Benjamin G Butt"

Article Synopsis
  • VPS4, an AAA-type ATPase, is recruited to viral assembly complexes in human cytomegalovirus infections to help with membrane constriction and fission, interacting with the viral protein pUL71.* -
  • A specific peptide motif within pUL71 is crucial for this interaction, predicted to bind to VPS4A similarly to how cellular ESCRT-III components interact.* -
  • This recruitment of VPS4A by pUL71 isn't essential for viral replication or morphogenesis, suggesting that its function remains unclear and highlighting a novel viral strategy that mimics cellular processes.*
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Myelin is a multilayered membrane that tightly wraps neuronal axons, enabling efficient, high-speed signal propagation. The axon and myelin sheath form tight contacts, mediated by specific plasma membrane proteins and lipids, and disruption of these contacts causes devastating demyelinating diseases. Using two cell-based models of demyelinating sphingolipidoses, we demonstrate that altered lipid metabolism changes the abundance of specific plasma membrane proteins.

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Article Synopsis
  • The HOPS complex plays a key role in the fusion of late endosomes and autophagosomes with lysosomes in eukaryotic cells, with specific regions of its components being crucial for proper assembly.
  • The study focuses on the C-terminal zinc finger domain of VPS39 to understand its role in protein interactions within the HOPS complex.
  • Researchers successfully expressed and purified VPS39's zinc-binding region, discovering it forms a non-native structure due to purification challenges, which could inform future protein design strategies.
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Herpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)-1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show that interaction between homologues of pUL7 and pUL51 is conserved across human herpesviruses, as is their association with -Golgi membranes.

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The substitution rates of viral polymerases have been studied extensively. However less is known about the tendency of these enzymes to 'slip' during RNA synthesis to produce progeny RNAs with nucleotide insertions or deletions. We recently described the functional utilization of programmed polymerase slippage in the family Potyviridae.

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