Publications by authors named "Mark A Benhaim"
Article Synopsis
- Influenza hemagglutinin (HA) is crucial for the virus's entry as it helps with receptor binding and fusion of membranes, with clear structures observed at two stages: prefusion and postfusion.
- Research has started to uncover the intermediate stages of HA during the fusion process, which aids in understanding its activation and how it changes shape to complete fusion.
- This study utilized hydrogen-deuterium exchange mass spectrometry to compare HA subtypes H1 and H3, revealing distinct behaviors in their structural changes during fusion, especially when influenced by a particular antibody.
Article Synopsis
- The envelope glycoprotein (Env) is crucial for HIV's ability to evade the immune system and is highly variable among different strains of the virus.
- Research using hydrogen/deuterium-exchange mass spectrometry (HDX-MS) indicates that the dynamics and structural flexibility of Env differ significantly across various HIV isolates.
- These differences affect neutralization sensitivity, receptor activation, and the stability of the Env trimer, with certain mutations stabilizing some isolates but having minimal impact on others.
HIV-1 Env mediates viral entry into host cells and is the sole target for neutralizing antibodies. However, Env structure and organization in its native virion context has eluded detailed characterization. Here, we used cryo-electron tomography to analyze Env in mature and immature HIV-1 particles.
View Article and Find Full Text PDFProtein-mediated membrane fusion is a highly regulated biological process essential for cellular and organismal functions and infection by enveloped viruses. During viral entry the membrane fusion reaction is catalyzed by specialized protein machinery on the viral surface. These viral fusion proteins undergo a series of dramatic structural changes during membrane fusion where they engage, remodel, and ultimately fuse with the host membrane.
View Article and Find Full Text PDFMuch of our understanding of protein structure and mechanistic function has been derived from static high-resolution structures. As structural biology has continued to evolve it has become clear that high-resolution structures alone are unable to fully capture the mechanistic basis for protein structure and function in solution. Recently Hydrogen/Deuterium-exchange Mass Spectrometry (HDX-MS) has developed into a powerful and versatile tool for structural biologists that provides novel insights into protein structure and function.
View Article and Find Full Text PDFThe ability of naturally occurring proteins to change conformation in response to environmental changes is critical to biological function. Although there have been advances in the de novo design of stable proteins with a single, deep free-energy minimum, the design of conformational switches remains challenging. We present a general strategy to design pH-responsive protein conformational changes by precisely preorganizing histidine residues in buried hydrogen-bond networks.
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