Viral membrane fusion articles within Nature Communications

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  • Article
    | Open Access

    Membrane fusion is essential for cellular entry of enveloped viruses. Here, authors use time-resolved cryo-electron tomography and subtomogram averaging to capture 3D organization and population evolution of intermediates during membrane fusion of CHIKV, a medically important alphavirus.

    • Vidya Mangala Prasad
    • , Jelle S. Blijleven
    •  & Kelly K. Lee

  • Article
    | Open Access

    The mechanism of flavivirus activation for membrane fusion is not yet understood. Here, Vaney et al. describe how the viral pr protein, derived from an HSP40/DnaJ chaperonin, interacts with a pH sensing loop in the envelope protein E for fusogenic activation.

    • Marie-Christine Vaney
    • , Mariano Dellarole
    •  & Félix A. Rey

  • Article
    | Open Access

    Adeno-associated viruses can be secreted in a pre-lytic manner as free or extracellular vesicle (EV)-associated particles. Here, Elmore et al. show that the recently identified membrane-associated accessory protein (MAAP) functions as an AAV egress factor via association to EVs.

    • Zachary C. Elmore
    • , L. Patrick Havlik
    •  & Aravind Asokan

  • Article
    | Open Access

    The recently identified Wuhan spiny eel influenza virus (WSEIV) sequence is more closely related to influenza B than A viruses. Here, the authors functionally characterize the putative surface glycoproteins of WSEIV and show that its NA-like protein has sialidase activity and its HA-like protein binds monosialic ganglioside 2.

    • Guha Asthagiri Arunkumar
    • , Disha Bhavsar
    •  & Florian Krammer

  • Article
    | Open Access

    SARS-CoV-2 S protein prematurely refolds to the post-fusion conformation, compromising immunogenic properties and prefusion trimer yield. Here, Juraszek et al. present a stable SARS-CoV-2 S-closed protein variant with increased expression and correct folding, predominantly in closed prefusion conformation.

    • Jarek Juraszek
    • , Lucy Rutten
    •  & Johannes P. M. Langedijk

  • Article
    | Open Access

    The spike protein of coronaviruses (S-protein) is an envelope-anchored trimeric type I transmembrane glycoprotein that mediates receptor binding and the fusion of the viral and host cell membranes. Here the authors report the conformational states of HCoV-229E S trimer and observe the conformational changes in S1 subunit from closed state to activated state for receptor binding.

    • Xiyong Song
    • , Yuejun Shi
    •  & Guiqing Peng

  • Article
    | Open Access

    Herpesvirus virions have an outer lipid membrane dotted with glycoproteins that enable fusion with cell membranes to initiate entry and establish infection. Here the authors elucidate the structural mechanism of a neutralizing antibody derived from a patient infected by the herpesvirus varicella-zoster virus and targeted to its fusogen, glycoprotein-B.

    • Stefan L. Oliver
    • , Yi Xing
    •  & Ann M. Arvin

  • Article
    | Open Access

    HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic tail (CT), and show that the CT folds into membrane attached amphipathic helices that wrap around the TMD thereby forming a support baseplate for the rest of Env, and they also provide insights into the dynamic coupling across the TMD between the ectodomain and CT.

    • Alessandro Piai
    • , Qingshan Fu
    •  & James J. Chou

  • Article
    | Open Access

    Rabies virus (RABV) infection of unvaccinated individuals can be treated with post exposure prophylaxis. Here, Hellert et al. analyze the structure of a broadly neutralizing human antibody in complex with its target domain in the RABV glycoprotein and demonstrate that it blocks the acid-induced conformational change required for membrane fusion.

    • Jan Hellert
    • , Julian Buchrieser
    •  & Félix A. Rey

  • Article
    | Open Access

    The respiratory syncytial virus (RSV) F glycoprotein forms a trimeric complex and mediates viral entry. Using structures of RSV F in complex with antibodies, Gilman et al. here show a breathing motion of the prefusion conformation of F, resulting in transient opening of the trimeric complex in solution and on the cell surface.

    • Morgan S. A. Gilman
    • , Polina Furmanova-Hollenstein
    •  & Jason S. McLellan

  • Article
    | Open Access

    Here, the authors present the structure of the HIV envelope (Env) protein from a transmitted founder virus and show that, while the overall structure of the Env trimer is similar to other closed trimers, the fusion peptide is buried in the hydrophobic core of the trimer, which is similar to open state trimers.

    • Neeti Ananthaswamy
    • , Qianglin Fang
    •  & Venigalla B. Rao

  • Article
    | Open Access

    The fusion peptide (FP) of HIV envelope (Env) is critical in the cell entry process. Here, Kumar et al. present crystal structures of B41 SOSIP.664 Env trimer and show the dynamic nature of the FP and proximal region, which likely relates to conformational rearrangements required for membrane fusion.

    • Sonu Kumar
    • , Anita Sarkar
    •  & Ian A. Wilson

  • Article
    | Open Access

    Viral fusion proteins undergo extensive conformational changes during entry but intermediate conformations often remain unknown. Here, the authors show how Gn of Rift Valley fever virus fusion protein shields hydrophobic fusion loops of Gc and how these loops embed in the target membrane at acidic conditions.

    • Steinar Halldorsson
    • , Sai Li
    •  & Juha T. Huiskonen

  • Article
    | Open Access

    Coronaviruses have a relatively high mutation rate, potentially allowing fast adaptation to changing pressures. Here, Wong et al. provide the structure of the receptor-binding domain (RBD) of the human coronavirus HCoV-229E and its receptor and analyze the evolution of the RBD over the past 50 years.

    • Alan H. M. Wong
    • , Aidan C. A. Tomlinson
    •  & James M. Rini

  • Article
    | Open Access

    An efficient vaccine for human metapneumovirus (hMPV) will likely rely on neutralizing antibodies against the fusion protein (F). Here, the authors determine the crystal structure of pre-fusion-stabilized hMPV F and identify a dense glycan shield that affects generation of neutralizing antibodies.

    • Michael B. Battles
    • , Vicente Más
    •  & Jason S. McLellan

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