Unusual molecular architecture of the machupo virus attachment glycoprotein by Bowden, T, Crispin, M, Graham, S, Harvey, D, Grimes, J, Jones, E, Stuart, D

“…New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. …”

Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies. by Bowden, T, Crispin, M, Jones, E, Stuart, D

“…The glycoproteins present on these viruses are responsible for mediating host cell attachment and fusion and are key targets for the design of antiviral entry inhibitors. …”

Molecular determinants of cellular attachment-mediated zoonosis of emerging paramyxo- and arenaviruses. by Pryce, R

“…The ability of a virus to specifically attach to cell-surface receptors during host-cell entry is a critical determinant of cross-species transmission. …”

Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly by Bowden, T, Crispin, M, Harvey, D, Jones, E, Stuart, D

“…These data reveal that henipaviral attachment glycoproteins undergo common structural transitions upon receptor binding and further define the structural template for antihenipaviral drug design. …”

Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2. by Bowden, T, Aricescu, A, Gilbert, R, Grimes, J, Jones, E, Stuart, D

“…Here we report crystal structures of both Nipah and Hendra attachment glycoproteins in complex with human EFNB2. …”

Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design by Bowden, T, Crispin, M, Harvey, D, Aricescu, A, Grimes, J, Jones, E, Stuart, D

“…Identification of ephrin-B2 and ephrin-B3 as cellular receptors for these viruses has enabled the development of immunotherapeutic reagents which prevent virus attachment and subsequent fusion. Here we present the structural analysis of the protein and carbohydrate components of the unbound viral attachment glycoprotein of NiV glycoprotein (NiV-G) at a 2.2-A resolution. …”

Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies (Biochemical Society Transactions (2010) 38, 5 (1349-1355)) by Bowden, T, Crispin, M, Jones, E, Stuart, D

Timing of galectin-1 exposure differentially modulates Nipah virus entry and syncytium formation in endothelial cells. by Garner, O, Yun, T, Pernet, O, Aguilar, H, Park, A, Bowden, T, Freiberg, A, Lee, B, Baum, L

“…However, galectins play multiple roles in regulating host-pathogen interactions; for example, galectins can promote attachment of HIV to T cells and macrophages and attachment of HSV-1 to keratinocytes but can also inhibit influenza entry into airway epithelial cells. …”

Toremifene interacts with and destabilizes the Ebola virus glycoprotein by Zhao, Y, Ren, J, Harlos, K, Jones, D, Zeltina, A, Bowden, T, Padilla-Parra, S, Fry, E, Stuart, D

“…EBOV has a membrane envelope decorated by trimers of a glycoprotein (GP, cleaved by furin to form GP1 and GP2 subunits), which is solely responsible for host cell attachment, endosomal entry and membrane fusion. GP is thus a primary target for the development of antiviral drugs. …”

Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission. by Crispin, M, Harvey, D, Bitto, D, Bonomelli, C, Edgeworth, M, Scrivens, J, Huiskonen, J, Bowden, T

“…In contrast, the protruding E2 attachment glycoprotein primarily contained conserved under-processed oligomannose-type structures when produced in both rodent and mosquito cell lines. …”

Toremifene interacts with and destabilizes the Ebola virus glycoprotein. by Zhao, Y, Ren, J, Harlos, K, Jones, D, Zeltina, A, Bowden, T, Padilla-Parra, S, Fry, E, Stuart, D

“…EBOV has a membrane envelope decorated by trimers of a glycoprotein (GP, cleaved by furin to form GP1 and GP2 subunits) which is solely responsible for host cell attachment, endosomal entry and membrane fusion. GP is thus a primary target for the development of antiviral drugs. …”

Uukuniemi Phlebovirus assembly and secretion leave a functional imprint on the virion glycome. by Crispin, M, Harvey, D, Bitto, D, Halldorsson, S, Bonomelli, C, Edgeworth, M, Scrivens, J, Huiskonen, J, Bowden, T

“…Both glycoproteins display poly-N-acetyllactosamines, consistent with virion assembly in the medial Golgi apparatus, whereas oligomannose-type glycans required for DC-SIGN-dependent cellular attachment are predominant on Gc. Local virion structure and the route of viral egress from the cell leave a functional imprint on the phleboviral glycome.…”

Native functionality and therapeutic targeting of arenaviral glycoproteins. by Crispin, M, Zeltina, A, Zitzmann, N, Bowden, T

“…Surface glycoproteins direct cellular targeting, attachment, and membrane fusion of arenaviruses and are the primary target for neutralizing antibodies. …”

Native functionality and therapeutic targeting of arenaviral glycoproteins by Crispin, M, Zeltina, A, Zitzmann, N, Bowden, T

“…Surface glycoproteins direct cellular targeting, attachment, and membrane fusion of arenaviruses and are the primary target for neutralising antibodies. …”

Responding to emerging viral pathogens: Characterization of neutralizing epitopes on the Nipah virus glycoproteins and the humoral immune response against SARS-CoV-2 by Avanzato, VA

“…Virion surface displayed viral glycoproteins mediate the critical processes of cellular attachment and membrane fusion that are required for infection. …”

Role of glycoproteins in virus-human cell interactions by Bowden, T, Fry, E

“…We illustrate this by providing examples from recent studies and show that clear differences exist between viruses which use individual glycoproteins for attachment and fusion, and those that use a single glycoprotein for both functions. …”

A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus by Stelfox, A, Bowden, T

“…The bat-borne paramyxovirus, Sosuga virus (SosV), is one of many paramyxoviruses recently identified and classified within the newly established genus Pararubulavirus, family Paramyxoviridae The envelope surface of SosV presents a receptor-binding protein (RBP), SosV-RBP, which facilitates host-cell attachment and entry. Unlike closely related hemagglutinin neuraminidase RBPs from other genera of the Paramyxoviridae, SosV-RBP and other pararubulavirus RBPs lack many of the stringently conserved residues required for sialic acid recognition and hydrolysis. …”

Structure of the Lassa virus glycan shield provides a model for immunological resistance by Watanabe, Y, Raghwani, j, Allen, J, Seabright, G, Li, S, Moser, F, Huiskonen, J, Strecker, T, Bowden, T, Crispin, M

“…Our analysis reveals the presence of underprocessed oligomannose-type glycans, which form punctuated clusters that obscure the proteinous surface of both the GP1 attachment and GP2 fusion glycoprotein subunits of the Lassa virus GPC. …”

A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex by Avanzato, V, Oguntuyo, K, Escalera-Zamudio, M, Gutierrez, B, Golden, M, Kosakovsky Pond, S, Pryce, R, Walter, T, Seow, J, Doores, K, Pybus, O, Munster, V, Lee, B, Bowden, T

“…The 2 glycoproteins displayed on the surface of the virus, NiV-G and NiV-F, mediate host-cell attachment and membrane fusion, respectively, and are targets of the host antibody response. …”

Conformational states and immunological targeting of the arenaviral glycoprotein complex: implications for therapeutic design by Ng, WM

“…The GP1 subunit of the envelope glycoprotein spike complex (GP) is responsible for receptor attachment during host cell entry. Here, I report the GP1 structure of OW Loei River virus (LORV) and the GP1 structures of NW Junín virus (JUNV) and NW Machupo virus (MACV) in complex with neutralising antibodies (nAbs). …”