Ma, H. et al. LDLRAD3 is a receptor for Venezuelan equine encephalitis virus. Nature 588, 308–314 (2020).
Weaver, S. C. & Barrett, A. D. T. Transmission cycles, host vary, evolution and emergence of arboviral illness. Nat. Rev. Microbiol. 2, 789–801 (2004).
Zaid, A. et al. Arthritogenic alphaviruses: epidemiological and scientific perspective on rising arboviruses. Lancet Infect. Dis. 21, e123–e133 (2021).
Marsh, M. & Helenius, A. Virus entry into animal cells. Adv. Virus Res. 36, 107–151 (1989).
Kielian, M., Chanel-Vos, C. & Liao, M. Alphavirus entry and membrane fusion. Viruses 2, 796–825 (2010).
Lescar, J. et al. The fusion glycoprotein shell of Semliki Forest virus: an icosahedral meeting primed for fusogenic activation at endosomal pH. Cell 105, 137–148 (2001).
Smith, T. J. et al. Putative receptor binding websites on alphaviruses as visualized by cryoelectron microscopy. Proc. Natl Acad. Sci. USA 92, 10648–10652 (1995).
Zhang, W., Heil, M., Kuhn, R. J. & Baker, T. S. Heparin binding websites on Ross River virus revealed by electron cryo-microscopy. Virology 332, 511–518 (2005).
Basore, Ok. et al. Cryo-EM construction of Chikungunya virus in complex with the Mxra8 receptor. Cell 177, 1725–1737 (2019).
Carleton, M., Lee, H., Mulvey, M. & Brown, D. T. Role of glycoprotein PE2 in formation and maturation of the Sindbis virus spike. J. Virol. 71, 1558–1566 (1997).
Mulvey, M. & Brown, D. T. Involvement of the molecular chaperone BiP in maturation of Sindbis virus envelope glycoproteins. J. Virol. 69, 1621–1627 (1995).
Heidner, H. W., Knott, T. A. & Johnston, R. E. Differential processing of Sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cells. J. Virol. 70, 2069–2073 (1996).
Leung, J. Y. S., Ng, M. M. L. & Chu, J. J. H. Replication of alphaviruses: a assessment on the entry course of of alphaviruses into cells. Adv. Virol. 2011, 249640 (2011).
Holland Cheng, R. et al. Nucleocapsid and glycoprotein group in an enveloped virus. Cell 80, 621–630 (1995).
Kostyuchenko, V. A. et al. The construction of Barmah Forest virus as revealed by cryo-electron microscopy at a 6-Angstrom decision has detailed transmembrane protein structure and interactions. J. Virol. 85, 9327–9333 (2011).
Paredes, A. M. et al. Three-dimensional construction of a membrane-containing virus. Proc. Natl Acad. Sci. USA 90, 9095–9099 (1993).
Tanaka, A. et al. Genome-wide screening uncovers the significance of N-sulfation of heparan sulfate as a bunch cell issue for Chikungunya virus an infection. J. Virol. 91, e00432-17 (2017).
Sanchez-Garcia, R. et al. DeepEMhancer: a deep studying answer for cryo-EM quantity put up-processing. Commun. Biol. 4, 1–8 (2021).
Mistry, J. et al. Pfam: the protein households database in 2021. Nucleic Acids Res. 49, D412–D419 (2021).
Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein constructions and complexes. Nucleic Acids Res. 46, W296–W303 (2018).
Zhang, R. et al. 4.Four Å cryo-EM construction of an enveloped alphavirus Venezuelan equine encephalitis virus. EMBO J. 30, 3854–3863 (2011).
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, Ok. Features and improvement of Coot. Acta Crystallogr. D 66, 486–501 (2010).
Afonine, P. V. et al. Towards automated crystallographic construction refinement with phenix.refine. Acta Crystallogr. D 68, 352–367 (2012).
Ryman, Ok. D. et al. Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses. J. Virol. 81, 3563–3573 (2007).
Gardner, C. L., Ebel, G. D., Ryman, Ok. D. & Klimstra, W. B. Heparan sulfate binding by pure japanese equine encephalitis viruses promotes neurovirulence. Proc. Natl Acad. Sci. USA 108, 16026–16031 (2011).
Porta, J. et al. Locking and blocking the viral panorama of an alphavirus with neutralizing antibodies. J. Virol. 88, 9616–9623 (2014).
Johnson, B. J. B., Brubaker, J. R., Roehrig, J. T. & Trent, D. W. Variants of Venezuelan equine encephalitis virus that resist neutralization outline a site of the E2 glycoprotein. Virology 177, 676–683 (1990).
Roehrig, J. T., Hunt, A. R., Kinney, R. M. & Mathews, J. H. In vitro mechanisms of monoclonal antibody neutralization of alphaviruses. Virology 165, 66–73 (1988).
Song, H. et al. Molecular foundation of arthritogenic alphavirus receptor MXRA8 binding to Chikungunya virus envelope protein. Cell 177, 1714–1724 (2019).
Zhang, R. et al. Mxra8 is a receptor for a number of arthritogenic alphaviruses. Nature 557, 570–574 (2018).
Nikolic, J. et al. Structural foundation for the recognition of LDL-receptor members of the family by VSV glycoprotein. Nat. Commun. 9, 1029 (2018).
Verdaguer, N., Fita, I., Reithmayer, M., Moser, R. & Blaas, D. X-ray construction of a minor group human rhinovirus sure to a fraction of its mobile receptor protein. Nat. Struct. Mol. Biol. 11, 429–434 (2004).
Ko, S. Y. et al. A virus-like particle vaccine prevents equine encephalitis virus an infection in nonhuman primates. Sci. Transl. Med. 11, eaav3113 (2019).
Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced movement for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).
Zhang, Ok. Gctf: actual-time CTF dedication and correction. J. Struct. Biol. 193, 1–12 (2016).
Wagner, T. et al. SPHIRE-crYOLO is a quick and correct absolutely automated particle picker for cryo-EM. Commun. Biol. 2, 218 (2019).
Zivanov, J. et al. New instruments for automated excessive-decision cryo-EM construction dedication in RELION-3. eLife 7, e42166 (2018).
Pettersen, E. F. et al. UCSF ChimeraX: construction visualization for researchers, educators, and builders. Protein Sci. 30, 70–82 (2021).
Fass, D., Blacklow, S., Kim, P. S. & Berger, J. M. Molecular foundation of familial hypercholesterolaemia from construction of LDL receptor module. Nature 388, 691–693 (1997).
Henikoff, S. & Henikoff, J. G. Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA 89, 10915–10919 (1992).
Roehrig, J. T. & Mathews, J. H. The neutralization web site on the E2 glycoprotein of Venezuelan equine encephalomyelitis (TC-83) virus consists of a number of conformationally steady epitopes. Virology 142, 347–356 (1985).