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The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change.

Schelling P, Guglielmi KM, Kirchner E, Paetzold B, Dermody TS, Stehle T
J Biol Chem 282 11582-9 (2007)
Cited: 21 times
EuropePMC logo PMID: 17303562

Abstract

Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry.

Articles - 2oj5 mentioned but not cited (6)

  1. Structure of reovirus sigma1 in complex with its receptor junctional adhesion molecule-A. Kirchner E, Guglielmi KM, Strauss HM, Dermody TS, Stehle T. PLoS Pathog 4 e1000235 (2008)
  2. Structure-based mechanism of CMP-2-keto-3-deoxymanno-octulonic acid synthetase: convergent evolution of a sugar-activating enzyme with DNA/RNA polymerases. Heyes DJ, Levy C, Lafite P, Roberts IS, Goldrick M, Stachulski AV, Rossington SB, Stanford D, Rigby SE, Scrutton NS, Leys D. J Biol Chem 284 35514-35523 (2009)
  3. Structure and Sialyllactose Binding of the Carboxy-Terminal Head Domain of the Fibre from a Siadenovirus, Turkey Adenovirus 3. Singh AK, Berbís MÁ, Ballmann MZ, Kilcoyne M, Menéndez M, Nguyen TH, Joshi L, Cañada FJ, Jiménez-Barbero J, Benkő M, Harrach B, van Raaij MJ. PLoS One 10 e0139339 (2015)
  4. Structural Insights into Reovirus σ1 Interactions with Two Neutralizing Antibodies. Dietrich MH, Ogden KM, Katen SP, Reiss K, Sutherland DM, Carnahan RH, Goff M, Cooper T, Dermody TS, Stehle T. J Virol 91 e01621-16 (2017)
  5. An Unusual Aspartic Acid Cluster in the Reovirus Attachment Fiber σ1 Mediates Stability at Low pH and Preserves Trimeric Organization. Glorani G, Ruwolt M, Holton N, Loll B, Neu U. J Virol 96 e0033122 (2022)
  6. The Reovirus σ1 Attachment Protein Influences the Stability of Its Entry Intermediate. Garcia ML, Danthi P. J Virol 97 e0058523 (2023)


Reviews citing this publication (4)

  1. Virus-Receptor Interactions: The Key to Cellular Invasion. Maginnis MS. J Mol Biol 430 2590-2611 (2018)
  2. Survey of the year 2007 commercial optical biosensor literature. Rich RL, Myszka DG. J Mol Recognit 21 355-400 (2008)
  3. From touchdown to transcription: the reovirus cell entry pathway. Danthi P, Guglielmi KM, Kirchner E, Mainou B, Stehle T, Dermody TS. Curr Top Microbiol Immunol 343 91-119 (2010)
  4. Virus-associated disruption of mucosal epithelial tight junctions and its role in viral transmission and spread. Tugizov S. Tissue Barriers 9 1943274 (2021)

Articles citing this publication (11)

  1. Crystal structure of reovirus attachment protein σ1 in complex with sialylated oligosaccharides. Reiter DM, Frierson JM, Halvorson EE, Kobayashi T, Dermody TS, Stehle T. PLoS Pathog 7 e1002166 (2011)
  2. The GM2 glycan serves as a functional coreceptor for serotype 1 reovirus. Reiss K, Stencel JE, Liu Y, Blaum BS, Reiter DM, Feizi T, Dermody TS, Stehle T. PLoS Pathog 8 e1003078 (2012)
  3. Reovirus preferentially infects the basolateral surface and is released from the apical surface of polarized human respiratory epithelial cells. Excoffon KJ, Guglielmi KM, Wetzel JD, Gansemer ND, Campbell JA, Dermody TS, Zabner J. J Infect Dis 197 1189-1197 (2008)
  4. Isolation of reovirus T3D mutants capable of infecting human tumor cells independent of junction adhesion molecule-A. van den Wollenberg DJ, Dautzenberg IJ, van den Hengel SK, Cramer SJ, de Groot RJ, Hoeben RC. PLoS One 7 e48064 (2012)
  5. Utilization of sialylated glycans as coreceptors enhances the neurovirulence of serotype 3 reovirus. Frierson JM, Pruijssers AJ, Konopka JL, Reiter DM, Abel TW, Stehle T, Dermody TS. J Virol 86 13164-13173 (2012)
  6. Structure of Serotype 1 Reovirus Attachment Protein σ1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope. Stettner E, Dietrich MH, Reiss K, Dermody TS, Stehle T. J Virol 89 6136-6140 (2015)
  7. Optimum length and flexibility of reovirus attachment protein σ1 are required for efficient viral infection. Bokiej M, Ogden KM, Ikizler M, Reiter DM, Stehle T, Dermody TS. J Virol 86 10270-10280 (2012)
  8. Serotype-specific differences in inhibition of reovirus infectivity by human-milk glycans are determined by viral attachment protein σ1. Iskarpatyoti JA, Morse EA, McClung RP, Ikizler M, Wetzel JD, Contractor N, Dermody TS. Virology 433 489-497 (2012)
  9. A comparative molecular force spectroscopy study of homophilic JAM-A interactions and JAM-A interactions with reovirus attachment protein sigma1. Vedula SR, Lim TS, Kirchner E, Guglielmi KM, Dermody TS, Stehle T, Hunziker W, Lim CT. J Mol Recognit 21 210-216 (2008)
  10. Reovirus σ1 Conformational Flexibility Modulates the Efficiency of Host Cell Attachment. Diller JR, Halloran SR, Koehler M, Dos Santos Natividade R, Alsteens D, Stehle T, Dermody TS, Ogden KM. J Virol 94 e01163-20 (2020)
  11. The Orchestra of Reovirus Cell Entry. Mainou BA. Curr Clin Microbiol Rep 4 142-149 (2017)


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