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SDZ 35-682, a new picornavirus capsid-binding agent with potent antiviral activity.

Rosenwirth B, Oren DA, Arnold E, Kis ZL, Eggers HJ
Antiviral Res 26 65-82 (1995)
Cited: 13 times
EuropePMC logo PMID: 7741522

Abstract

SDZ 35-682 is a potent and selective inhibitor of the replication of members of the picornavirus group. It inhibits several rhinovirus serotypes and echovirus 9 at concentrations as low as 0.1 micrograms/ml, without exerting any effect on cell proliferation up to 30 micrograms/ml. As observed with other capsid-binding antipicornavirus compounds, there is a wide variation in sensitivity of the different serotypes within the rhinovirus group. The point of interference of SDZ 35-682 in a single cycle of virus growth is an early event taking place before 2 or 3 h of echo- or rhinovirus replication, respectively. By incorporation of neutral red into the viral capsid and measurement of acquisition of photoresistance it is shown that uncoating of echovirus 9 is inhibited by SDZ 35-682. In addition, efficiency of adsorption of echovirus 9 is reduced by SDZ 35-682. To demonstrate that SDZ 35-682, like other uncoating inhibitors of picornaviruses, binds to the hydrophobic pocket beneath the canyon floor co-crystallization with HRV 14 was performed. Considerable conformational changes occur in VP1 in the HRV 14/SDZ 35-682 complex. SDZ 35-682 is 19 A long from end to end and thus fills the entire hydrophobic pocket including its innermost end; it is less flexible than other long antiviral agents. It has been suggested that compounds filling the entire hydrophobic pocket will affect the uncoating process of the virion. Thus, inhibition of viral uncoating, as demonstrated with echovirus 9, probably is the predominant mode of action of SDZ 35-682.

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Articles - 1hrv mentioned but not cited (1)

  1. Anomalies in the refinement of isoleucine. Berntsen KR, Vriend G. Acta Crystallogr D Biol Crystallogr 70 1037-1049 (2014)


Reviews citing this publication (4)

  1. Selective inhibitors of picornavirus replication. De Palma AM, Vliegen I, De Clercq E, Neyts J. Med Res Rev 28 823-884 (2008)
  2. Perspectives for the treatment of infections with Flaviviridae. Leyssen P, De Clercq E, Neyts J. Clin Microbiol Rev 13 67-82, table of contents (2000)
  3. Selective human enterovirus and rhinovirus inhibitors: An overview of capsid-binding and protease-inhibiting molecules. Shih SR, Chen SJ, Hakimelahi GH, Liu HJ, Tseng CT, Shia KS. Med Res Rev 24 449-474 (2004)
  4. Rhinovirus Inhibitors: Including a New Target, the Viral RNA. Real-Hohn A, Blaas D. Viruses 13 1784 (2021)

Articles citing this publication (7)

  1. Suppression of feline coronavirus replication in vitro by cyclosporin A. Tanaka Y, Sato Y, Osawa S, Inoue M, Tanaka S, Sasaki T. Vet Res 43 41 (2012)
  2. Anti-rhinovirus activity of 3-methylthio-5-aryl-4-isothiazolecarbonitrile derivatives. Garozzo A, Cutrì CC, Castro A, Tempera G, Guerrera F, Sarvà MC, Geremia E. Antiviral Res 45 199-210 (2000)
  3. A novel benzonitrile analogue inhibits rhinovirus replication. Lacroix C, Querol-Audí J, Roche M, Franco D, Froeyen M, Guerra P, Terme T, Vanelle P, Verdaguer N, Neyts J, Leyssen P. J Antimicrob Chemother 69 2723-2732 (2014)
  4. Inhibition of fowlpox virus by an aqueous acetone extract from galls of Guiera senegalensis J. F. Gmel (Combretaceae). Lamien CE, Meda A, Mans J, Romito M, Nacoulma OG, Viljoen GJ. J Ethnopharmacol 96 249-253 (2005)
  5. Antiviral activity of WIN 54954 in coxsackievirus B2 carrier state infected human myocardial fibroblasts. Heim A, Pfetzing U, Müller G, Grumbach IM. Antiviral Res 37 47-56 (1998)
  6. Mutation in loop I of VP1 of Theiler's virus delays viral RNA release into cells and enhances antibody-mediated neutralization: a mechanism for the failure of persistence by the mutant virus. McCright IJ, Tsunoda I, Libbey JE, Fujinami RS. J Neurovirol 8 100-110 (2002)
  7. Equine Rhinitis A Virus Mutants with Altered Acid Resistance Unveil a Key Role of VP3 and Intrasubunit Interactions in the Control of the pH Stability of the Aphthovirus Capsid. Caridi F, Cañas-Arranz R, Vázquez-Calvo A, Sobrino F, Martín-Acebes MA. J Virol 90 9725-9732 (2016)


Related citations provided by authors (5)

  1. Structure Determination of Antiviral Compound Sch 38057 Complexed with Human Rhinovirus 14. Zhang A, Nanni RG, Li T, Arnold GF, Oren DA, Jacobo-Molina A, Williams RL, Kamer G, Rubenstein DA, Li Y, Rozhon E, Cox S, Buontempo P, O'Connell J, Schwartz J, Miller G, Bauer B, Versace R, Pinto P, Ganguly A, Girijavallabhan V, Arnold E J. Mol. Biol. 230 857- (1993)
  2. Three-Dimensional Structure-Activity Relationships for Antiviral Agents that Interact with Picornavirus Capsids. Zhang A, Nanni RG, Oren DA, Rozhon EJ, Arnold E Semin. Virol. 3 453- (1992)
  3. Analysis of the Structure of a Common Cold Virus, Human Rhinovirus 14, Refined at a Resolution of 3.0 Angstroms. Arnold E, Rossmann MG J. Mol. Biol. 211 763- (1990)
  4. The Use of Molecular-Replacement Phases for the Refinement of the Human Rhinovirus 14 Structure. Arnold E, Rossmann MG Acta Crystallogr., A, Found. Crystallogr. 44 270- (1988)
  5. Structure of a Human Common Cold Virus and Functional Relationship to Other Picornaviruses. Rossmann MG, Arnold E, Erickson JW, Frankenberger EA, Griffith JP, Hecht H-J, Johnson JE, Kamer G, Luo M, Mosser AG, Rueckert RR, Sherry B, Vriend G Nature 317 145- (1985)

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