Cross-protection Correlates with Delayed Antibody Formation to Challenge Virus after Immunization with Sindbis Virus

Smith-Owirodu, Althea; Wust, Carl J.; Gates, D. W.; Brown, Arthur

doi:10.1099/0022-1317-51-2-351

Cited by 4 publications

(3 citation statements)

References 29 publications

(4 reference statements)

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“…This is in accordance with previous investigations resulting in the present classification (KARABATSOS, 1975;STEC et al, 1986), although humoral crossprotection between members classified in one antigenic complex is described (e. g., SCHMALJOHN et al, 1982). Cell-mediated cross-protection between members of different complexes has been shown (SMITH- OWIRODU et al, 1980;WOLCOTT et al, 1982).…”

Section: Discussionsupporting

confidence: 93%

Studies on the Role of Linear Epitopes in Neutralization of Alphaviruses

Truyen

Kaaden

1990

Journal of Veterinary Medicine, Series B

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Summary By using three synthetic peptides (16–19 amino acids in length) representing different regions of glycoproteins E1 (peptide 3) and E2 (peptides 1 and 2) of Sindbis and Semliki Forest virus and isolated glycoprotein fractions of both viruses in reduced and non‐reduced form, the role of linear epitopes for the neutralization was investigated. The reaction patterns of sera induced by immunization with these antigens indicate that conformational epitopes do play the major role in neutralization of alphaviruses. Furthermore, no cross‐neutralization of these alphaviruses classified in different antigenic complexes within this genus was found. Zusammenfassung Untersuchungen zur Bedeutung linearer Epitope bei der Neutralisation von Alphaviren Mit Hilfe dreier synthetischer Peptide (16–19 Aminosäuren), die aus den Hüllproteinen gpE1 und gpE2 von Sindbis‐ und Semliki Forest‐Virus abgeleitet worden waren, wurde die Rolle linearer Epitope bei der antikörper‐vermittelten Neutralisation dieser Viren untersucht. Ergänzt wurden diese Versuche durch die Verwendung isolierter intakter Glykoproteine in reduzierter und nicht‐reduzierter Form. Die Reaktionsmuster der durch Verimpfung dieser Immunogene gewonnenen Kaninchenseren legen den Schluß nahe, daß den konformationsabhängigen Epitopen eine entscheidende Rolle bei der Neutralisation zukommt. Eine Kreuzneutralisation zwischen diesen beiden, in unterschiedlichen antigenen Komplexen klassifizierten Alphaviren wurde nicht nachgewiesen.

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Section: Discussionsupporting

confidence: 93%

Studies on the Role of Linear Epitopes in Neutralization of Alphaviruses

Truyen

Kaaden

1990

Journal of Veterinary Medicine, Series B

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“…These results lend additional support to our previously published evidence suggesting that viral proteins expressed by infected cells are immunologically distinct from virion proteins recognized in antibody-dependent cross-reactions between SIN and SF viruses (8,14,27,31). The existence of immunologically unique cell-membrane-associated viral antigens is supported by additional evidence from other laboratories working with alphaviruses, although the work has not involved cross-reactivity between distinct alphavirus subgroups.…”

Section: E1 E2supporting

confidence: 88%

Identification of immunologically cross-reactive proteins of Sindbis virus: evidence for unique conformation of E1 glycoprotein from infected cells

Wolcott¹,

Wust²,

Brown³

1984

J Virol

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Hyperimmune antisera to purified Sindbis (SIN) or Semliki Forest (SF) virus were used to identify alphavirus-specific and cross-reactive proteins in virions and infected cells. The hyperimmune sera participated in homologous and cross-cytolysis of alphavirus-infected cells, and the use of monospecific antisera to SIN structural proteins suggested that El and E2 could serve as target proteins in cytolysis. Proteins from purified virions or infected cells were extracted with Nonidet P-40, denatured by procedures for sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to nitrocellulose solid supports, and reacted with hyperimmune sera and '251-labeled protein A (immunoblotting on denatured proteins). Alternatively, native proteins extracted by mild Nonidet P-40 treatment were precipitated with hyperimmune sera before denaturation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After immunoblotting, homologous antiserum reacted with the virus structural proteins El, E2, capsid extracted from purified virions, and the counterparts of these proteins extracted from infected cells. In addition, PE2 and a 92,000-molecular-weight protein from infected cells reacted with homologous antiserum. These proteins were also immunoprecipitated with homologous antiserum. After immunoblotting. the Sindbis capsid protein was shown to be cross-reactive whether derived from purified virions or from infected cells; no cross-reactivity was observed with PE2 or E2 from either source. and the El glycoprotein was shown to be cross-reactive only when obtained from virions. However, the El glycoprotein could be crossimmunoprecipitated from infected cells (as well as from disrupted virions). and, in addition, capsid and a 92,000-molecular-weight protein were cross-immunoprecipitated from infected cells. These results suggest that a native conformation of the cell-associated El glycoproteins may be required for immunological crossreactivity (immune precipitation), whereas virion but not cell-associated El retains immunological crossreactivity after denaturation (immunoblot technique). The findings extend our previously published evidence which suggested that alphavirus maturation is accompanied by a change in immunological crossreactivity with respect to El.

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“…Anti-alphaviral IgG responses are well described as mediators of protection [ 5 , 7 , 46 , 81 ], with T cells perhaps playing a minor role [ 56 , 82 ]. The alphavirus cross-protection literature has traditionally implicated T cells [ 51 , 94 , 95 , 96 , 97 , 98 ], although antibody responses have also been implicated [ 42 , 50 ] and cross-reactive and cross-neutralizing antibodies are well described [ 43 , 44 , 45 , 99 ].…”

Section: Resultsmentioning

confidence: 99%

Arthritogenic Alphavirus Vaccines: Serogrouping Versus Cross-Protection in Mouse Models

et al. 2020

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Chikungunya virus (CHIKV), Ross River virus (RRV), o’nyong nyong virus (ONNV), Mayaro virus (MAYV) and Getah virus (GETV) represent arthritogenic alphaviruses belonging to the Semliki Forest virus antigenic complex. Antibodies raised against one of these viruses can cross-react with other serogroup members, suggesting that, for instance, a CHIKV vaccine (deemed commercially viable) might provide cross-protection against antigenically related alphaviruses. Herein we use human alphavirus isolates (including a new human RRV isolate) and wild-type mice to explore whether infection with one virus leads to cross-protection against viremia after challenge with other members of the antigenic complex. Persistently infected Rag1-/- mice were also used to assess the cross-protective capacity of convalescent CHIKV serum. We also assessed the ability of a recombinant poxvirus-based CHIKV vaccine and a commercially available formalin-fixed, whole-virus GETV vaccine to induce cross-protective responses. Although cross-protection and/or cross-reactivity were clearly evident, they were not universal and were often suboptimal. Even for the more closely related viruses (e.g., CHIKV and ONNV, or RRV and GETV), vaccine-mediated neutralization and/or protection against the intended homologous target was significantly more effective than cross-neutralization and/or cross-protection against the heterologous virus. Effective vaccine-mediated cross-protection would thus likely require a higher dose and/or more vaccinations, which is likely to be unattractive to regulators and vaccine manufacturers.

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Cross-protection Correlates with Delayed Antibody Formation to Challenge Virus after Immunization with Sindbis Virus

Cited by 4 publications

References 29 publications

Studies on the Role of Linear Epitopes in Neutralization of Alphaviruses

Studies on the Role of Linear Epitopes in Neutralization of Alphaviruses

Identification of immunologically cross-reactive proteins of Sindbis virus: evidence for unique conformation of E1 glycoprotein from infected cells

Arthritogenic Alphavirus Vaccines: Serogrouping Versus Cross-Protection in Mouse Models

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