Recognition of Synthetic Peptides with Sequences of Rubella Virus E1 Polypeptide by Antibodies and T Lymphocytes

Ilonen, Jorma; Seppänen, H; Närvänen, Ale; Korkolainen, Mirja; Salmi, A.

doi:10.1089/vim.1992.5.221

Cited by 13 publications

(3 citation statements)

References 20 publications

(23 reference statements)

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“…We identified and further characterized three major T helper cell epitopes in RVE1 glycoprotein. Both fusion proteins and synthetic peptides have been applied to this kind of study [13][14][15][16]. Lovett and coworkers detected PBMC responses to a fusion protein covering aa 162-332 in 17 (41%) of 41 studied seropositive donors.…”

Section: Discussionmentioning

confidence: 99%

Definition of three minimal T helper cell epitopes of rubella virus E1 glycoprotein

Marttila

Ilonen

Lehtinen

et al. 1996

Clinical and Experimental Immunology

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SUMMARYTo characterize T cell-recognized epitopes on rubella virus (RV) E1 glycoprotein, IL-2-dependent RVspecific T cell lines were established from 14 rubella-seropositive healthy donors. The responses of these lines were studied by using a panel of 94 partially overlapping synthetic peptides of 15 amino acids (aa) length covering the known nucleotide sequence of RVE1 glycoprotein. Two to seven peptidedefined epitopes were recognized by the T cell lines, but a large interindividual variation was found. T cell reactivity was most often localized to the regions between aa 276 and 290, aa 381 and 395 and aa 410 and 420. Analysis of overlapping, truncated peptides revealed three minimal T helper cell epitopes VIGSQARK, KFVTAALLN and RVIDPAAQ in aa positions 280-287, 385-393 and 412-419, respectively.

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Section: Discussionmentioning

confidence: 99%

Definition of three minimal T helper cell epitopes of rubella virus E1 glycoprotein

Marttila

Ilonen

Lehtinen

et al. 1996

Clinical and Experimental Immunology

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“…Monoclonal antibodies (MAbs) were used to define the neutralizing domains on the E1 glycoprotein whose amino acid sequences were determined by overlapping synthetic peptides (9,11,12,14,21,22,24). One of these domains was defined by three independent MAbs that recognized the same sequence, represented by the synthetic peptide SP15 (E1 amino acids 208 to 239) (4, 25).…”

Section: Rubella Virus (Rv) Is the Etiologic Agent Of German Measlesmentioning

confidence: 99%

Evaluation of Antibodies against a Rubella Virus Neutralizing Domain for Determination of Immune Status

Córdoba

Lanoel

Grutadauria

et al. 2000

Clin Diagn Lab Immunol

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The protective immune responses against rubella virus (RV) are related to its neutralizing epitopes, an issue that is important to consider when assessing the immune status of patients with remote infection. In the present paper, we compare the antibodies detected by a synthetic-peptide-based enzyme immunoassay (EIA) with antibodies detected by the traditional technique of hemagglutination inhibition (HIA) in patients with remote RV infection. The synthetic peptide used as an antigen (SP15) represents a neutralizing epitope that corresponds to amino acids 208 to 239 of the E1 glycoprotein. The SP15-EIA was developed, all variables that affected the assay were standardized, and the test was validated using reference sera. Serum samples (n ‫؍‬ 129) from patients with remote RV infection were tested by HIA and SP15-EIA. Discrepant sera were assayed by MEIA (IMX/Abbot). The comparison between HIA and SP15-EIA, taking HIA as the standard methodology for determining immune status, showed that SP15-EIA is very specific and sensitive for detecting protecting antibodies (specificity, 100%; sensitivity, 98.20%). This study demonstrates that antibodies against the neutralizing domain represented by SP15 would be important in the memory response after natural infection and may be a good tool in the determination of the true immune status of patients with remote infection with regard to RV. Rubella virus (RV) is the etiologic agent of German measlesand is the sole member of the genus Rubivirus in the Togaviridae family. During the first trimester of pregnancy, the infection may induce congenital malformations and viral persistence in the human fetus (26).The RV virion contains an RNA genome enclosed in an icosahedral capsid composed of protein C (33 kDa). Surrounding this nucleocapsid is a lipid bilayer, in which viral glycoproteins E1 (58 kDa) and E2 (42 to 47 kDa) are embedded (18). The humoral immune response to RV is predominantly to the E1 glycoprotein and persists indefinitely after infection (13,17).The E1 glycoprotein has been suggested to be the immunodominant antigen, since most virus-neutralizing antibodies are directed against this subunit. Monoclonal antibodies (MAbs) were used to define the neutralizing domains on the E1 glycoprotein whose amino acid sequences were determined by overlapping synthetic peptides (9,11,12,14,21,22,24). One of these domains was defined by three independent MAbs that recognized the same sequence, represented by the synthetic peptide SP15 (E1 amino acids 208 to 239) (4, 25). Moreover, SP15 was shown to induce polyvalent antibodies with neutralizing and hemagglutination inhibition activity in mice and rabbits. The sequence of SP15 is present in several strains of RV, such as Therien, Judith, M33, HPV77, RA27/3, Gilchrist, wildtype Cordoba, and Kara 95 (5, 25).Other authors using a similar synthetic peptide, BCH-178C (E1 amino acids 213 to 239), showed the existence of human antibodies that recognize this domain (15,16,27). These authors indicate that BCH-178C can favorably replace curr...

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“…Both E1 and E2 provide life-long immunity, but the E1 glycoprotein is the major outward projecting structure and contains epitopes recognized by neutralizing and hemagglutinating inhibition antibodies, properties that make this protein a major candidate for a subunit or synthetic vaccine (5,6,(14)(15)(16). Many investigators have reported several sequences of amino acids of E1 with the ability to induce neutralizing antibodies (7,8,16). Overlapping synthetic peptides have permitted successful identification of neutralization domains.…”

mentioning

confidence: 99%

Presence of a neutralizing domain in isolates of rubella virus in Cordoba, Argentina

Córdoba

Grutadauria

Cuffini

et al. 1997

Clin Diagn Lab Immunol

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We studied the presence of a neutralizing epitope of rubella virus (RV) in locally circulating strains in Cordoba, Argentina, using binding by the monoclonal antibody (MAb) H3. This epitope is contained in a sequence of the E1 glycoprotein (E1 208-239) represented by the synthetic peptide SP15. H3 MAb showed specific binding to SP15 by enzyme-linked immunosorbent assay (ELISA). One wild-type postnatal isolate, four clones derived from this isolate, and one congenital isolate were reactive with H3 by ELISA. These results suggest that the region of RV represented by SP15 is a domain present in locally circulating strains.

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Recognition of Synthetic Peptides with Sequences of Rubella Virus E1 Polypeptide by Antibodies and T Lymphocytes

Cited by 13 publications

References 20 publications

Definition of three minimal T helper cell epitopes of rubella virus E1 glycoprotein

Definition of three minimal T helper cell epitopes of rubella virus E1 glycoprotein

Evaluation of Antibodies against a Rubella Virus Neutralizing Domain for Determination of Immune Status

Presence of a neutralizing domain in isolates of rubella virus in Cordoba, Argentina

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