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Titolo:
The molecular basis of virus crossreactivity and neutralisation after immunisation with optimised chimeric peptides mimicking a putative helical epitope of the measles virus hemagglutinin protein
Autore:
El Kasmi, KC; Theisen, D; Brons, NHC; Muller, CP;
Indirizzi:
Lab Natl Sante, L-1011 Luxembourg, Luxembourg Lab Natl Sante Luxembourg Luxembourg L-1011 -1011 Luxembourg, Luxembourg Univ Tubingen, Fak Med, D-72076 Tubingen, Germany Univ Tubingen TubingenGermany D-72076 ak Med, D-72076 Tubingen, Germany
Titolo Testata:
MOLECULAR IMMUNOLOGY
fascicolo: 14-15, volume: 35, anno: 1998,
pagine: 905 - 918
SICI:
0161-5890(199810)35:14-15<905:TMBOVC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
B-CELL EPITOPES; SEMLIKI FOREST VIRUS; HELPER T-CELLS; FUSION PROTEIN; MONOCLONAL-ANTIBODIES; SYNTHETIC PEPTIDES; IMMUNE-RESPONSE; IMMUNOGENICITY; VACCINE; DETERMINANTS;
Keywords:
measles virus; neutralisation; B cell epitope; T cell epitope; synthetic peptides;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Muller, CP Lab Natl Sante, POB 1102, L-1011 Luxembourg, Luxembourg Lab Natl Sante POB 1102 Luxembourg Luxembourg L-1011 uxembourg
Citazione:
K.C. El Kasmi et al., "The molecular basis of virus crossreactivity and neutralisation after immunisation with optimised chimeric peptides mimicking a putative helical epitope of the measles virus hemagglutinin protein", MOL IMMUNOL, 35(14-15), 1998, pp. 905-918

Abstract

The loop comprising aminoacids H236-256, connects two strands of sheet 1 of the propeller-like hemagglutinin (H) protein of the measles virus (MV) and contains a putative active site residue (R-253), a residue implicated in CD46-downregulation (R-243) and the minimal epitope E245L-QL(249) of the neutralising and protective monoclonal antibody BH129. The objective of this study was to design synthetic peptides which induce neutralising antibodiesagainst this important functional domain. Peptide-design was based on the colinear synthesis of this sequential B cell epitope (BCE) with different Tcell epitopes (TCE). Chimeric constructs were systematically optimised with respect to length and copy number of the BCE and the nature and orientation of the TCE. Surprisingly, the induction of MV-crossreactive antibodies did not correlate with the antigenicity of the peptides. The best MV-crossreactive antibodies were obtained with TB oriented constructs containing TCEsof the MV fusion (F) protein and the BCE H236-250 (TB15mer) or H236-255 (TB20mer). In vitro virus-neutralising sera were obtained solely with the latter construct. A glycine scan showed that binding to MV depended on a defined pattern of contact residues compatible with the putative alpha helical nature of this epitope. The contact residues of the neutralising serum (S244EL-QL(249)) differed from those of the non-neutralising serum (S244EL246) but no unique differences in the immunoglobulin subclasses were detected. Surface plasmon resonance measurements detected a higher affinity for the neutralising serum compared to the TB15mer serum. These results emphasize the need of an optimal design of immunogenic peptides which cannot always be guided by the antigenicity of the peptide constructs. This study demonstratesthat neutralising antibodies can be generated with peptides mimicking thishelical epitope, provided that the critical contact residues are recognized with high affinity and underlines the potential of the epitope as an element of a future subunit vaccine. (C) 1998 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 03:45:56