Epitope mapping of monoclonal antibodies against human immunodeficiency virus type 1 structural proteins by using peptides

Niedrig, M.; Hinkula, Jorma; Weigelt, Wolfgang; L’age-Stehr, Johanna; Pauli, Georg; Rosen, J; Wahrén, Britta

doi:10.1128/jvi.63.8.3525-3528.1989

Cited by 54 publications

(12 citation statements)

References 18 publications

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“…In HIV-1-CA-NTD, the presence of a relevant epitope within H4 (region 77-85, EAADWDRLH) has also been reported (Niedrig et al, 1989;Hinkula et al, 1990). Sequences containing this epitope have been used for HIV-1 diagnostic purposes Lottersberger et al, 2003Lottersberger et al, , 2004.…”

Section: Mapping Epitopes On Eiav-ca-ntdmentioning

confidence: 99%

Systematic epitope analysis of the p26 EIAV core protein

Soutullo

Santi

Perín

et al. 2007

J of Molecular Recognition

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The major core protein of equine infectious anemia virus (EIAV), p26, is one of the primary immunogenic structural proteins during a persistent infection of horses and is highly conserved among antigenically variants of viral isolates. In order to investigate its immune profile in more detail for a better diagnostic, an epitope mapping was carried out by means of two libraries of overlapping peptide fragments prepared by simultaneous and parallel SPPS on derivatized cellulose membranes (SPOT synthesis). Polyclonal equine sera from infected horses were used for the biological assay. Particularly two promising continuous epitopes (NAMRHL and MYACRD) were localized on the C-terminal extreme of p26, region 194-222. A cyclic synthetic fragment of 29 amino acid residues containing the identified epitopes was designed and studied. A significant conformational change towards a helical structure was observed when the peptide was cyclized by a bridge between Cys198 and Cys218. This observation correlated with an improvement of its ability to be recognized by specific antibodies in an EIA (Enzyme-linked Immunosorbent assay). These results suggest that the conformationally restricted synthetic antigen adequately mimics the native structure of this region of p26 core protein.

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Section: Mapping Epitopes On Eiav-ca-ntdmentioning

confidence: 99%

Systematic epitope analysis of the p26 EIAV core protein

Soutullo

Santi

Perín

et al. 2007

J of Molecular Recognition

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“…Short synlhetic pepiides of 10-30 residues usually coupled to protein carriers, have been successfully used bolh as immunogens [27] and as probes for antibody characterization [28][29][30]. It is feasible lo chemically synthesize long peptides or proleins of about 100 iiniino acids in Icnglh, These chemically synthesized proicins have been reported to bear sirong functional and structural similarities to ihe native moleeule [21,22.31].…”

Section: Results and Drscusslonmentioning

confidence: 99%

Fine Molecular Specificity of Linear and Assembled Antibody Binding Sites in HIV‐1 p24

Haaheim

Maskell²,

Mascagni³

et al. 1991

Scand J Immunol

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A set of seven murine monoclonal antibodies were generated against a chemically synthesized 11-kDa 104-mer peptide covering the C-terminal residues 270-373 of the p24 gag protein (HIV-1BRU strain). All monoclonal antibodies recognized HIV-1IIIB infected MOLT3 cells by fluorescence and gave positive Western blot signals with viral gag peptides (p55 and/or p24). Oligopeptide binding regions were located with competitive enzyme-linked immunosorbent assays. Detailed epitope scanning analyses (the Geysen technique) were performed by serological testing of the monoclonal antibodies against 99 overlapping hexapeptides which corresponded to the entire 104-mer region. The antibodies bound to p24 peptide sequences located within the 275-293 and 351-368 regions. One antibody (LH104-B) which reacted with residues 357-362 bound to p55 alone. In contrast, another antibody (LH104-I), which recognized the residues 358-363, i.e. with five out of six residues in common with antibody LH104-B for its epitope region, reacted exclusively with p24. At least two of the antibodies (LH104-C and -A) which bound to p24 alone, apparently recognized conformational epitopes. They gave positive reactions with the regions 288-293/351-356 and 284-289/351-356, respectively. This work shows that chemical synthesis of large peptides is a viable alternative approach to immunochemical studies of viral proteins.

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“…The definition of the antigenic structure of HIV-1 capsid proteins has been the subject of recent investigations [Coates et al, 1987;Ferns et al, 1987;Di Marzo-Veronese et al, 1985;Niedrig et al, 1988;Spence et al, 1989a, b;Niedrig et al, 1989, Tersmette et al, 1989Papsidero et al, 1989;Argos, 19891. Results described in this paper indicate the presence of a highly immunogenic domain on the carboxyterminal moiety of a recombinant p24 molecule (r-p39). Within the maximal extension so far determined for such a domain (amino acids 168-208), we mapped a minimal number of four distinct B cell epitopes, of which three clustered in a single dominant determinant.…”

Section: Discussionmentioning

confidence: 99%

“…Variation in biological properties between different isolates may in turn be related to the clinical course [Asjo et al, 1986;Cheng-Mayer et al, 1988;Tersmette et al, 19881. For both purposes, the aim of raising and characterizing MAbs directed to gag proteins has been recently pursued by many laboratories [Ferns et al, 1987;Di Marzo-Veronese et al, 1985;Niedrig et al, 1988Niedrig et al, ,1989Spence et al, 1989a;Tersmette et al, 19891. In the present work a recombinant p24 sequence was overexpressed in Escherichia coli and used as an immunogen to generate a panel of murine anti-p24 MAbs. The recognized B-cell epitopes were classified by crossinhibition assays and their localization was studied by analyzing MAb reactivity in Western blots against a set of deletion variants of p24.…”

Section: Introductionmentioning

confidence: 99%

Major antigenic domain recognized by monoclonal antibodies maps within the carboxy‐terminal moiety of a recombinant human immunodeficiency virus‐1 p24 protein

Gallina

Rossi

Mariani³

et al. 1990

Journal of Medical Virology

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Antigenicity in mice of a recombinant polypeptide including the complete amino acid sequence of mature human immunodeficiency virus type 1 p24 protein was studied by induction of monoclonal antibodies (MAbs). A panel of nine recloned hybridomas secreting MAbs with anti-p24 reactivity was isolated and further characterized. Competitive inhibition experiments suggested that the MAbs could be grouped into four epitopic classes corresponding to at least two distinct determinants. Analysis of reactivity to recombinant p24 deletion variants indicated that all the recognized epitopes are localized within a carboxy-terminal domain (amino acids 168-208) which should be largely exposed in recombinant as well as authentic antigen. Lack of response to N-terminal and central portions of p24 suggests that the antigenicity of those regions in the natural polypeptide is strongly conformation-dependent.

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Epitope mapping of monoclonal antibodies against human immunodeficiency virus type 1 structural proteins by using peptides

Cited by 54 publications

References 18 publications

Systematic epitope analysis of the p26 EIAV core protein

Systematic epitope analysis of the p26 EIAV core protein

Fine Molecular Specificity of Linear and Assembled Antibody Binding Sites in HIV‐1 p24

Major antigenic domain recognized by monoclonal antibodies maps within the carboxy‐terminal moiety of a recombinant human immunodeficiency virus‐1 p24 protein

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