CCL

Összesen 5 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM065577
Első szerző:Gogolák Péter (biológus, immunológus)
Cím:Mapping of a Protective Helper T Cell Epitope of Human Influenza A Virus Hemagglutinin / Péter Gogolák, Ágnes Simon, Attila Horváth, Bence Réthi, István Simon, Katalin Berkics, Éva Rajnavölgyi, Gábor K. Tóth
Dátum:2000
ISSN:0006-291X
Megjegyzések:The synthetic peptide comprising the 317-341 region of human influenza A virus (H1N1 subtype) hemagglutinin elicits peptide-specific antibody and helper T cell responses and confers protection against lethal virus infection. Molecular mapping of the 317-329 region, which encompasses the epitope recognized by peptide-specific T cells, revealed that the minimal size required for T cell activation was the 317-326 segment. The most likely peptide alignment, which placed 320Leu to pocket 1 of the I-E(d) peptide binding groove, was predicted by molecular mechanics calculations performed with the parental and with the Ala-substituted analogs. In line with the prediction data, the results of the peptide binding assay, where the relative binding efficiency to I-E(d) molecules expressed on the surface of antigen-presenting cells was monitored, identified the 320-326 core sequence interacting with the major histocompatibility class II peptide binding groove. Functional analysis of Ala-substituted variants by functional assays and by calculating the surface-accessible areas of the single peptidic amino acids in the I-E(d)-peptide complexes demonstrated that 324Pro is a primary contact residue for the T cell receptor. Our results show that this type of analysis offers a suitable tool for molecular mapping of helper T cell epitopes and thus provides valuable data for subunit vaccine design.Copyright 2000 Academic Press.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications 270 : 1 (2000), p. 190-198. -
További szerzők:Simon Ágnes (1969-) (laboratóriumi szakorvos) Horváth Attila (orvos) Réthi Bence (1973-) (biológus, immunológus) Simon István Berkics Katalin Rajnavölgyi Éva (1950-) (immunológus) Tóth Gábor K.
Pályázati támogatás:T022540
OTKA
T030826
OTKA
T030566
OTKA
FKFP 0186/1999
Egyéb
AKP 98-13 3,3
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM065568
Első szerző:Rajnavölgyi Éva (immunológus)
Cím:A repetitive sequence of Epstein-Barr virus nuclear antigen 6 comprises overlapping T cell epitopes which induce HLA-DR-restricted CD4+ T lymphocytes / Éva Rajnavölgyi, Noémi Nagy, Britt Thuresson, Zsuzsa Dosztányi, Ágnes Simon, István Simon, Robert W. Karr, Ingemar Ernberg, Eva Klein, Kerstin I. Falk
Dátum:2000
ISSN:1460-2377
Megjegyzések:Most human adults carry the Epstein-Barr virus (EBV) and develop immunological memory against the structural and the virus-encoded cellular proteins. The EBV nuclear antigen 6 (EBNA6) elicits cytotoxic T cell responses and it also maintains a persistent antibody response. The majority of sera from EBV-seropositive individuals reacts with a synthetic peptide, p63, comprising 21 amino acids of a repetitive region of EBNA6. CD4(+) T lymphocytes, with specificity for p63, could be recalled from the T cell repertoire of EBV carriers that expressed certain HLA-DR allotypes which were identified as good binders of p63 by an in vitro flow cytometric assay. Analysis of the HLA-DR/p63 interaction by molecular mechanics calculations indicated the presence of multiple overlapping epitopes which were predicted to bind in a HLA-DRB1 allo- and subtype-specific manner. Specific activation of p63-selected long-term CD4(+) T cell cultures resulted in a proliferative response, in the production of IL-2 and in the secretion of high levels of tumor necrosis factor as measured by bioassays. Proliferation and cytokine production of p63-specific T cells could be induced by p63-loaded HLA-DR-matched antigen-presenting cells and by B cells co-expressing relevant HLA-DR molecules and EBNA6. Our results show that peptides of an EBNA6 repeat region induce CD4(+) T cells which can react with EBNA6-carrying cells in many individuals. We suggest that these T(h) cells may be important in conditioning dendritic cells for initiation potent virus-specific immune responses, provide help for EBV-specific B cells, drive IgG isotype switch and support the sustained effector function of memory cytotoxic T lymphocytes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
human CD4+ T lymphocyte
HLA-DR-peptide interaction
virus-specific interactions
Megjelenés:International Immunology. - 12 : 3 (2000), p. 281-293. -
További szerzők:Nagy Noémi, M. (1960-) (vegyész, angol szakfordító) Thuresson, Britt Dosztányi Zsuzsanna Simon Ágnes (1969-) (laboratóriumi szakorvos) Simon István Karr, Robert W. Ernberg, Ingemar Klein Éva Falk, Kerstin I.
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM065637
Első szerző:Simon Ágnes (laboratóriumi szakorvos)
Cím:Stabilization centers and protein stability / Á. Simon, Z. Dosztányi, C. Magyar, G. Szirtes, É. Rajnavölgyi, I. Simon
Dátum:2001
ISSN:1432-881X
Megjegyzések:The well-balanced stability of protein structures allows large-scale fluctuations, which are indispensable in many biochemical functions, ensures the long-term persistence of the equilibrium structure and it regulates the degradation of proteins to provide amino acids for biosynthesis. This balance is studied in the present work with two sets of proteins by analyzing stabilization centers, defined as certain clusters of residues involved in cooperative long-range interactions. One data set contains 56 proteins, which belong to 16 families of homologous proteins, derived from organisms of various physiological temperatures. The other set is composed of 31 major histocompatibility complex (MHC)?peptide complexes, which represent peptide transporters complexed with peptide ligands that apparently contribute to the stabilization of the MHC proteins themselves. We show here that stabilization centers, which had been identified as special clusters of residues that protect the protein structure, evolved to serve also as regulators of function ? related degradation of useless protein as part of protein housekeeping.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Protein thermostability
Major histocompatibility complex protein
Protein stability
Megjelenés:Theoretical Chemistry Accounts. - 106 : 1-2 (2001), p. 121-127. -
További szerzők:Dosztányi Zsuzsanna Magyar Csaba Szirtes G. Rajnavölgyi Éva (1950-) (immunológus) Simon István
Pályázati támogatás:T 017157
OTKA
T 030566
OTKA
FKFP 0186/199
Egyéb
AKP 98-13 3,3
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM065583
Első szerző:Simon Ágnes (laboratóriumi szakorvos)
Cím:Modeling MHC class II molecules and their bound peptides as expressed at the cell surface / Á. Simon, I. Simon, É. Rajnavölgyi
Dátum:2002
ISSN:0161-5890
Megjegyzések:A detailed insight to the structure of a given major histocompatibility complex (MHC)-peptide complex can strongly support and also improve the analysis of the peptide binding capabilities of the MHC molecule and the characterization of the developing T cell response. The number of MHC class II-peptide crystal structures is limited, therefore constructing and analyzing computer models can serve as efficient complementary tools when someone deals with experimentally determined binding and/or functional data. Commercial programs are available for modeling protein and protein-protein complexes, in general. However, more accurate results can be obtained if the parameters are directly optimized to a given complex, especially in the case of special proteins as MHC class II, an integral membrane protein, whose functional parts behave like regular globular proteins. Here, we present the optimization of an approach used for modeling MHC class II molecules complexed with various peptides fitting into the binding groove and several ways to analyze them with the help of experimental data.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
MHC class II
Molecular modeling
Energy minimization
MHC-peptide complex
Megjelenés:Molecular Immunology. - 38 : 9 (2002), p. 681-687. -
További szerzők:Simon István Rajnavölgyi Éva (1950-) (immunológus)
Pályázati támogatás:T30566
OTKA
T34131
OTKA
T 30826
OTKA
NKFP 0186/1999
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM065567
Első szerző:Simon Ágnes (laboratóriumi szakorvos)
Cím:Function-Related Regulation of the Stability of MHC Proteins / Á. Simon, Zs. Dosztányi, É. Rajnavölgyi, I. Simon
Dátum:2000
ISSN:0006-3495
Megjegyzések:Proteins must be stable to accomplish their biological function and to avoid enzymatic degradation. Constitutive proteolysis, however, is the main source of free amino acids used for de novo protein synthesis. In this paper the delicate balance of protein stability and degradability is discussed in the context of function of major histocompatibility complex (MHC) encoded protein. Classical MHC proteins are single-use peptide transporters that carry proteolytic degradation products to the cell surface for presenting them to T cells. These proteins fulfill their function as long as they bind their dissociable ligand, the peptide. Ligand-free MHC molecules on the cell surface are practically useless for their primary biological function, but may acquire novel activity or become an important source of amino acids when they lose their compact stable structure, which resists proteolytic attacks. We show in this paper that one or more of the stabilization centers responsible for the stability of MHC-peptide complexes is composed of residues of both the protein and the peptide, therefore missing in the ligand-free protein. This arrangement of stabilization centers provides a simple means of regulation; it makes the useful form of the protein stable, whereas the useless form of the same protein is unstable and therefore degradable.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 79 : 5 (2000), p. 2305-2313. -
További szerzők:Dosztányi Zsuzsanna Rajnavölgyi Éva (1950-) (immunológus) Simon István
Pályázati támogatás:T017157
OTKA
NKFP 0186/1999
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1