Notes: Specificity of anti-MHC Class II Antibody Binding to Synthetic Peptides

1989 ◽  
Vol 44 (9-10) ◽  
pp. 886-889
Author(s):  
Alberto Chersi ◽  
Teresa F. Romano ◽  
Emilio Ruocco
Keyword(s):  
Amino Acid ◽  
Mhc Class Ii ◽  
Sequence Homology ◽  
Synthetic Peptides ◽  
Class Ii ◽  
Amino Acid Sequences ◽  
Beta Chain ◽  
Small Peptides ◽  
Histocompatibility Antigens ◽  
High Sequence Homology

Abstract This study indicates that antibodies raised against a DR4 , w6; DQw 1,3 positive cell line may bind to synthetic peptides selected from the polymorphic amino acid se­quences 51 -59 and 63 -79 on the DQw 2 beta chain. This cross-reaction may be explained by the relatively high sequence homology of these sequences in the beta chains of class II histocompatibility antigens, and suggests that anti­ body binding to small peptides may be scarsely selective. Based on the observations of the reactivity of the anti­ bodies with several cell lines, and comparison of the amino acid sequences of beta chains of DR and DQ molecules, an attempt to identify the cross-reacting epitope is presented.

Molecular characterization of MHC class II DRA cDNA in Deoni cattle

2018 ◽  
Author(s):  
K. Swathi ◽  
M. Gnana Prakash ◽  
D. Sakaram ◽  
T. Raghunandan ◽  
A. Sarat Chandra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mhc Class Ii ◽  
Signal Peptide ◽  
Class Ii ◽  
Glycosylation Site ◽  
Amino Acid Sequences ◽  
Conserved Residues ◽  
A2 Domain

The present study was undertaken to clone and characterize DRA gene in Deoni cattle. The cDNA for the DRA gene was amplified by using specific primers designed based on available cattle sequences and purified products were cloned in competent E.coli (DH5á) strain. The full length 1013bp product of cDNA of DRA contained a single ORF of 762 nucleotides that coded for 253 amino acids translated product. Twenty four amino acids formed signal peptide while 229 constituted mature peptide. The deduced amino acid sequences resembled those of class II molecules of other species for all the conserved residues having critical functional role. But a single N-linked glycosylation site in á1 was observed in cattle and buffalo when compared to human and swine which contain a second site in á2 domain. The signal peptide was found more variable among the species compared. Comparison of nucleotide and amino acid sequences among related species and dendrogram constructed revealed that the cattle sequences are more similar to buffalo sequences.

Preparation and Isolation of Antibodies to Human MHC Class II alpha Chains by Aid of Synthetic Peptides

1989 ◽  
Vol 44 (9-10) ◽  
pp. 813-818
Author(s):  
Alberto Chersi ◽  
Teresa F. Romano ◽  
Francesco Chillemi
Keyword(s):  
Mhc Class Ii ◽  
Sequence Homology ◽  
Synthetic Peptides ◽  
Class Ii ◽  
Hla Class Ii ◽  
Human Cells ◽  
Hla Dq ◽  
Class Ii Alpha

Abstract Antibodies against HLA Class II alpha chains were prepared by using as immunogens synthetic peptides selected from the HLA -DQ 1 alpha chains sequence. Antibodies raised against peptide E2 , a 15-residue fragment of the polymorphic first domain, reacted preferentially with cells with the DQ 1 phenotype; however, despite the low sequence homology of this fragment with corresponding segments in DQw2 and DQw3 alpha chains, a partial crossreactivity with cells not expressing the DQw 1 specificity was detected. Antibodies to peptide H , selected from the monomorphic frame, might be specific for DO alloantigens, and presumably do not react with DR antigens. The two peptides, in addition, bind anti-Class II antibodies from the serum of a rabbit immunized with human cells, and appear to represent immunogenic linear determinants in the native glycoprotein molecule.

scholarly journals Induction of neonatal lupus in pups of mice immunized with synthetic peptides derived from amino acid sequences of the serotoninergic 5-HT4 receptor

2001 ◽  
Vol 31 (2) ◽  
pp. 573-579 ◽  
Author(s):  
Pierre Eftekhari ◽  
Jean-Christophe Roegel ◽  
Frank Lezoualc'h ◽  
Rodolphe Fischmeister ◽  
Jean-Louis Imbs ◽  
...  
Keyword(s):  
Amino Acid ◽  
Synthetic Peptides ◽  
Amino Acid Sequences ◽  
Neonatal Lupus

Notes: Partial Characterization of anti-H L A Class II Antibodies Isolated by Aid of Sepharose-Peptide Immunoadsorbents

1991 ◽  
Vol 46 (3-4) ◽  
pp. 321-324
Author(s):  
Alberto Chersi ◽  
Maria Cristina Morganti-Kossmann
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Membrane Proteins ◽  
Synthetic Peptides ◽  
Class Ii ◽  
Late Response ◽  
Early Immune Response ◽  
Hla Dq ◽  
Class Ii Antigens

Synthetic peptides selected from HLA-DQ and HLADP glycoproteins were coupled to Sepharose, and used for the isolation of anti-HLA Class II antibodies from the immune sera of rabbits immunized with human lymphoblastoid cells expressing Class II antigens. Antibodies from early and late bleedings displayed remarkable differences in affinity for peptides and for soluble membrane proteins: these differences might be due to an early immune response directed preferentially against surface linear determinants, and to a late response to assembled (discontinuous) sites. The possibility that such antibodies might be used for the identification of amino acid stretches involved in the formation of the same assembled determinant is considered.

scholarly journals Conformation of MHC class II I-Ag7 is sensitive to the P9 anchor amino acid in bound peptide

2007 ◽  
Vol 19 (9) ◽  
pp. 1103-1113 ◽  
Author(s):  
A. Gardiner ◽  
K. A. Richards ◽  
A. J. Sant ◽  
L. S. Arneson
Keyword(s):  
Amino Acid ◽  
Mhc Class Ii ◽  
Class Ii

MHC Class II Beta-Chain Expression in the Rainbow Trout

1992 ◽  
Vol 35 (6) ◽  
pp. 687-694 ◽  
Author(s):  
H. R. JUUL-MADSEN ◽  
J. GLAMANN ◽  
H. O. MADSEN ◽  
M. SIMONSEN
Keyword(s):  
Rainbow Trout ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Beta Chain

scholarly journals Correlation of structure with T cell responses of the three members of the HLA-DRw52 allelic series.

1989 ◽  
Vol 170 (3) ◽  
pp. 1027-1032 ◽  
Author(s):  
J Gorski ◽  
C Irle ◽  
E M Mickelson ◽  
M J Sheehy ◽  
A Termijtelen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Theoretical Model ◽  
T Cell ◽  
Gene Conversion ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Allelic Series ◽  
T Cell Clones ◽  
Cell Responses ◽  
Cell Clones

A third allele at the DRB3 locus, DRw52c, represents an intermediate sequence between DRw52a and DRw52b and may have arisen by a gene conversion-like event. The recognition of cells bearing these molecules by a number of alloreactive and antigen-specific DR-restricted T cell clones was analyzed. On the basis of a theoretical model of HLA class II structure, distinct amino acid clusters have been identified as motifs controlling TCR recognition. These are located both in the cleft and in the alpha-helical edge of the MHC class II recognition platform. Motifs shared between two alleles may restrict public T cell clones.

scholarly journals Phage Display Detection of Mimotopes that Are Shared Epitopes of Clinically and Epidemiologically Relevant Enterobacteria

2020 ◽  
Vol 8 (5) ◽  
pp. 780
Author(s):  
Armando Navarro ◽  
Delia Licona-Moreno ◽  
Alejandro Monsalvo-Reyes ◽  
Ulises Hernández-Chiñas ◽  
Carlos A. Eslava-Campos
Keyword(s):  
Amino Acid ◽  
Western Blot ◽  
Phage Display ◽  
Synthetic Peptides ◽  
Amino Acid Sequences ◽  
Serum Samples ◽  
E Coli ◽  
Peptide Mimotopes ◽  
Human Sera ◽  
Shared Epitopes

Background: Escherichia coli and Salmonella are etiologic agents of intestinal infections. A previous study showed the presence of shared epitopes between lipopolysaccharides (LPSs) of E. coli O157 and Salmonella. Aim: Using phage display, the aim of this study is to identify mimotopes of shared epitopes in different enterobacterial LPSs. Methods: We use anti-LPS IgG from E. coli O157 and Salmonella to select peptide mimotopes of the M13 phage. The amino acid sequence of the mimotopes is used to synthesize peptides, which are in turn used to immunize rabbits. The antibody response of the resulting sera against the LPSs and synthetic peptides (SPs) is analyzed by ELISA and by Western blot assays, indicating that LPS sites are recognized by the same antibody. In a complementary test, the reactions of human serum samples obtained from the general population against the SPs and LPSs are also analyzed. Results: From the last biopanning phase, sixty phagotopes are selected. The analysis of the peptide mimotope amino acid sequences shows that in 4 of them the S/N/A/PF motif is a common sequence. Antibodies from the sera of immunized rabbits with SP287/3, SP459/1, SP308/3, and SP073/14 react against both their own peptide and the different LPSs. The Western blot test shows a sera reaction against both the lateral chains and the cores of the LPSs. The analysis of the human sera shows a response against the SPs and LPSs. Conclusion: The designed synthetic peptides are mimotopes of LPS epitopes of Salmonella and E. coli that possess immunogenic capacity. These mimotopes could be considered for use in the design of vaccines against both enterobacteria.

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