Eintrag weiter verarbeiten
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that re...
Gespeichert in:
Zeitschriftentitel: | The Journal of experimental medicine |
---|---|
Personen und Körperschaften: | , , , , |
In: | The Journal of experimental medicine, 180, 1994, 5, S. 1873-1888 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Rockefeller University Press
|
Schlagwörter: |
author_facet |
Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C |
---|---|
author |
Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C |
spellingShingle |
Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C The Journal of experimental medicine Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. Immunology Immunology and Allergy |
author_sort |
johansson, p j |
spelling |
Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C 0022-1007 1540-9538 Rockefeller University Press Immunology Immunology and Allergy http://dx.doi.org/10.1084/jem.180.5.1873 <jats:p>Human immunoglobulin M (IgM) rheumatoid factors (RFs) show primary direct enzyme-linked immunosorbent assay (ELISA) reactivity with Fab rather than Fc fragments of monoclonal antibody (mAb) II-481 directed against the Fc gamma-binding site of herpes simplex virus glycoprotein gE. This preferential anti-Fab specificity suggests that RFs react with antigen-binding portions of mAb II-481 as anti-idiotypic antibodies directed at the combining site regions of mAb reacting with the Fc gamma-binding region of gE. Analysis of this idiotype-anti-idiotype reaction employed polymerase chain reaction amplification and sequencing of the variable heavy and light (VH and VL) regions of mAb II-481. When VH and VL regions of mAb II-481 were synthesized as overlapping 7-mer peptides on polypropylene pins, a panel of 10 polyclonal and 6 monoclonal human IgM RFs reacted primarily with epitopes within the three solvent-exposed mAb II-481 complementarity determining regions (CDRs). Preincubation of single CDR heptamer peptides with IgM RFs in free solution, resulted in 63-100% inhibition of RF binding to mAb II-481 on the ELISA plate, confirming the antigenic importance of linear CDR regions for RF reactivity. Combinations of two or three CDR peptides frequently produced 94-100% inhibition of RF binding to whole mAb II-481. Control peptides, singly or in combination, showed no inhibition. Computer modeling suggested that the RF-reactive mAb II-481 Fv region and a previously demonstrated RF-reactive CH3 epitope displayed considerable three-dimensional similarities in conformation. These studies may provide insight into limited shape homologies possibly involved in an RF anti-idiotypic reaction.</jats:p> Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. The Journal of experimental medicine |
doi_str_mv |
10.1084/jem.180.5.1873 |
facet_avail |
Online Free |
finc_class_facet |
Medizin |
format |
ElectronicArticle |
fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA4NC9qZW0uMTgwLjUuMTg3Mw |
id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA4NC9qZW0uMTgwLjUuMTg3Mw |
institution |
DE-Pl11 DE-Rs1 DE-14 DE-105 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Zi4 DE-Gla1 DE-15 |
imprint |
Rockefeller University Press, 1994 |
imprint_str_mv |
Rockefeller University Press, 1994 |
issn |
0022-1007 1540-9538 |
issn_str_mv |
0022-1007 1540-9538 |
language |
English |
mega_collection |
Rockefeller University Press (CrossRef) |
match_str |
johansson1994fvstructureofmonoclonalantibodyii481againstherpessimplexvirusfcgammabindingglycoproteingecontainsimmunodominantcomplementaritydeterminingregionepitopesthatreactwithhumanimmunoglobulinmrheumatoidfactors |
publishDateSort |
1994 |
publisher |
Rockefeller University Press |
recordtype |
ai |
record_format |
ai |
series |
The Journal of experimental medicine |
source_id |
49 |
title |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_unstemmed |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_full |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_fullStr |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_full_unstemmed |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_short |
Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_sort |
fv structure of monoclonal antibody ii-481 against herpes simplex virus fc gamma-binding glycoprotein ge contains immunodominant complementarity determining region epitopes that react with human immunoglobulin m rheumatoid factors. |
topic |
Immunology Immunology and Allergy |
url |
http://dx.doi.org/10.1084/jem.180.5.1873 |
publishDate |
1994 |
physical |
1873-1888 |
description |
<jats:p>Human immunoglobulin M (IgM) rheumatoid factors (RFs) show primary direct enzyme-linked immunosorbent assay (ELISA) reactivity with Fab rather than Fc fragments of monoclonal antibody (mAb) II-481 directed against the Fc gamma-binding site of herpes simplex virus glycoprotein gE. This preferential anti-Fab specificity suggests that RFs react with antigen-binding portions of mAb II-481 as anti-idiotypic antibodies directed at the combining site regions of mAb reacting with the Fc gamma-binding region of gE. Analysis of this idiotype-anti-idiotype reaction employed polymerase chain reaction amplification and sequencing of the variable heavy and light (VH and VL) regions of mAb II-481. When VH and VL regions of mAb II-481 were synthesized as overlapping 7-mer peptides on polypropylene pins, a panel of 10 polyclonal and 6 monoclonal human IgM RFs reacted primarily with epitopes within the three solvent-exposed mAb II-481 complementarity determining regions (CDRs). Preincubation of single CDR heptamer peptides with IgM RFs in free solution, resulted in 63-100% inhibition of RF binding to mAb II-481 on the ELISA plate, confirming the antigenic importance of linear CDR regions for RF reactivity. Combinations of two or three CDR peptides frequently produced 94-100% inhibition of RF binding to whole mAb II-481. Control peptides, singly or in combination, showed no inhibition. Computer modeling suggested that the RF-reactive mAb II-481 Fv region and a previously demonstrated RF-reactive CH3 epitope displayed considerable three-dimensional similarities in conformation. These studies may provide insight into limited shape homologies possibly involved in an RF anti-idiotypic reaction.</jats:p> |
container_issue |
5 |
container_start_page |
1873 |
container_title |
The Journal of experimental medicine |
container_volume |
180 |
format_de105 |
Article, E-Article |
format_de14 |
Article, E-Article |
format_de15 |
Article, E-Article |
format_de520 |
Article, E-Article |
format_de540 |
Article, E-Article |
format_dech1 |
Article, E-Article |
format_ded117 |
Article, E-Article |
format_degla1 |
E-Article |
format_del152 |
Buch |
format_del189 |
Article, E-Article |
format_dezi4 |
Article |
format_dezwi2 |
Article, E-Article |
format_finc |
Article, E-Article |
format_nrw |
Article, E-Article |
_version_ |
1792339190307880969 |
geogr_code |
not assigned |
last_indexed |
2024-03-01T15:44:10.791Z |
geogr_code_person |
not assigned |
openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Fv+structure+of+monoclonal+antibody+II-481+against+herpes+simplex+virus+Fc+gamma-binding+glycoprotein+gE+contains+immunodominant+complementarity+determining+region+epitopes+that+react+with+human+immunoglobulin+M+rheumatoid+factors.&rft.date=1994-11-01&genre=article&issn=1540-9538&volume=180&issue=5&spage=1873&epage=1888&pages=1873-1888&jtitle=The+Journal+of+experimental+medicine&atitle=Fv+structure+of+monoclonal+antibody+II-481+against+herpes+simplex+virus+Fc+gamma-binding+glycoprotein+gE+contains+immunodominant+complementarity+determining+region+epitopes+that+react+with+human+immunoglobulin+M+rheumatoid+factors.&aulast=Williams&aufirst=R+C&rft_id=info%3Adoi%2F10.1084%2Fjem.180.5.1873&rft.language%5B0%5D=eng |
SOLR | |
_version_ | 1792339190307880969 |
author | Johansson, P J, Malone, C, Swietnicki, W, Dunn, B M, Williams, R C |
author_facet | Johansson, P J, Malone, C, Swietnicki, W, Dunn, B M, Williams, R C, Johansson, P J, Malone, C, Swietnicki, W, Dunn, B M, Williams, R C |
author_sort | johansson, p j |
container_issue | 5 |
container_start_page | 1873 |
container_title | The Journal of experimental medicine |
container_volume | 180 |
description | <jats:p>Human immunoglobulin M (IgM) rheumatoid factors (RFs) show primary direct enzyme-linked immunosorbent assay (ELISA) reactivity with Fab rather than Fc fragments of monoclonal antibody (mAb) II-481 directed against the Fc gamma-binding site of herpes simplex virus glycoprotein gE. This preferential anti-Fab specificity suggests that RFs react with antigen-binding portions of mAb II-481 as anti-idiotypic antibodies directed at the combining site regions of mAb reacting with the Fc gamma-binding region of gE. Analysis of this idiotype-anti-idiotype reaction employed polymerase chain reaction amplification and sequencing of the variable heavy and light (VH and VL) regions of mAb II-481. When VH and VL regions of mAb II-481 were synthesized as overlapping 7-mer peptides on polypropylene pins, a panel of 10 polyclonal and 6 monoclonal human IgM RFs reacted primarily with epitopes within the three solvent-exposed mAb II-481 complementarity determining regions (CDRs). Preincubation of single CDR heptamer peptides with IgM RFs in free solution, resulted in 63-100% inhibition of RF binding to mAb II-481 on the ELISA plate, confirming the antigenic importance of linear CDR regions for RF reactivity. Combinations of two or three CDR peptides frequently produced 94-100% inhibition of RF binding to whole mAb II-481. Control peptides, singly or in combination, showed no inhibition. Computer modeling suggested that the RF-reactive mAb II-481 Fv region and a previously demonstrated RF-reactive CH3 epitope displayed considerable three-dimensional similarities in conformation. These studies may provide insight into limited shape homologies possibly involved in an RF anti-idiotypic reaction.</jats:p> |
doi_str_mv | 10.1084/jem.180.5.1873 |
facet_avail | Online, Free |
finc_class_facet | Medizin |
format | ElectronicArticle |
format_de105 | Article, E-Article |
format_de14 | Article, E-Article |
format_de15 | Article, E-Article |
format_de520 | Article, E-Article |
format_de540 | Article, E-Article |
format_dech1 | Article, E-Article |
format_ded117 | Article, E-Article |
format_degla1 | E-Article |
format_del152 | Buch |
format_del189 | Article, E-Article |
format_dezi4 | Article |
format_dezwi2 | Article, E-Article |
format_finc | Article, E-Article |
format_nrw | Article, E-Article |
geogr_code | not assigned |
geogr_code_person | not assigned |
id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA4NC9qZW0uMTgwLjUuMTg3Mw |
imprint | Rockefeller University Press, 1994 |
imprint_str_mv | Rockefeller University Press, 1994 |
institution | DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15 |
issn | 0022-1007, 1540-9538 |
issn_str_mv | 0022-1007, 1540-9538 |
language | English |
last_indexed | 2024-03-01T15:44:10.791Z |
match_str | johansson1994fvstructureofmonoclonalantibodyii481againstherpessimplexvirusfcgammabindingglycoproteingecontainsimmunodominantcomplementaritydeterminingregionepitopesthatreactwithhumanimmunoglobulinmrheumatoidfactors |
mega_collection | Rockefeller University Press (CrossRef) |
physical | 1873-1888 |
publishDate | 1994 |
publishDateSort | 1994 |
publisher | Rockefeller University Press |
record_format | ai |
recordtype | ai |
series | The Journal of experimental medicine |
source_id | 49 |
spelling | Johansson, P J Malone, C Swietnicki, W Dunn, B M Williams, R C 0022-1007 1540-9538 Rockefeller University Press Immunology Immunology and Allergy http://dx.doi.org/10.1084/jem.180.5.1873 <jats:p>Human immunoglobulin M (IgM) rheumatoid factors (RFs) show primary direct enzyme-linked immunosorbent assay (ELISA) reactivity with Fab rather than Fc fragments of monoclonal antibody (mAb) II-481 directed against the Fc gamma-binding site of herpes simplex virus glycoprotein gE. This preferential anti-Fab specificity suggests that RFs react with antigen-binding portions of mAb II-481 as anti-idiotypic antibodies directed at the combining site regions of mAb reacting with the Fc gamma-binding region of gE. Analysis of this idiotype-anti-idiotype reaction employed polymerase chain reaction amplification and sequencing of the variable heavy and light (VH and VL) regions of mAb II-481. When VH and VL regions of mAb II-481 were synthesized as overlapping 7-mer peptides on polypropylene pins, a panel of 10 polyclonal and 6 monoclonal human IgM RFs reacted primarily with epitopes within the three solvent-exposed mAb II-481 complementarity determining regions (CDRs). Preincubation of single CDR heptamer peptides with IgM RFs in free solution, resulted in 63-100% inhibition of RF binding to mAb II-481 on the ELISA plate, confirming the antigenic importance of linear CDR regions for RF reactivity. Combinations of two or three CDR peptides frequently produced 94-100% inhibition of RF binding to whole mAb II-481. Control peptides, singly or in combination, showed no inhibition. Computer modeling suggested that the RF-reactive mAb II-481 Fv region and a previously demonstrated RF-reactive CH3 epitope displayed considerable three-dimensional similarities in conformation. These studies may provide insight into limited shape homologies possibly involved in an RF anti-idiotypic reaction.</jats:p> Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. The Journal of experimental medicine |
spellingShingle | Johansson, P J, Malone, C, Swietnicki, W, Dunn, B M, Williams, R C, The Journal of experimental medicine, Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors., Immunology, Immunology and Allergy |
title | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_full | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_fullStr | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_full_unstemmed | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_short | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
title_sort | fv structure of monoclonal antibody ii-481 against herpes simplex virus fc gamma-binding glycoprotein ge contains immunodominant complementarity determining region epitopes that react with human immunoglobulin m rheumatoid factors. |
title_unstemmed | Fv structure of monoclonal antibody II-481 against herpes simplex virus Fc gamma-binding glycoprotein gE contains immunodominant complementarity determining region epitopes that react with human immunoglobulin M rheumatoid factors. |
topic | Immunology, Immunology and Allergy |
url | http://dx.doi.org/10.1084/jem.180.5.1873 |