Source:http://linkedlifedata.com/resource/pubmed/id/20619902
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
2010-10-11
|
pubmed:abstractText |
The cytokine interleukin (IL)-2 functions as a growth factor and central regulator in the immune system. Using a recombinant goose IL-2 (goIL-2) monomer expressed in prokaryotic cells as an immunogen, we synthesized 5 goIL-2 neutralizing mAbs to identify the functional domains of goIL-2, and used these mAbs to finely map the functional domains of the goIL-2 protein. The mimotopes of the 5 anti-goIL-2 mAbs, including HHDPWDXLP, ESLSRXXMXXLXP, SHHLPTSXL, HPDPWDAPLSS, and HEPWQLXL, were identified using a phage display library and peptide-competitive enzyme-linked immunosorbent assay (ELISA). These mimotopes constitute 1 conformational functional domain in the goIL-2 molecule--T¹¹I¹?K¹?D¹?E¹?K¹?L²?G²¹T²²S²³M²?K²?L²?E³?L³¹Y³²T³³P³?E³?S?¹W?²Q?³T??L??Q?? (domain I). The neutralizing mAbs to goIL-2 inhibited the in vitro lymphocyte proliferation stimulated by domain I peptides of goIL-2. A tertiary structural model of goIL-2 showed that domain I is positioned in helix A, long A-B loop, and the N-terminal of helix B. These data provide a clue for defining the interaction between goIL-2 and its receptor.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Neutralizing,
http://linkedlifedata.com/resource/pubmed/chemical/Avian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
1873-2534
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier B.V. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:day |
15
|
pubmed:volume |
138
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
45-50
|
pubmed:meshHeading |
pubmed-meshheading:20619902-Amino Acid Sequence,
pubmed-meshheading:20619902-Animals,
pubmed-meshheading:20619902-Antibodies, Monoclonal,
pubmed-meshheading:20619902-Antibodies, Neutralizing,
pubmed-meshheading:20619902-Avian Proteins,
pubmed-meshheading:20619902-Epitope Mapping,
pubmed-meshheading:20619902-Epitopes,
pubmed-meshheading:20619902-Geese,
pubmed-meshheading:20619902-Interleukin-2,
pubmed-meshheading:20619902-Lymphocyte Activation,
pubmed-meshheading:20619902-Models, Molecular,
pubmed-meshheading:20619902-Molecular Sequence Data,
pubmed-meshheading:20619902-Peptide Library,
pubmed-meshheading:20619902-Protein Structure, Tertiary,
pubmed-meshheading:20619902-Recombinant Proteins
|
pubmed:year |
2010
|
pubmed:articleTitle |
Identification of functional domains in goose interleukin 2.
|
pubmed:affiliation |
Key Laboratory of Animal Epidemic Etiology & Immunological Prevention of Ministry of Agriculture, Zhejiang University, Hangzhou 310029, PR China.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|