Zhu Shen

Medical University of South Carolina

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Mary Seabury Stone

Medical University of South Carolina

Prasad Kumarasinghe

University of Western Australia

Angela Moore

Arlington Center for Dermatology

Robert T. Brodell

State Street (United States)

Steffen Emmert

Universitätsmedizin Rostock

Zoe Diana Draelos

Dermatology Consulting Services

Pearl E. Grimes

Vitiligo and Pigmentation Institute of Southern California

William H. Eaglstein

Medical University of South Carolina

Michel Mcdonald

Medical University of South Carolina

Cathy Massoud

Brown University

Cooperative Institutions

Medical University of South Carolina

291

UConn Health

286

American Academy of Dermatology

282

Adult and Pediatric Dermatology

University of Pennsylvania

RELX Group (United States)

Ackerman Academy of Dermatopathology

University of California, San Francisco

Northwestern University

Harvard University

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[Construction and screening of the human phage antibody library from a patient with melanoma].

PubMed (2004)

Jun Yang Tianwen Gao Gang Wang Lei Wang Zhu Shen

To construct and screen the human phage antibody library from a patient with melanoma.Total RNA was extracted from the peripheral blood mononuclear cells (PBMCs) of a patient with melanoma who has survived for twenty years. The heavy chain Fd fragments and kappa light chains were amplified by RT-PCR. The amplified products were cloned into phagemid vector to construct Fab antibody library. The library was panned with two kinds of melanoma cells for 4 rounds.Antibody library contained 1.2 x 10(8) different clones. Specific phage antibodies against one of the two melanoma cells were obtained after 4 rounds of panning.Specific human phage antibodies against melanoma cells were obtained.

Panning (audio)

Phagemid

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Editorial board

Journal of the American Academy of Dermatology (2023)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(23)00070-1

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Editorial board

Journal of the American Academy of Dermatology (2023)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(23)03049-9

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Editorial Board

Journal of the American Academy of Dermatology (2022)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(22)03011-0

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Editorial Board

Journal of the American Academy of Dermatology (2023)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(23)02615-4

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Editorial Board

Journal of the American Academy of Dermatology (2023)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(23)01089-7

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Editorial Board

Journal of the American Academy of Dermatology (2023)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

10.1016/s0190-9622(23)00785-5

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Screening and identification of epitopes on human immunoglobulin E from 7~(TM) phage display peptide library

Di-Si Junyi Daxue xuebao (2005)

Lin Gao Chunyan Yu Zhu Shen Zhang Ying-qi Zhen Yan

AIM: To identify and characterize epitopes of human immunoglobulin E screened from 7 TMphage display peptide library. METHODS: The epitopes of human immunoglobulin E were screened from 7 TMphage display peptide library by using anti-IgE antibody as target protein and were identified by sandwich ELISA. RESULTS: After 3 rounds of screening, 15 of the 48 phage clones were identified as positive clones, which could bind to anti-human IgE antibody. The amino acid sequences of the positive clones were DHIDMGL, DHMWLGL, DHQDAGF and DHMDQNL. Competitive ELISA results demonstrated the competitive binding of the 4 sequences and IgG to anti-IgE mAb. Multiple antigenic peptides dot blot displayed that the screened multipeptides could specifically bind to anti-IgE antibody. CONCLUSION: The screened epitopes are similar in their framwork, and of extensive amino acid homology with IgE-CH3 region. These phage display peptides can bind specifically to anti-IgE antibody, providing a basis for further research on IgG related multipeptide vaccine.

Homology

Linear epitope

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Editorial board

Journal of the American Academy of Dermatology (2022)

Dirk M. Elston Jane M. Grant‐Kels James C. Smith Richard Dobson Jeffrey D. Bernhard

Editorial board

10.1016/s0190-9622(22)00617-x

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