BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 3490

Peptides:

Sequences

SGVYKVAYDWQH(13/42)
VHWDFRQWWQPS(10/42)
HHWNSLWWPWKT(9/42)
HFWHWPLWTRDH(5/42)
HHYWWPWQITNS(5/42)
TWWHWPRMYMGL(1/15)
WHWWPHWDTGRA(1/15)
WYPYNWTHWFTH(1/15)
HLWYPWIWPMQQ(1/15)
WHWNAWNWSSQQ(1/15)
WHWSWLVHPHTL(1/15)
LTNNLHKQVGPW(1/15)
WHFTWWVDNRMT(1/15)
HFMSYAGASTWA(1/15)
GLHTSATNLYLH(1/15)
GSAPLLTVDTSK(1/15)
WEYSVVTPVDFL(1/15)
GLTSQRLDGLPP(1/15)
NPHIAHSLHSWV(1/15)
HPHDYNDLTSPF(1/15)

Sequences Features:

Motif:

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 32413370

Target Name:

Anti-HIV-1 monoclonal antibody Y498

Template Name:

Not determined.

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

Ph.D.-12 phage display library (X12)

Affinity Measurement Method:

ELISA

Affinity Measurement Description:

A phage ELISA was performed to determine the binding 12 mer-peptides. The results were measured at a wavelength of 450 nm.

Brief Description:

A random phage display peptide library (PhD-12) was purchased from New England Biolabs.After three rounds of selection, the selected phage clones were identified by single-strand D sequencing and phage ELISA, and the encoded peptide sequences were deduced. The concentration of washing buffer was increased gradually each round to a maximum of 0.5%TBST.

BiopanningDataSet Comments:

To identify the key amino acid recognition site contacted with neutralizing antibody Y498, peptides were panned from the PhD-12 peptide library and predicted using online software. Then, four key amino acid sites, G367, D368, E370, and V372 located on the CD4 binding loop on gp120 of envelope of human immunodeficiency virus-1 (HIV-1), were found to determine the neutralization of antibody Y498. Residue E370 is in the deep part of the CD4 binding loop, which affects Y498-mediated neutralization.

Curator:

Chunchao Pu

Curation Date:

2020-12-01

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