scholarly journals QSYP Peptide Sequence Is Selected from Phage Display Libraries by Bovine IgG Contaminants in Monoclonal Antibody Preparations

BioTechniques ◽  
2003 ◽  
Vol 34 (1) ◽  
pp. 132-141 ◽  
Author(s):  
J.M. Jacobs ◽  
B.W. Bailey ◽  
J.B. Burritt ◽  
S.G. Morrison ◽  
R.P. Morrison ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
Peptide Sequence ◽  
Phage Display Libraries ◽  
Antibody Preparations

Utilization of multiple phage display libraries for the identification of dissimilar peptide motifs that bind to a B7-1 monoclonal antibody

1996 ◽  
Vol 1 (2) ◽  
pp. 79-86 ◽  
Author(s):  
P. A. De Ciechi ◽  
C. S. Devine ◽  
S. C. Lee ◽  
S. C. Howard ◽  
P. O. Olins ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
Peptide Motifs ◽  
Phage Display Libraries

scholarly journals The epitope recognized by rituximab

Blood ◽  
2006 ◽  
Vol 108 (6) ◽  
pp. 1975-1978 ◽  
Author(s):  
Mascha Binder ◽  
Florian Otto ◽  
Roland Mertelsmann ◽  
Hendrik Veelken ◽  
Martin Trepel
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
B Cell ◽  
Malignant Lymphoma ◽  
Disulfide Bridge ◽  
Extracellular Loop ◽  
Cell Antigen ◽  
Phage Display Libraries ◽  
Sequence Patterns ◽  
Blocking Capacity

AbstractRituximab is a monoclonal antibody widely used in the treatment of malignant lymphoma and autoimmunity. Its epitope within the B-cell antigen CD20 is largely unknown. We used phage display libraries to select peptides binding to rituximab. Enriched peptides showed 2 sequence patterns: one motif (CALMIANSC) is related to (170)ANPS(173) within CD20, while another motif (WEWTI) may mimic the CD20 segment (182)YCYSI(185). Phages displaying either motif specifically bound rituximab. Binding to rituximab by the CD20 peptides ANPS and YCYSI was weak when used separately and enhanced when both peptides were linked. Recombinant CD20 extracellular loop proteins blocked binding of the selected CWWEWTIGC phage to rituximab, suggesting that CWWEWTIGC mimics the epitope. Blocking capacity was strongly reduced upon mutation of the CD20 strings ANPS or YCYSI. We conclude that rituximab binds a discontinuous epitope in CD20, comprised of (170)ANPS(173) and (182)YCYSI(185), with both strings brought in steric proximity by a disulfide bridge between C(167) and C(183).

scholarly journals Characterization of a novel protective monoclonal antibody that recognizes an epitope common to Vibrio cholerae Ogawa and Inaba serotypes

Microbiology ◽  
2009 ◽  
Vol 155 (7) ◽  
pp. 2353-2364 ◽  
Author(s):  
Madushini N. Dharmasena ◽  
Shelly J. Krebs ◽  
Ronald K. Taylor
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
Vibrio Cholerae ◽  
Lipid A ◽  
Passive Immunization ◽  
Peptide Mimics ◽  
Peptide Mimic ◽  
Phage Display Libraries ◽  
Identification And Characterization

A novel protective monoclonal antibody (mAb) that recognizes a lipopolysaccharide (LPS) epitope common between serotypes Ogawa and Inaba of the O1 serogroup of Vibrio cholerae was characterized and the potential to develop peptide mimics of this protective LPS epitope was investigated. mAb 72.1 recognizes both Ogawa and Inaba LPS and it is vibriocidal and protective in passive immunization against infection by strains of both serotypes. The cDNA-derived amino acid sequence of mAb 72.1 is closely related to the previously characterized mAb ZAC-3, which is thought to recognize an epitope in the lipid A core region of O1 LPS. In an attempt to develop a peptide mimic-based vaccine against V. cholerae, phage display libraries were screened with mAb 72.1 and 11 peptide mimics were identified. Remarkably, all of the peptide sequences identified from linear phage display libraries contained two cysteine residues, suggesting that mAb 72.1 preferentially binds to peptides constrained with a disulphide bond. One of the peptide mimics was immunologically characterized. Although immunization of mice with this peptide mimic conjugated to KLH elicited antibodies against the peptide itself, these antibodies did not cross-react with Ogawa or Inaba LPS. Effectiveness of a peptide mimic as a vaccine may depend on how well the peptide can mimic the carbohydrate interactions when binding to the anti-carbohydrate antibody. Thus, investigating how peptides and LPS bind to mAb 72.1 may be useful in improving current peptide mimics or designing more effective peptide mimics. Identification and characterization of novel protective anti-LPS antibodies may be useful in studying protective epitopes of LPS, which may help develop LPS-based therapeutics against V. cholerae.

scholarly journals Screening of potent neutralizing antibodies against SARS-CoV-2 using convalescent patients-derived phage-display libraries

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Yongbing Pan ◽  
Jianhui Du ◽  
Jia Liu ◽  
Hai Wu ◽  
Fang Gui ◽  
...  
Keyword(s):  
Phage Display ◽  
Neutralizing Antibodies ◽  
Variable Region ◽  
Neutralizing Antibody ◽  
Chain Gene ◽  
Prophylactic Efficacy ◽  
Heavy Chains ◽  
Effective Interventions ◽  
Phage Display Libraries

AbstractAs the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to threaten public health worldwide, the development of effective interventions is urgently needed. Neutralizing antibodies (nAbs) have great potential for the prevention and treatment of SARS-CoV-2 infection. In this study, ten nAbs were isolated from two phage-display immune libraries constructed from the pooled PBMCs of eight COVID-19 convalescent patients. Eight of them, consisting of heavy chains encoded by the immunoglobulin heavy-chain gene-variable region (IGHV)3-66 or IGHV3-53 genes, recognized the same epitope on the receptor-binding domain (RBD), while the remaining two bound to different epitopes. Among the ten antibodies, 2B11 exhibited the highest affinity and neutralization potency against the original wild-type (WT) SARS-CoV-2 virus (KD = 4.76 nM for the S1 protein, IC50 = 6 ng/mL for pseudoviruses, and IC50 = 1 ng/mL for authentic viruses), and potent neutralizing ability against B.1.1.7 pseudoviruses. Furthermore, 1E10, targeting a distinct epitope on RBD, exhibited different neutralization efficiency against WT SARS-CoV-2 and its variants B.1.1.7, B.1.351, and P.1. The crystal structure of the 2B11–RBD complexes revealed that the epitope of 2B11 highly overlaps with the ACE2-binding site. The in vivo experiment of 2B11 using AdV5-hACE2-transduced mice showed encouraging therapeutic and prophylactic efficacy against SARS-CoV-2. Taken together, our results suggest that the highly potent SARS-CoV-2-neutralizing antibody, 2B11, could be used against the WT SARS-CoV-2 and B.1.1.7 variant, or in combination with a different epitope-targeted neutralizing antibody, such as 1E10, against SARS-CoV-2 variants.

Sign in / Sign up

Export Citation Format

Share Document