Optimization of blood sampling time for isolation of antigen binding single-domain antibodies from immunized llamas

被引:0
|
作者
Harmsen, Michiel M. [1 ]
Harders, Frank [1 ]
van de Water, Sandra [1 ]
van Solt, Conny S. [1 ]
Koets, Ad P. [1 ]
van der Wal, Fimme J. [1 ]
Gupta, Nishi [1 ]
机构
[1] Wageningen Univ & Res, Wageningen Biovet Res, Lelystad, Netherlands
关键词
Plasma cell; Phage display; Recombinant antibody; Blood sampling; Nanobody; Single-domain antibody; GENERATION;
D O I
10.1016/j.jim.2025.113844
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Single-domain antibody fragments (VHHs) binding specific antigens are often isolated by llama immunization and phage display selection. We determined the optimal blood sampling time for generating phage display libraries with a high frequency of antigen-binding VHHs. Two llamas were immunized with 7 antigens. Blood samples collected with 2-3 day interval up to 11 days post immunization were used for deep sequencing and phage display selection of VHHs. The frequency of VHH clones was determined by the identification of unique VHH sequences in deep sequenced libraries. On average, the highest clone frequency was found in libraries generated 5 days post immunization. Polyclonal phage ELISA also suggested day 5 as the optimal blood sampling time.
引用
收藏
页数:5
相关论文
共 50 条
  • [41] Analysis of the binding loops configuration and surface adaptation of different crystallized single-domain antibodies in response to various antigens
    Al Qaraghuli, Mohammed M.
    Ferro, Valerie A.
    JOURNAL OF MOLECULAR RECOGNITION, 2017, 30 (04)
  • [42] Real-time analysis of epithelial-mesenchymal transition using fluorescent single-domain antibodies
    Maier, Julia
    Traenkle, Bjoern
    Rothbauer, Ulrich
    SCIENTIFIC REPORTS, 2015, 5
  • [43] Impact of Noncanonical Disulfide Bond on Thermal Resistance and Binding Affinity of Shark-Derived Single-Domain Antibodies
    Qiu, Shuo
    Liu, Chang
    Li, Guoqiang
    Lin, Hong
    Cao, Limin
    Wang, Kaiqiang
    Wang, Xiudan
    Sui, Jianxin
    ACS BIOMATERIALS SCIENCE & ENGINEERING, 2025,
  • [44] Real-time analysis of epithelial-mesenchymal transition using fluorescent single-domain antibodies
    Julia Maier
    Bjoern Traenkle
    Ulrich Rothbauer
    Scientific Reports, 5
  • [45] Isolation of Panels of Llama Single-Domain Antibody Fragments Binding All Nine Neuraminidase Subtypes of Influenza A Virus
    Harmsen, Michiel M.
    Blokker, Juliette C.
    Pritz-Verschuren, Sylvia B.
    Bartelink, Willem
    van der Burg, Herman
    Koch, Guus
    ANTIBODIES, 2013, 2 (02): : 168 - 192
  • [46] Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies
    Ikeuchi, Emina
    Kuroda, Daisuke
    Nakakido, Makoto
    Murakami, Akikazu
    Tsumoto, Kouhei
    SCIENTIFIC REPORTS, 2021, 11 (01)
  • [47] Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies
    Emina Ikeuchi
    Daisuke Kuroda
    Makoto Nakakido
    Akikazu Murakami
    Kouhei Tsumoto
    Scientific Reports, 11
  • [48] Single-domain antibodies reveal unique borrelicidal epitopes on the Lyme disease vaccine antigen, outer surface protein A (OspA)
    Vance, David J.
    Basir, Saiful
    Piazza, Carol Lyn
    Willsey, Graham G.
    Haque, H. M. Emranul
    Tremblay, Jacque M.
    Rudolph, Michael J.
    Muriuki, Beatrice
    Cavacini, Lisa
    Weis, David D.
    Shoemaker, Charles B.
    Mantis, Nicholas J.
    INFECTION AND IMMUNITY, 2024, 92 (04)
  • [49] Direct Injection of Functional Single-Domain Antibodies from E. coli into Human Cells
    Blanco-Toribio, Ana
    Muyldermans, Serge
    Frankel, Gad
    Angel Fernandez, Luis
    PLOS ONE, 2010, 5 (12):
  • [50] Selection of cholera toxin specific IgNAR single-domain antibodies from a naive shark library
    Liu, Jinny L.
    Anderson, George P.
    Delehanty, James B.
    Baumann, Richard
    Hayhurst, Andrew
    Goldman, Ellen R.
    MOLECULAR IMMUNOLOGY, 2007, 44 (07) : 1775 - 1783