IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-38525-2.html
   My bibliography  Save this article

Antibody binding reports spatial heterogeneities in cell membrane organization

Author

Listed:
  • Daniel P. Arnold

    (University of California, Santa Barbara)

  • Yaxin Xu

    (University of California, Santa Barbara)

  • Sho C. Takatori

    (University of California, Santa Barbara)

Abstract

The spatial organization of cell membrane glycoproteins and glycolipids is critical for mediating the binding of ligands, receptors, and macromolecules on the plasma membrane. However, we currently do not have the methods to quantify the spatial heterogeneities of macromolecular crowding on live cell surfaces. In this work, we combine experiment and simulation to report crowding heterogeneities on reconstituted membranes and live cell membranes with nanometer spatial resolution. By quantifying the effective binding affinity of IgG monoclonal antibodies to engineered antigen sensors, we discover sharp gradients in crowding within a few nanometers of the crowded membrane surface. Our measurements on human cancer cells support the hypothesis that raft-like membrane domains exclude bulky membrane proteins and glycoproteins. Our facile and high-throughput method to quantify spatial crowding heterogeneities on live cell membranes may facilitate monoclonal antibody design and provide a mechanistic understanding of plasma membrane biophysical organization.

Suggested Citation

  • Daniel P. Arnold & Yaxin Xu & Sho C. Takatori, 2023. "Antibody binding reports spatial heterogeneities in cell membrane organization," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38525-2
    DOI: 10.1038/s41467-023-38525-2
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-38525-2
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-023-38525-2?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Kai Simons & Elina Ikonen, 1997. "Functional rafts in cell membranes," Nature, Nature, vol. 387(6633), pages 569-572, June.
    2. David J. Busch & Justin R. Houser & Carl C. Hayden & Michael B. Sherman & Eileen M. Lafer & Jeanne C. Stachowiak, 2015. "Intrinsically disordered proteins drive membrane curvature," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    3. Tore Skotland & Kirsten Sandvig, 2019. "The role of PS 18:0/18:1 in membrane function," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    4. Zilu Zhou & Chengzhong Ye & Jingshu Wang & Nancy R. Zhang, 2020. "Surface protein imputation from single cell transcriptomes by deep neural networks," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    5. Yi-Chih Lin & Christophe Chipot & Simon Scheuring, 2020. "Annexin-V stabilizes membrane defects by inducing lipid phase transition," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    6. Inhee Chung & Mike Reichelt & Lily Shao & Robert W. Akita & Hartmut Koeppen & Linda Rangell & Gabriele Schaefer & Ira Mellman & Mark X. Sliwkowski, 2016. "High cell-surface density of HER2 deforms cell membranes," Nature Communications, Nature, vol. 7(1), pages 1-11, November.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Arun Shivanandan & Jayakrishnan Unnikrishnan & Aleksandra Radenovic, 2015. "Accounting for Limited Detection Efficiency and Localization Precision in Cluster Analysis in Single Molecule Localization Microscopy," PLOS ONE, Public Library of Science, vol. 10(3), pages 1-15, March.
    2. Haruka Kemmoku & Kanoko Takahashi & Kojiro Mukai & Toshiki Mori & Koichiro M. Hirosawa & Fumika Kiku & Yasunori Uchida & Yoshihiko Kuchitsu & Yu Nishioka & Masaaki Sawa & Takuma Kishimoto & Kazuma Tan, 2024. "Single-molecule localization microscopy reveals STING clustering at the trans-Golgi network through palmitoylation-dependent accumulation of cholesterol," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Xinchun Zhou & Jinghe Mao & Junmei Ai & Youping Deng & Mary R Roth & Charles Pound & Jeffrey Henegar & Ruth Welti & Steven A Bigler, 2012. "Identification of Plasma Lipid Biomarkers for Prostate Cancer by Lipidomics and Bioinformatics," PLOS ONE, Public Library of Science, vol. 7(11), pages 1-11, November.
    4. San Hadži & Zala Živič & Matic Kovačič & Uroš Zavrtanik & Sarah Haesaerts & Daniel Charlier & Janez Plavec & Alexander N. Volkov & Jurij Lah & Remy Loris, 2024. "Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    5. Matthias Pöhnl & Marius F. W. Trollmann & Rainer A. Böckmann, 2023. "Nonuniversal impact of cholesterol on membranes mobility, curvature sensing and elasticity," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    6. Danchin, Antoine, 1999. "From function to sequence, an integrated view of the genome texts," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 273(1), pages 92-98.
    7. Marta Ukleja & Lara Kricks & Gabriel Torrens & Ilaria Peschiera & Ines Rodrigues-Lopes & Marcin Krupka & Julia García-Fernández & Roberto Melero & Rosa Campo & Ana Eulalio & André Mateus & María López, 2024. "Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
    8. Talia Zeppelin & Lucy Kate Ladefoged & Steffen Sinning & Xavier Periole & Birgit Schiøtt, 2018. "A direct interaction of cholesterol with the dopamine transporter prevents its out-to-inward transition," PLOS Computational Biology, Public Library of Science, vol. 14(1), pages 1-24, January.
    9. D’Emiliano, D. & Casieri, C. & Paci, M. & De Luca, F., 2007. "Detection of ganglioside clustering in DOPC bilayers by 1H-NMR spectroscopy," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 374(1), pages 293-303.
    10. Alexander P. Fellows & Ben John & Martin Wolf & Martin Thämer, 2024. "Spiral packing and chiral selectivity in model membranes probed by phase-resolved sum-frequency generation microscopy," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38525-2. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.