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Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission

Author

Listed:
  • Shiheng Liu

    (University of California
    University of California)

  • Xian Xia

    (University of California
    University of California)

  • Eric Calvo

    (National Institute of Allergy and Infectious Diseases, National Institutes of Health)

  • Z. Hong Zhou

    (University of California
    University of California)

Abstract

Female mosquitoes inject saliva into vertebrate hosts during blood feeding. This process transmits mosquito-borne human pathogens that collectively cause ~1,000,000 deaths/year. Among the most abundant and conserved proteins secreted by female salivary glands is a high-molecular weight protein called salivary gland surface protein 1 (SGS1) that facilitates pathogen transmission, but its mechanism remains elusive. Here, we determine the native structure of SGS1 by the cryoID approach, showing that the 3364 amino-acid protein has a Tc toxin-like Rhs/YD shell, four receptor domains, and a set of C-terminal daisy-chained helices. These helices are partially shielded inside the Rhs/YD shell and poised to transform into predicted transmembrane helices. This transformation, and the numerous receptor domains on the surface of SGS1, are likely key in facilitating sporozoite/arbovirus invasion into the salivary glands and manipulating the host’s immune response.

Suggested Citation

  • Shiheng Liu & Xian Xia & Eric Calvo & Z. Hong Zhou, 2023. "Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36577-y
    DOI: 10.1038/s41467-023-36577-y
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    References listed on IDEAS

    as
    1. Daniel Roderer & Evelyn Schubert & Oleg Sitsel & Stefan Raunser, 2019. "Towards the application of Tc toxins as a universal protein translocation system," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    2. Christos Gatsogiannis & Felipe Merino & Daniel Roderer & David Balchin & Evelyn Schubert & Anne Kuhlee & Manajit Hayer-Hartl & Stefan Raunser, 2018. "Tc toxin activation requires unfolding and refolding of a β-propeller," Nature, Nature, vol. 563(7730), pages 209-213, November.
    3. Jason N. Busby & Santosh Panjikar & Michael J. Landsberg & Mark R. H. Hurst & J. Shaun Lott, 2013. "The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device," Nature, Nature, vol. 501(7468), pages 547-550, September.
    4. Verity A. Jackson & Dimphna H. Meijer & Maria Carrasquero & Laura S. Bezouwen & Edward D. Lowe & Colin Kleanthous & Bert J. C. Janssen & Elena Seiradake, 2018. "Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
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