8FJP
Cryo-EM structure of native mosquito salivary gland surface protein 1 (SGS1)
Summary for 8FJP
Entry DOI | 10.2210/pdb8fjp/pdb |
EMDB information | 29245 |
Descriptor | salivary gland surface protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | rhs/yd-repeats, mosquito salivary protein, receptor domain, pathogen transmission, allergen |
Biological source | Aedes aegypti (yellow fever mosquito) |
Total number of polymer chains | 1 |
Total formula weight | 381099.30 |
Authors | Liu, S.,Xia, X.,Calvo, E.,Zhou, Z.H. (deposition date: 2022-12-20, release date: 2023-03-01, Last modification date: 2024-10-23) |
Primary citation | Liu, S.,Xia, X.,Calvo, E.,Zhou, Z.H. Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission. Nat Commun, 14:899-899, 2023 Cited by PubMed 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. PubMed: 36797290DOI: 10.1038/s41467-023-36577-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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