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8FJP

Cryo-EM structure of native mosquito salivary gland surface protein 1 (SGS1)

Summary for 8FJP
Entry DOI10.2210/pdb8fjp/pdb
EMDB information29245
Descriptorsalivary 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 Keywordsrhs/yd-repeats, mosquito salivary protein, receptor domain, pathogen transmission, allergen
Biological sourceAedes aegypti (yellow fever mosquito)
Total number of polymer chains1
Total formula weight381099.30
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 citationLiu, 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: 36797290
DOI: 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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