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TitleNative structure of mosquito salivary protein uncovers domains relevant to pathogen transmission.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 899, Year 2023
Publish dateFeb 17, 2023
AuthorsShiheng Liu / Xian Xia / Eric Calvo / Z Hong Zhou /
PubMed AbstractFemale 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 ...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.
External linksNat Commun / PubMed:36797290 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

29245

8fjp

EMDB-29245, PDB-8fjp:
Cryo-EM structure of native mosquito salivary gland surface protein 1 (SGS1)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • aedes aegypti (yellow fever mosquito)
KeywordsALLERGEN / Rhs/YD-repeats / mosquito salivary protein / receptor domain / pathogen transmission

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