{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu S"],"funding":["Intramural NIH HHS","NCRR NIH HHS","Foundation for the National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["899"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9935623"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"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 recep"],"journal":["Nature communications"],"pubmed_title":["Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission."],"pmcid":["PMC9935623"],"funding_grant_id":["R01 GM071940","S10 OD018111","AI001246","S10 RR023057","R01GM071940","ZIA AI001246"],"pubmed_authors":["Zhou ZH","Xia X","Liu S","Calvo E"],"additional_accession":[]},"is_claimable":false,"name":"Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission.","description":"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 recep","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-05-28T18:33:45.185Z","creation":"2025-04-19T02:46:20.28Z"},"accession":"S-EPMC9935623","cross_references":{"pubmed":["36797290"],"doi":["10.1038/s41467-023-36577-y"]}}