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Publication Abstract from PubMed

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.

Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission.,Liu S, Xia X, Calvo E, Zhou ZH Nat Commun. 2023 Feb 17;14(1):899. doi: 10.1038/s41467-023-36577-y. PMID:36797290^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.