7TDR
Labrum-interacting protein from saliva LIPS-2 (34K-2) from Aedes albopictus, selenomethionine derivative
Summary for 7TDR
Entry DOI | 10.2210/pdb7tdr/pdb |
Descriptor | 34k2 salivary protein, SULFATE ION, NITRATE ION, ... (4 entities in total) |
Functional Keywords | mosquito, saliva, feeding behaviour, protein-protein interaction, proboscis, cuticle, signaling protein |
Biological source | Aedes albopictus (Asian tiger mosquito) |
Total number of polymer chains | 1 |
Total formula weight | 35876.93 |
Authors | Gabrieli, P.,Forneris, F. (deposition date: 2022-01-03, release date: 2022-07-27, Last modification date: 2024-10-09) |
Primary citation | Arnoldi, I.,Mancini, G.,Fumagalli, M.,Gastaldi, D.,D'Andrea, L.,Bandi, C.,Di Venere, M.,Iadarola, P.,Forneris, F.,Gabrieli, P. A salivary factor binds a cuticular protein and modulates biting by inducing morphological changes in the mosquito labrum. Curr.Biol., 32:3493-, 2022 Cited by PubMed Abstract: The mosquito proboscis is an efficient microelectromechanical system, which allows the insect to feed on vertebrate blood quickly and painlessly. Its efficiency is further enhanced by the insect saliva, although through unclear mechanisms. Here, we describe the initial trigger of an unprecedented feedback signaling pathway in Aedes mosquitoes affecting feeding behavior. We identified LIPS proteins in the saliva of Aedes mosquitoes that promote feeding in the vertebrate skin. LIPS show a new all-helical protein fold constituted by two domains. The N-terminal domain interacts with a cuticular protein (Cp19) located at the tip of the mosquito labrum. Upon interaction, the morphology of the labral cuticle changes, and this modification is most likely sensed by proprioceptive neurons. Our study identifies an additional role of mosquito saliva and underlines that the external cuticle is a possible site of key molecular interactions affecting the insect biology and its vector competence. PubMed: 35835123DOI: 10.1016/j.cub.2022.06.049 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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