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7TDR

Labrum-interacting protein from saliva LIPS-2 (34K-2) from Aedes albopictus, selenomethionine derivative

Summary for 7TDR
Entry DOI10.2210/pdb7tdr/pdb
Descriptor34k2 salivary protein, SULFATE ION, NITRATE ION, ... (4 entities in total)
Functional Keywordsmosquito, saliva, feeding behaviour, protein-protein interaction, proboscis, cuticle, signaling protein
Biological sourceAedes albopictus (Asian tiger mosquito)
Total number of polymer chains1
Total formula weight35876.93
Authors
Gabrieli, P.,Forneris, F. (deposition date: 2022-01-03, release date: 2022-07-27, Last modification date: 2024-10-09)
Primary citationArnoldi, 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: 35835123
DOI: 10.1016/j.cub.2022.06.049
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.28 Å)
Structure validation

227111

數據於2024-11-06公開中

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