6HOX

Crystal structure of the binding domain of Paraclostridial Mosquitocidal Protein 1

6HOX の概要

• エントリーDOI: 10.2210/pdb6hox/pdb
• 分子名称: Binding domain (Hc) of Paraclostridial Mosquitocidal Protein 1, DI(HYDROXYETHYL)ETHER, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: neurotoxin, botulinum, paraclostridium bifermentans, anopheles, toxin
• 由来する生物種: Paraclostridium bifermentans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52910.54

構造登録者

Masuyer, G.,Stenmark, P. (登録日: 2018-09-18, 公開日: 2019-07-10, 最終更新日: 2024-01-24)

主引用文献

Contreras, E.,Masuyer, G.,Qureshi, N.,Chawla, S.,Dhillon, H.S.,Lee, H.L.,Chen, J.,Stenmark, P.,Gill, S.S.
A neurotoxin that specifically targets Anopheles mosquitoes.
Nat Commun, 10:2869-2869, 2019

PubMed Abstract: Clostridial neurotoxins, including tetanus and botulinum neurotoxins, generally target vertebrates. We show here that this family of toxins has a much broader host spectrum, by identifying PMP1, a clostridial-like neurotoxin that selectively targets anopheline mosquitoes. Isolation of PMP1 from Paraclostridium bifermentans strains collected in anopheline endemic areas on two continents indicates it is widely distributed. The toxin likely evolved from an ancestral form that targets the nervous system of similar organisms, using a common mechanism that disrupts SNARE-mediated exocytosis. It cleaves the mosquito syntaxin and employs a unique receptor recognition strategy. Our research has an important impact on the study of the evolution of clostridial neurotoxins and provides the basis for the use of P. bifermentans strains and PMP1 as innovative, environmentally friendly approaches to reduce malaria through anopheline control.

PubMed: 31253776
DOI: 10.1038/s41467-019-10732-w

実験手法

X-RAY DIFFRACTION (1.95 Å)