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https://hdl.handle.net/10442/18221
Εξειδίκευση τύπου : | Ανακοίνωση σε συνέδριο |
Τίτλος: | Structural and biochemical studies of an odorant binding protein from the malaria vector anopheles gambiae |
Δημιουργός/Συγγραφέας: | Liggri, P. Tsitsanou, K. [EL] Ζωγράφος, Σπύρος Ε.[EN] Zographos, Spyros E. |
Εκδότης: | John Wiley & Sons, Ltd |
Ημερομηνία: | 2019 |
Γλώσσα: | Αγγλικά |
ISSN: | 2211-5463 |
DOI: | 10.1002/2211-5463.12675 |
Περίληψη: | Anopheles gambiae is the primary mosquito vector responsible for
the transmission of malaria, causing more than 1 million deaths
each year. Mosquitoes rely on olfaction to find mates, food, and
sources of blood meals. Odorant binding proteins (OBPs) that
mediate the initial steps in the transduction cascade of olfactory
signals in insects have been suggested to play an essential role in
the detection and transportation of semiochemicals to odorant
receptors (ORs), and thus, they constitute promising targets for
the design of novel repellent/attractant molecules. Therefore, a
detailed knowledge of their 3D structures and functionalities may
provide a valuable tool for the structure-based discovery of novel
olfactory disruptors of insect host-seeking behavior to be used in
more effective mosquito control strategies. Herein, we present the
novel 3D crystal structure of AgamOBP, an OBP that displays
the highest levels of expression in the female antenna. These
levels also appear to be affected by the circadian cycle as they
dramatically reduced in constant dark (DD) conditions compared
to light-dark (LD) circles. Furthermore, co-crystallization and
fluorescence displacement experiments revealed the ligand-binding
site of AgamOBP as well as the binding modes and specificities
of various natural volatile compounds with repellent properties.
This information will contribute to the better understanding of
the molecular basis of odorant perception. In addition, it will
guide the generation of OBP-structure-based “olfactophore”
models to be used in extensive virtual screening processes for the
identification of novel candidate disruptors of host-seeking mosquito behavior. Such compounds, with enhanced binding affinity
and specificity for a key OBP can be used at lower concentrations and be detected over longer distances, thus providing new
effective repellents for the prevention of mosquito-borne diseases. |
Όνομα εκδήλωσης: | 44th FEBS Congress, From Molecules to Living Systems |
Ημ/νία έναρξης εκδήλωσης : | 2019-07-06 |
Ημ/νία λήξης εκδήλωσης : | 2019-07-11 |
Τόπος εκδήλωσης: | Krakow, Poland |
Τίτλος πηγής δημοσίευσης: | FEBS Open Bio |
Τόμος/Κεφάλαιο: | 9 |
Τεύχος: | Supplement 1 |
Σελίδες: | 269 |
Θεματική Κατηγορία: | [EL] Χημική Βιολογία[EN] Chemical Biology [EL] Βιοχημεία[EN] Biochemistry [EL] Δομική Βιολογία[EN] Structural Biology [EL] Φαρμακευτική[EN] Pharmacy and materia medica |
Λέξεις-Κλειδιά: | Malaria Anopheles gambiae Odorant binding proteins (OBPs) Repellents mosquito-borne diseases odorant receptors (ORs) AgamOBP1 |
Κάτοχος πνευματικών δικαιωμάτων: | Copyright © 2019 The Authors. FEBS Open Bio |
Ηλεκτρονική διεύθυνση στον εκδότη (link): | https://febs.onlinelibrary.wiley.com/doi/10.1002/2211-5463.12675 |
Ηλεκτρονική διεύθυνση περιοδικού (link) : | https://febs.onlinelibrary.wiley.com/journal/22115463 |
Σημειώσεις: | Poster: P-27-070 |
Εμφανίζεται στις συλλογές: | Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο
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