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Int J Biol Macromol. 2017 Sep;102:336-350. doi: 10.1016/j.ijbiomac.2017.04.018. Epub 2017 Apr 8.

Purification and characterization of Cc-Lec, C-type lactose-binding lectin: A platelet aggregation and blood-clotting inhibitor from Cerastes cerastes venom.

Author information

1
USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria.
2
Poitiers University, Laboratory of Ecological and Biological Interactions, 15 Rue de l'Hôtel Dieu, Poitiers, France.
3
USTHB, Faculty of Chemistry, Laboratory of Theoretical Physico-Chemistry and Computer Chemistry, BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria.
4
USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria. Electronic address: flaraba@hotmail.com.

Abstract

In this study, we reported for the first time the biochemical and structural characterization of Cc-Lec, a C-type lectin purified from Cerastes cerastes venom by affinity chromatography. This lectin was homogeneous by SDS-PAGE, and was shown to be a 34 271.59Da polypeptide by Electrospray mass spectrometry MS-ES-TOF. Its identified sequence of 160 amino acids corresponding to one subunit, revealed a high identity with other related proteins. Cc-Lec modeled 3D structure appeared as homodimer cross-linked by one disulfide bridge. Cc-Lec exhibited a calcium dependent hemagglutinating activity against human group O erythrocytes. Cc-Lec inhibited platelet aggregation induced by ADP, arachidonic acid or fibrinogen suggesting its interaction with their specific receptors namely P2Y1 and/or P2Y12, GPIIb/IIIa and TPα respectively. Cc-Lec was not lethal for mice until 10mg/kg administered by i.p. route. The lectin displayed a lasting anticoagulation on mice plasma even two days post-injection. This anticoagulation seems to be related to its interaction with coagulation factors Xa and IXa. Therefore, Cc-Lec prevented FXa amidolytic activity with Km=4.3310-4μg/mL and ki=14.4μg/mL. It seems to interact with these targets through CRD domain which could make it a good target as a pharmacological promising molecule in thrombosis diagnosis and therapy.

KEYWORDS:

Antiplatelet aggregation; C-type lectin; Cerastes cerastes; Coagulation; Homology modeling

PMID:
28400185
DOI:
10.1016/j.ijbiomac.2017.04.018
[Indexed for MEDLINE]

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