Crotacetin, a novel snake venom C-type lectin homolog of convulxin, exhibits an unpredictable antimicrobial activity
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- 作者：Gandhi Rádis-Baptista (1)
Frederico Bruno Mendes Batista Moreno (1) (3)
Lucas de Lima Nogueira (1)
Alice M. C. Martins (4)
Daniela de Oliveira Toyama (5)
Marcos Hikari Toyama (6)
Benildo Sousa Cavada (1)
Walter Filgueira de Azevedo Jr. (3)
Tetsuo Yamane (7) (8) - 关键词：Crotalus durissus venom ; snake venom C ; type lectin ; crotacetin ; convulxin ; platelet aggregation ; antimicrobial activity
- 刊名：Cell Biochemistry and Biophysics
- 出版年：2006
- 出版时间：March 2006
- 年：2006
- 卷：44
- 期：3
- 页码：412-423
- 全文大小：858KB
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Frederico Bruno Mendes Batista Moreno (1) (3)
Lucas de Lima Nogueira (1)
Alice M. C. Martins (4)
Daniela de Oliveira Toyama (5)
Marcos Hikari Toyama (6)
Benildo Sousa Cavada (1)
Walter Filgueira de Azevedo Jr. (3)
Tetsuo Yamane (7) (8)
1. Department of Biochemistry and Molecular Biology, Federal University of Ceará, Ceara, Brazil
3. Department of Physics-IBILCE/UNESP, S?o Paulo, Brazil
4. Department of Clinical and Toxicological Analysis, Federal University of Ceará, Ceara, Brazil
5. Department of Biochemistry, UNICAMP, S?o Paulo, Brazil
6. Department of Fundamental Chemistry, UNESP, S?o Paulo, Brazil
7. Laboratory of Molecular Biology, IPEN-CNEN, S?o Paulo, Brazil
8. Center of Biothecnology of Amazon, CBA, Manaus, Brazil
文摘
Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins that are capable of interfering with blood stasis. A very well-studied svC-type lectin is the heterodimeric toxin, convulxin (CVX), from the venom of South American rattlesnake Crotalus durissus terrificus. CVX is able to activate platelets and induce their aggregation by acting via p62/GPVI collagen receptor. By using polymerase chain reaction homology screening, we have cloned several cDNA precursors of CVX subunit homologs. One of them, named crotacetin (CTC) β-subunit, predicts a polypeptide with a topology very similar to the tridimensional conformations of other subunits of CVX-like snake toxins, as determined by computational analysis. Using gel permeation and reverse-phase high-performance liquid chromatography, CTC was purified from C. durissus venoms. CTC can be isolated from the venom of several C. durissus subspecies, but its quantitative predominance is in the venom of C. durissus cascavella. Functional analysis indicates that CTC induces platelet aggregation, and, importantly, exhibits an antimicrobial activity against Gram-positive and-negative bacteria, comparable with CVX.