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Carballar-Lejarazú R Rodríguez MH de la Cruz Hernández-Hernández F Ramos-Castañeda J Possani LD Zurita-Ortega M Reynaud-Garza E Hernández-Rivas R Loukeris T Lycett G Lanz-Mendoza H 《Cellular and molecular life sciences : CMLS》2008,65(19):3081-3092
Scorpine is an antimicrobial peptide whose structure resembles a hybrid between a defensin and a cecropin. It exhibits antibacterial
activity and inhibits the sporogonic development of parasites responsible for murine malaria. In this communication we report
the production of scorpine in a heterelogous system, using a specific vector containing its cloned gene. The recombinantly
expressed scorpine (RScp) in Anopheles gambie cells showed antibacterial activity against Bacillus subtilis and Klebsiella pneumoniae, at 5 and 10 μM, respectively. It also produced 98% mortality in sexual stages of Plasmodium berghei at 15 μM and 100% reduction in Plasmodium falciparum parasitemia at 5 μM. RScp also inhibited virus dengue-2 replication in C6/36 mosquito cells. In addition, we generated viable
and fertile transgenic Drosophila that overexpresses and correctly secretes RScp into the insect hemolymph, suggesting that the generation of transgenic mosquitoes
resistant to different pathogens may be viable.
Received 6 May 2008; received after revision 24 July 2008; accepted 29 July 2008 相似文献
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Diego-García E Abdel-Mottaleb Y Schwartz EF de la Vega RC Tytgat J Possani LD 《Cellular and molecular life sciences : CMLS》2008,65(1):187-200
Among the scorpion venom components whose function are poorly known or even show contrasting pharmacological results are those
called “orphan peptides”. The most widely distributed are named β-KTx or scorpine-like peptides. They contain three disulfide
bridges with two recognizable domains: a freely moving N-terminal amino acid sequence and a tightly folded C-terminal region
with a cysteine-stabilized α/β (CS-αβ) motif. Four such peptides and three cloned genes are reported here. They were assayed
for their cytolytic, antimicrobial and K
+ channel-blocking activities. Two main characteristics were found: the existence of an unusual structural and functional diversity,
whereby the full-length peptide can lyse cells or kill microorganisms, and a C-terminal domain containing the CS-αβ motif
that can block K
+ channels. Furthermore, sequence analyses and phylogenetic reconstructions are used to discuss the evolution of this type
of peptide and to highlight the versatility of the CS-αβ structures.
Received 13 August 2007; received after revision 30 October 2007; accepted 2 November 2007 相似文献
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