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Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the Scorpion Mesobuthus martensii Karsch.
Shi, Wanxia; He, Pengchen; Zeng, Xian-Chun; Wu, Weiwei; Chen, Xiaoming.
Afiliación
  • Shi W; State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China. shiwxia@sina.com.
  • He P; State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China. Hepengchencug@163.com.
  • Zeng XC; State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China. xianchun_zeng@hotmail.com.
  • Wu W; State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China. wuweiweicug@163.com.
  • Chen X; State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China. chenxiaomingcug@163.com.
Molecules ; 23(12)2018 Dec 14.
Article en En | MEDLINE | ID: mdl-30558111
Highly acidic peptides with no disulfide bridges are widely present in the scorpion venoms; however, none of them has been functionally characterized so far. Here, we cloned the full-length cDNA of a short-chain highly acidic peptide (referred to as HAP-1) from a cDNA library made from the venom glands of the Chinese scorpion Mesobuthus martensii Karsch. HAP-1 contains 19 amino acid residues with a predicted IP value of 4.25. Acidic amino residues account for 33.3% of the total residues in the molecule of HAP-1. HAP-1 shows 76⁻98% identities to some scorpion venom peptides that have not yet been functionally characterized. Secondary structure prediction showed that HAP-1 contains a beta-sheet region (residues 9⁻17), and two coiled coil regions (residues 1⁻8 and 18⁻19) located at the N-terminal and C-terminal regions of the peptide, respectively. Antimicrobial assay showed that HAP-1 does not have any effect on the growth of the bacterium Staphylococcus aureus AB94004. However, it potently inhibits the antimicrobial activity of a 13-mer peptide from M. martensii Karsch against Staphylococcus aureus AB94004. This finding is the first characterization of the function of such highly acidic peptides from scorpions.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Venenos de Escorpión / Escorpiones / Antiinfecciosos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Venenos de Escorpión / Escorpiones / Antiinfecciosos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza