Learn More
Three new cysteine-free venom peptides, which are referred to as Heterin-1, Heterin-2 and Spiniferin, respectively, were identified from the scorpion Heterometrus spinifer. Heterin-1, Heterin-2 and Spiniferin contain 43, 24 and 13 amino acid residues, respectively. Genomic analysis showed that the genomic organizations of the three peptides are consistent(More)
Three novel cysteine-free venom peptides, which were referred to as Pantinin-1, Pantinin-2 and Pantinin-3, respectively, have been identified from the scorpion Pandinus imperator by cDNA cloning strategy. The precursor of each peptide consists of a signal peptide, a mature peptide with no disulfide bridges, and an acidic propeptide with a typical processing(More)
BmKbpp is a novel cationic and α-helical peptide from the Chinese scorpion Mesobuthus martensii Karsch, of which function or biological activity has not been characterized so far. Here we showed that BmKbpp possesses strong antimicrobial activity against both Gram-positive and Gram-negative bacteria with a MIC range from 2.3 μM to 68.2 μM for the majority(More)
Few diazotrophs have been found to belong to the family Cytophagaceae so far. In the present study, a Gram-negative, rod-shaped bacterium that forms red colonies, was isolated from sands of the Takalamakan desert. It was designated H4XT. Phylogenetic and biochemical analysis indicated that the isolate is a new species of the genus Pontibacter. The 16S rRNA(More)
A red-pigmented, Gram-negative, strictly aerobic, rod-shaped bacterium which was motile by gliding, designated strain 1351T, was isolated from the soil of Lengduo, Tibet in China and subjected to a polyphasic taxonomic analysis. The isolate grows optimally at 30°C and pH 7. It grows with NaCl tolerated up to 1.5% (optimum, 0.5%). Phylogenetic analysis based(More)
The venom peptides from the scorpion Heterometrus spinifer have been poorly characterized so far. Here, we identified a novel class of antimicrobial peptides from the venom gland of H. spinifer, which were referred to as HsAp, HsAp2, HsAp3 and HsAp4, respectively. Each of the four peptides consists of 29 amino acid residues, and is cationic and weakly(More)
It was shown that peptides containing trypsin inhibitor-like cysteine-rich (TIL) domain are able to inhibit proteinase activities, and thus play important roles in various biological processes, such as immune response and anticoagulation. However, only a limited number of the TIL peptides have been identified and characterized so far; and little has been(More)
The full-length cDNA sequences of two novel cysteine-rich peptides (referred to as HsVx1 and MmKTx1) were obtained from scorpions. The two peptides represent a novel class of cysteine-rich peptides with a unique cysteine pattern. The genomic sequence of HsVx1 is composed of three exons interrupted by two introns that are localized in the mature peptide(More)
The cDNA sequence encoding a novel BmKBT-like peptide (referred to as BmKBy) was cloned and sequenced from the scorpion Mesobuthus martensii Karsch. Functional analysis indicated that both BmKBT and BmKBy possess strong toxicity in mice, but very weak toxicity in cotton bollworm. Phylogenetic analysis showed that BmKBy and BmKBT represent evolutionary(More)
We studied microbial communities in two paddy soils, which did not receive nitrogen fertilization and were distinguished by the soil properties. The two microbial communities differed in the relative abundance of gram-negative bacteria and total microbial biomass. Variability in microbial communities between the two fields was related to the levels of(More)