Isolation and characterization of a non-specific lipid transfer protein from Chelidonium majus L. latex.
Plant non-specific lipid transfer proteins (nsLTPs) are small basic proteins, which mostly play a role in intracellular lipid transport and antimicrobial defense. Recently it was shown using shotgun proteomic approach that the whole plant extract of Chelidonium majus L. (Papaveraceae) contains relatively abundant nsLTPs. Therefore the aim of the work was to isolate and characterize nsLTP from C. majus latex. Results obtained using PCR approach with degenerate primers showed the presence of nsLTP protein in C. majus root latex, named CmLTP 9.5. The protein consists of 93 aa with a molecular weight of 9.5kDa (NCBI GenBank accession no. ALT21495, coded by KP733898). The mature form of CmLTP 9.5 has a molecular weight of 7.147kDa and contains typical eight strictly conserved cysteine residues. A 3D model of CmLTP 9.5 displays a hydrophobic cavity. The isolated protein fraction tested using diffusion method and critical dilution assay showed strong antibacterial activity towards Gram-negative Campylobacter jejuni as well as Gram-positive Listeria greyi and Clostridium perfringens. Further studies using protein expression system are required to fully understand CmLTP 9.5 mode of action.
['Nawrot|Robert|R|', 'Józefiak|Damian|D|', 'Sip|Anna|A|', 'Kuźma|Dorota|D|', 'Musidlak|Oskar|O|', 'Goździcka-Józefiak|Anna|A|']
D000595:Amino Acid Sequence D000900:Anti-Bacterial Agents D001419:Bacteria D002352:Carrier Proteins D028281:Chelidonium D008958:Models, Molecular D010802:Phylogeny D010940:Plant Proteins D000072417:Protein Domains
Non-specific lipid transfer protein Antibacterial activity 3D structure