Disease relevance of LOC548115

• The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein [1].
• Northern blot analysis, using the Ltp4-specific probe, indicated that Xanthomonas campestris pv. translucens induced an increase over basal levels of Ltp4 mRNA, while Pseudomonas syringae pv. japonica caused a decrease [2].

High impact information on LOC548115

• Specific adduction of plant lipid transfer protein by an allene oxide generated by 9-lipoxygenase and allene oxide synthase [3].
• Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification [4].
• CONCLUSION: The major allergen of maize is an LTP with a molecular weight of 9 kd that is highly homologous with the peach LTP, the major allergen of the Prunoideae subfamily [1].
• These results are consistent with the proposal that BLT4 LTPs have a lipid-transfer function associated with frost acclimation in barley [5].
• Differences between the maize LTP and the BLT4 family include amino acid substitutions around the entrance and inside the predicted hydrophobic binding tunnels of these proteins [5].

Biological context of LOC548115

• ECLTP (early culture lipid transfer protein) had homology to lipid transfer proteins (LTPs), and had an expression pattern similar to that of an LTP known to be a marker of the early stages of embryogenesis in the carrot somatic embryogenesis system [6].
• The complete amino acid sequences of proteins Cw18 and Cw21 were determined and found to be homologous to previously described, non-specific lipid transfer proteins from plants (32-62% identical positions) [7].
• Sequence analysis of Ltp1 showed that it contains an open reading frame of 351 bp interrupted by a single intron of 133 bp [8].
• Southern blot analysis indicated the existence of three or more Ltp4 genes per haploid genome and showed considerable polymorphism among barley cultivars [2].
• Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands [9].

Associations of LOC548115 with chemical compounds

• Molecular dynamics modelling shows that BLT4.9 can accommodate hexadecanoic acid in its binding tunnel in similar conformation to the maize LTP [5].
• Cadmium leads to stimulated expression of the lipid transfer protein genes in barley: implications for the involvement of lipid transfer proteins in wax assembly [10].
• Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins [11].

Other interactions of LOC548115

• The promoter of the barley aleurone-specific gene encoding a putative 7 kDa lipid transfer protein confers aleurone cell-specific expression in transgenic rice [12].

Analytical, diagnostic and therapeutic context of LOC548115

• Northern blot analysis showed that Ltp1 mRNA accumulates specifically in the aleurone layer of developing and germinating seeds [8].
• Interestingly, a novel non-specific lipid transfer protein-like protein (OsLTPL1) and a novel early nodulin-like protein (OsENODL1) were also identified in the more hydrophobic fractions from HPLC as beta-GlcY-reactive proteins [13].
• Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling [14].

References