An Antifungal Protein Purified from Pearl Millet Seeds Shows Sequence Homology to Lipid Transfer Proteins

Velazhahan, R.; Radhajeyalakshmi, R.; Thangavelu, R; Muthukrishnan, Subbaratnam

doi:10.1023/a:1012463315579

Cited by 23 publications

(12 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Many functions have been attributed to plant LTPs, including transport of hydrophobic molecules (such as phospholipids) between membranes, wax and cutin assembly (Cameron et al 2006, Han et al 2001, Pyee et al 1994), protection against fungal and bacterial pathogens (Carvalho and Gomes 2007, Gonorazky et al 2005, Lin et al 2007, Terras et al 1992, Velazhahan et al 2001, Yang et al 2006), mobilization of seed storage lipids (Edqvist and Farbos 2002, Tsuboi et al 1992) and cell wall extension (Nieuwland et al 2005). However, in this work, we show for the first time that Ca ‐LTP 1 also presents α ‐amylase inhibitory properties in vitro.…”

Section: Resultsmentioning

confidence: 99%

Characterisation, immunolocalisation and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annuum) seeds with novel α‐amylase inhibitory properties

Diz

Carvalho

Ribeiro

et al. 2011

Physiologia Plantarum

View full text Add to dashboard Cite

Lipid transfer proteins (LTPs) were thus named because they facilitate the transfer of lipids between membranes in vitro. This study was triggered by the characterization of a 9-kDa LTP from Capsicum annuum seeds that we call Ca-LTP(1) . Ca-LTP(1) was repurified, and in the last chromatographic purification step, propanol was used as the solvent in place of acetonitrile to maintain the protein's biological activity. Bidimensional electrophoresis of the 9-kDa band, which corresponds to the purified Ca-LTP(1) , showed the presence of three isoforms with isoelectric points (pIs) of 6.0, 8.5 and 9.5. Circular dichroism (CD) analysis suggested a predominance of α-helices, as expected for the structure of an LTP family member. LTPs immunorelated to Ca-LTP(1) from C. annuum were also detected by western blotting in exudates released from C. annuum seeds and also in other Capsicum species. The tissue and subcellular localization of Ca-LTP(1) indicated that it was mainly localized within dense vesicles. In addition, isolated Ca-LTP(1) exhibited antifungal activity against Colletotrichum lindemunthianum, and especially against Candida tropicalis, causing several morphological changes to the cells including the formation of pseudohyphae. Ca-LTP(1) also caused the yeast plasma membrane to be permeable to the dye SYTOX green, as verified by fluorescence microscopy. We also found that Ca-LTP(1) is able to inhibit mammalian α-amylase activity in vitro.

show abstract

Section: Resultsmentioning

confidence: 99%

Characterisation, immunolocalisation and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annuum) seeds with novel α‐amylase inhibitory properties

Diz

Carvalho

Ribeiro

et al. 2011

Physiologia Plantarum

View full text Add to dashboard Cite

show abstract

“…In addition to their speculated lipid transfer function, which is inconsistent with their cell wall location (Thoma et al ., 1994), other roles, such as participation in cuticle formation and embryogenesis (Sterk et al ., 1991), polygalacturonase‐mediated pectin degradation (Tomassen et al ., 2007), establishment of symbiosis (Krause et al ., 1994) and adaptation to abiotic stresses (Hughes et al ., 1992; Torres‐Schumann et al ., 1992; White et al ., 1994; Garcia‐Olmedo et al ., 1995; Jung et al ., 2003; Jang et al ., 2004; Carvalho et al ., 2006), have been suggested. It has also been suggested that LTPs are involved in plant defence against phytopathogens (Terras et al ., 1992; Molina et al ., 1993; Segura et al ., 1993; Dubreil et al ., 1998; Velazhahan et al ., 2001; Gonorazky et al ., 2005; Diz et al ., 2006; Lin et al ., 2007). LTPs are also clinically important as a result of their role in food allergies, because they are highly resistant to food processing and the gastrointestinal environment (Pastorello and Robino, 2004).…”

Section: Plant Peptidesmentioning

confidence: 99%

Plant peptides and peptidomics

Farrokhi¹,

Whitelegge²,

Brusslan³

2007

Plant Biotechnology Journal

121

View full text Add to dashboard Cite

SummaryExtracellular plant peptides perform a large variety of functions, including signalling and defence. Intracellular peptides often have physiological functions or may merely be the products of general proteolysis. Plant peptides have been identified and, in part, functionally characterized through biochemical and genetic studies, which are lengthy and in some cases impractical. Peptidomics is a branch of proteomics that has been developed over the last 5 years, and has been used mainly to study neuropeptides in animals and the degradome of proteases. Peptidomics is a fast, efficient methodology that can detect minute and transient amounts of peptides and identify their post-translational modifications. This review describes known plant peptides and introduces the use of peptidomics for the detection of novel plant peptides.

show abstract

“…The exuded LTP from cowpea was seen to be present in non-retained fraction after anion exchange chromatography and proved to be a basic protein with an apparent molecular mass of ~ 9 kDa (figures 2 and 3). This estimated Mr for the exuded LTP lies in the range of molecular masses found by several authors for these antimicrobial peptides isolated from other plants Cammue et al, 1995;Regente and de La Canal, 1995;Velazhahan et al, 2001). The isolation of the exuded LTP from cowpea seeds was performed basically by submitting the P1 fraction (basic fraction from DEAE-Sepharose) to Superdex peptide HR-10/ 30 chromatography in HPLC (figure 4).…”

mentioning

confidence: 84%

Purification and molecular mass determination of a lipid transfer protein exuded from Vigna unguiculata seeds

Diz

Carvalho

Gomes

2003

Braz. J. Plant Physiol.

View full text Add to dashboard Cite

Plants exude a variety of substances through their surface especially of roots and germinating seeds. Some of these released compounds seem to have an inhibitory action against certain pathogens. Lipid transfer proteins (LTPs) are 9 kDa cysteine-rich cationic peptides and are thought to play a role in the protection of plants against microbial infections. The aim of this work was to isolate and determine the molecular mass of a LTP present in the exudates of imbibed cowpea seeds. For exudation induction, 50 seeds were submerged in 50 mL sterile 100 mmol.L-1 Na-acetate buffer, pH 4.5 and shaken at 30 ºC for 24 h. The resulting exudate was subjected to ammonium sulphate fractionation and the pellet formed between 0 and 70 % saturation was dialysed and recovered by freeze drying. Further purification steps were carried out using chromatographic methods and the molecular mass of the LTP determined. All of these steps were monitored by SDS-Tricine gel electrophoresis and Western blotting using an anti-LTP serum. The purified LTP showed a relative molecular mass of 9 kDa.

show abstract

An Antifungal Protein Purified from Pearl Millet Seeds Shows Sequence Homology to Lipid Transfer Proteins

Cited by 23 publications

References 42 publications

Characterisation, immunolocalisation and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annuum) seeds with novel α‐amylase inhibitory properties

Characterisation, immunolocalisation and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annuum) seeds with novel α‐amylase inhibitory properties

Plant peptides and peptidomics

Purification and molecular mass determination of a lipid transfer protein exuded from Vigna unguiculata seeds

Contact Info

Product

Resources

About