Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with α-amylase inhibitor properties

Zottich, Umberto; Cunha, Maura Da; Carvalho, André O.; Dias, Germana Bueno; Silva, Nádia C.M.; Santos, Izabela S.; Nacimento, Viviane V. do; Miguel, Emílio C.; Machado, Olga Lima Tavares; Gomes, Valdirene Moreira

doi:10.1016/j.bbagen.2010.12.002

Cited by 99 publications

(57 citation statements)

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“…Zottich et al (2011) isolated a coffee LTP, which they named Cc-LTP1, and in the same study, they proved the existence of two isoforms of this protein. Therefore, we suggest the LTP isolated in this study is an isoform of Cc-LTP1 and thus we have named it Cc-LTP2.…”

Section: Discussionmentioning

confidence: 85%

“…Working on systemic acquired resistance, Maldonado et al (2002) showed that LTPs can also be directly related to defense signaling. Plant LTPs also show antimicrobial activity against a number of microorganisms, especially fungi (Diz et al, 2011;Zottich et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…The IgG fractions were recovered by dialysis in 0.15 M NaCl and freeze-dried. Pre-immune sera were collected before immunization (Zottich et al, 2011).…”

Section: Immunohistochemistry Assaymentioning

confidence: 99%

“…Thus, fraction D1 was lyophilized and subjected to a second purification step through the reverse-phase C18 column of the HPLC system. To better maintain the biological activity of the LTPs, the purification was carried out in 2-propanol solvent (Zottich et al, 2011), where 11 peaks were obtained (H1-H11, indicated only to H11; Figure 1B). As the subsequent purification process, the H11 peak was subjected to a second round of reverse-phase chromatography on the HPLC system, also in a C18 column, and three peaks were obtained ( Figure 1C).…”

Section: Ltp Purification and Characterizationmentioning

confidence: 99%

“…Several compounds with toxic activity against insects, such as legumins and cyclotides (Huang et al, 2009), and against fungi, such as LTP and glycine-rich protein (Zottich et al, 2011(Zottich et al, , 2013, have been isolated from coffee. In the present study, we report the characterization, immunolocalization, and antimicrobial activity of a new LTP called Cc-LTP2, which can be isolated from C. canephora seeds.…”

Section: Introductionmentioning

confidence: 99%

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Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Coffea canephora seeds

et al. 2016

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ABSTRACT. Coffee, an agronomical crop of great economic 2 G.C.V. Bard et al. Genetics and Molecular Research 15 (4): gmr15048859 importance, is also among the most commonly traded commodities in worldwide markets. Antimicrobial peptides, which play a role in plant defense, have been identified and isolated particularly from seeds. We isolated and immunolocalized Cc-LTP2, a new lipid transfer protein (LTP) from Coffea canephora seeds. We report its antimicrobial activity against various phytopathogenic fungi of economic importance, and against the bacterium Xanthomonas euvesicatoria. Peptides from C. canephora seeds were initially extracted using acid buffer and subjected to ion-exchange and reverse-phase chromatographies. A purified peptide of approximately 9 kDa, which we named Cc-LTP2, was then subjected to amino acid sequencing. The analyses showed that it was similar to LTPs isolated from various plants. The tissue and subcellular localization of C. canephora LTPs indicated that they were located in cell walls and intracellular palisade parenchyma, mainly in large vacuoles. The results of immunohistochemistry and histochemistry superposed from C. canephora seed tissues showed that LTPs and lipid bodies are present in organelles, supporting the hypothesis that LTPs from seeds are involved in lipid mobilization during germination. Cc-LTP2 did inhibit the development of the phytopathogenic fungi Colletotrichum lindemuthianum, Colletotrichum gloeosporioides, Fusarium solani, Fusarium lateritium, and Colletotrichum sp, but did inhibit X. euvesicatoria. Cc-LTP2 also increased membrane permeability and induced endogenous production of reactive oxygen species in all the fungi tested.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

“…The IgG fractions were recovered by dialysis in 0.15 M NaCl and freeze-dried. Pre-immune sera were collected before immunization (Zottich et al, 2011).…”

Section: Immunohistochemistry Assaymentioning

confidence: 99%

Section: Ltp Purification and Characterizationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Coffea canephora seeds

et al. 2016

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Lipid‐transfer proteins

Cheung

Wong

et al. 2012

Biopolymers

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Lipid-transfer proteins (LTPs) are basic proteins found in abundance in higher plants. LTPs play lots of roles in plants such as participation in cutin formation, embryogenesis, defense reactions against phytopathogens, symbiosis, and the adaptation of plants to various environmental conditions. In addition, LTPs from field mustard and Chinese daffodil exhibit antiproliferative activity against human cancer cells. LTPs from chili pepper and coffee manifest inhibitory activity against fungi pathogenic to humans such as Candida species. The intent of this article is to review LTPs in the plant kingdom.

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Thionin‐like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts

et al. 2014

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Plants defend themselves against pathogens with production of antimicrobial peptides (AMPs). Herein we describe the discovery of a new antifungal and antibacterial peptide from fruits of Capsicum annuum that showed similarity to an already well characterized family of plant AMPs, thionins. Other fraction composed of two peptides, in which the major peptide also showed similarity to thionins. Among the obtained fractions, fraction 1, which is composed of a single peptide of 7 kDa, was sequenced by Edman method and its comparative sequence analysis in database (nr) showed similarity to thionin-like peptides. Tests against microorganisms, fraction 1 presented inhibitory activity to the cells of yeast Saccharomyces cerevisiae, Candida albicans, and Candida tropicalis and caused growth reduction to the bacteria species Escherichia coli and Pseudomonas aeruginosa. Fraction 3 caused inhibitory activity only for C. albicans and C. tropicalis. This fraction was composed of two peptides of ∼7 and 10 kDa, and the main protein band correspondent to the 7 kDa peptide, also showed similarity to thionins. This plasma membrane permeabilization assay demonstrates that the peptides present in the fractions 1 and 3 induced changes in the membranes of all yeast strains, leading to their permeabilization. Fraction 1 was capable of inhibiting acidification of the medium of glucose-induced S. cerevisiae cells 78% after an incubation time of 30 min, and opposite result was obtained for C. albicans. Experiments demonstrate that the fraction 1 and 3 were toxic and induced changes in the membranes of all yeast strains, leading to their permeabilization.

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Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with α-amylase inhibitor properties

Cited by 99 publications

References 53 publications

Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Coffea canephora seeds

Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Coffea canephora seeds

Lipid‐transfer proteins

Thionin‐like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts

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