Chitinase and β-1,3-glucanase in the lutoid-body fraction of Hevea latex

Subroto, Toto; Koningsveld, G.A. van; Schreuder, Herman; Soedjanaatmadja, Ukun M.S.; Beintema, Jaap J.

doi:10.1016/0031-9422(96)00196-3

Cited by 51 publications

(37 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Hevamine, a class III chitinase derived from the latex of H. brasiliensis, has a pI of 9.5 and an optimum pH of 4, and both antifungal activity and lysozyme activity. 6) GLx Chi-A did not exhibit lysozyme activity (data not shown). The characteristics of GLx Chi-A were very different from those of hevamine, despite being the same class chitinases in plant latex.…”

Section: Discussionmentioning

confidence: 86%

“…Papaya (Carica papaya) and rubber trees make latex and produce a large amount of chitinases in it. [4][5][6] Considering that several plant chitinases exhibit antifungal activity in vivo and/or in vitro, [7][8][9][10] chitinases in latex appear to play an important role in defense against fungal pathogens, but there is little information on the antifungal activity of chitinases in latex. We screened various tropical plants that produce latex for chitinase activity.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

Taira¹,

Ohdomari²,

Nakama³

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 86%

mentioning

confidence: 99%

Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

Taira¹,

Ohdomari²,

Nakama³

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…In fact, 1,3-␤-glucanases have been found in the latex of the rubber tree Hevea brasiliensis (40,64). They exhibited high capability to bind to IgE antibodies from the sera of patients that were allergic to latex and constitute the latex allergen Hev b 2 (65,66), which exhibited isoforms of 35-38 kDa and a basic pI (Ͼ10). Although food and latex allergens have different ways of access to hypersensitive patients by ingestion and direct contact, respectively, latex 1,3-␤-glucanases were found to be strongly recognized by IgE from sera of atopic subjects that were allergic to tomato, potato, and banana (66).…”

Section: Discussionmentioning

confidence: 99%

Ole e 9, a Major Olive Pollen Allergen Is a 1,3-β-Glucanase

Huecas

Villalba

Rodrı́guez

2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Olive pollen allergy is a clinical disorder affecting the human population of Mediterranean areas. A novel major allergen, Ole e 9, has been isolated from olive pollen by gel permeation, hydrophobic affinity, and reversephase high performance liquid chromatographies. It is involved in the allergic responses of 65% of patients suffering olive pollinosis. Ole e 9 (molecular mass of 46.4 kDa) displays 1,3-␤-endoglucanase activity (38.9 ؎ 5.6 mg of glucose released/min ؋ mol of protein at pH 4.5-6.0 using laminarin as substrate). It is the first 1,3-␤-glucanase, a member of the "pathogenesis-related" protein family, detected in pollen tissue. Seven tryptic peptides of the allergen were sequenced by Edman degradation and used for designing primers to clone the cDNA codifying the protein. Specific cDNA for Ole e 9 was synthesized from total RNA and amplified using the polymerase chain reaction. The allergen sequence showed an open reading frame of 460 amino acids comprising a putative signal peptide of 26 residues. It shows 39, 33, and 32% sequence identity including the catalytic residues when compared with 1,3-␤-glucanases from wheat, willow, and Arabidopsis thaliana, respectively. Northern blot analysis showed that Ole e 9 transcript is specifically expressed in the pollen tissue, and highly conserved counterparts were only detected in taxonomically related pollens.

show abstract

“…In addition to a wide range of lowmolecular-weight polypeptides (Nessler and Burnett, 1992;Azarkan et al, 2004), several other proteins and enzymes have been identified in the latices of laticiferous plants. These include the wound-induced proteins trypsin inhibitor, class II chitinase, and glutaminyl cyclase in the latex of papaya (Carica papaya; Azarkan et al, 2004) as well as chitinases and b-1,3-glucanase in the latex of the rubber tree Hevea brasiliensis (Martin, 1991;Subroto et al, 1996). The latex from some plants is a good source of natural rubber, and H. brasiliensis is widely cultivated for this purpose.…”

mentioning

confidence: 99%

Polyphenoloxidase Silencing Affects Latex Coagulation in Taraxacum Species

et al. 2009

View full text Add to dashboard Cite

Latex is the milky sap that is found in many different plants. It is produced by specialized cells known as laticifers and can comprise a mixture of proteins, carbohydrates, oils, secondary metabolites, and rubber that may help to prevent herbivory and protect wound sites against infection. The wound-induced browning of latex suggests that it contains one or more phenoloxidizing enzymes. Here, we present a comprehensive analysis of the major latex proteins from two dandelion species, Taraxacum officinale and Taraxacum kok-saghyz, and enzymatic studies showing that polyphenoloxidase (PPO) is responsible for latex browning. Electrophoretic analysis and amino-terminal sequencing of the most abundant proteins in the aqueous latex fraction revealed the presence of three PPO-related proteins generated by the proteolytic cleavage of a single precursor (pre-PPO). The laticifer-specific pre-PPO protein contains a transit peptide that can target reporter proteins into chloroplasts when constitutively expressed in dandelion protoplasts, perhaps indicating the presence of structures similar to plastids in laticifers, which lack genuine chloroplasts. Silencing the PPO gene by constitutive RNA interference in transgenic plants reduced PPO activity compared with wild-type controls, allowing T. kok-saghyz RNA interference lines to expel four to five times more latex than controls. Latex fluidity analysis in silenced plants showed a strong correlation between residual PPO activity and the coagulation rate, indicating that laticifer-specific PPO plays a major role in latex coagulation and wound sealing in dandelions. In contrast, very little PPO activity is found in the latex of the rubber tree Hevea brasiliensis, suggesting functional divergence of latex proteins during plant evolution.

show abstract

Chitinase and β-1,3-glucanase in the lutoid-body fraction of Hevea latex

Cited by 51 publications

References 21 publications

Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

Ole e 9, a Major Olive Pollen Allergen Is a 1,3-β-Glucanase

Polyphenoloxidase Silencing Affects Latex Coagulation in Taraxacum Species

Contact Info

Product

Resources

About