First Simultaneous Isolation of a Ribosome Inactivating Protein and an Antifungal Protein from a Mushroom (Lyophyllum shimeji) Together with Evidence for Synergism of their Antifungal Effects

Lam, Sze‐Kwan; Ng, T.B.

doi:10.1006/abbi.2001.2506

Cited by 155 publications

(88 citation statements)

References 30 publications

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“…RIPs also show synergistic effects with other antifungal proteins. For example, Lam and Ng [147] isolated a fungal RIP together with an antifungal protein and could show that the two proteins act synergistically.…”

Section: Ribosomesmentioning

confidence: 98%

Antifungal proteins: targets, mechanisms and prospective applications

Theis

Ståhl

2004

Cellular and Molecular Life Sciences (CMLS)

192

135

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All organisms have evolved several defence systems in order to protect themselves against bacteria, fungi and viruses. Higher organisms have developed a complex network of humoral and cellular responses, called adaptive immunity. A second defence system, innate immunity, was discovered in the early 1980s, consisting of small cationic peptides with a broad antimicrobial spectrum. These proteins act immediately at sites of infection or inflammation. The production of proteins with antimicrobial activity was not limited to higher organisms but was also found in insects, plants and microorganisms. During the last 2 decades a broad range of proteins with very different structural features have been isolated and characterised from differing organisms ranging from bacteria to human beings. Over 500 cationic membrane-acting proteins with antimicrobial and antifungal activities have been identified to date. Apart from these proteins, a very large number of antifungal proteins active on the fungal cell wall, on enzymes of the cell wall synthesis machinery, the plasma membrane and on intracellular targets have been characterised.

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Section: Ribosomesmentioning

confidence: 98%

Antifungal proteins: targets, mechanisms and prospective applications

Theis

Ståhl

2004

Cellular and Molecular Life Sciences (CMLS)

192

135

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“…A fixed amount (4 -6 ng) of recombinant HIV-1 reverse transcriptase was used. The inhibitory activity of the lectin was calculated as percent inhibition as compared to a control without the protein [26,27].…”

Section: Assay For Hiv-1 Reverse Transcriptase Inhibitory Activitymentioning

confidence: 99%

Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

Zhao

et al. 2011

J. Basic Microbiol.

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A thermostable novel lectin with a molecular weight of 30.4 kDa was isolated from dried fruiting bodies of Agaricus arvensis. It was a dimer made up of two 15.2 kDa subunits. The lectin was unadsorbed on DEAE-cellulose in 10 mM phosphate buffer (pH 7.5), subsequently adsorbed on CM-cellulose in 10 mM NaAc buffer (pH 4.6) and then on SP-Sepharose in 10 mM NaAc buffer (pH 4.6), and finally purified by fast protein liquid chromatography-gel filtration on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 90 °C. The activity was preserved in concentrations of NaOH solution up to 50 mM, but was sensitive to HCl and declined to 12.5% in 12.5 mM HCl. The activity was unaffected by Ca(2+), Mn(2+), Zn(2+) and Mg(2+) ions, but was activated by Al(3+) and Fe(3+) ions. Among the carbohydrates tested, only inulin could inhibit the hemagglutinating activity of the lectin. It did not exhibit anti-HIV reverse transcriptase activity. Proliferation of HepG2 and MCF7 tumor cells was inhibited by the lectin with an IC(50) of 1.64 and 0.82 μM, respectively. The lectin was devoid of antifungal activity. The lectin has a remarkable thermostablity and a unique N-terminal amino acid sequence, TYAVLNFVYG. The present report is the first report on a lectin from wild mushroom Agaricus arvensis.

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“…The ricin toxin A chain exhibited enzymatic activity toward the ribosomes from Rhizoctonia solani and Alternaria alternata in in vitro depurination assays (Park et al 2002). The Lyophyllum antifungal protein, a type 2 RIP from Lyophyllum shimeji (mushroom), demonstrated enzymatic activity to Physalospora piricola in an in vitro plate assay, with an IC50 of 70 nM (Lam and Ng 2001). However, this protein did not show any effect to Rhizoctonia solani, Colletotrichum gossypii, or Coprinus comatus.…”

Section: Antiviral Activity Of Type 2 Ripsmentioning

confidence: 96%

Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

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As part of their defense system different plant species each express a diverse set of defense proteins, among them proteins with lectin domains. The whole group of plant lectins assembles all proteins that have the ability to recognize and bind specific carbohydrate structures. Based on the sequence and the conformation of the carbohydrate recognition domains several lectin families are distinguished. Although many lectins are composed only of carbohydrate binding domains, several lectins are chimeric proteins composed of a lectin domain and another unrelated domain. In some cases this second domain can be considered as a toxin domain. This chapter focuses on different types of plant AB toxins and their physiological importance in the battle against pathogens and predators. Most information is available on type 2 ribosome-inactivating proteins in which an N-glycosidase domain is linked through a disulfide bridge to a lectin domain. More recently chimeric proteins consisting of one or more lectin domains and a dirigent domain or aerolysin domain have also been discovered. Although these AB toxins all consist of a lectin domain and a toxin domain, the nature of the toxin and the lectin domain are different resulting in proteins with different carbohydrate binding properties as well as a different mode of action for toxicity.

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First Simultaneous Isolation of a Ribosome Inactivating Protein and an Antifungal Protein from a Mushroom (Lyophyllum shimeji) Together with Evidence for Synergism of their Antifungal Effects

Cited by 155 publications

References 30 publications

Antifungal proteins: targets, mechanisms and prospective applications

Antifungal proteins: targets, mechanisms and prospective applications

Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

Plant AB Toxins with Lectin Domains

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