Hydra actinoporin-like toxin-1, an unusual hemolysin from the nematocyst venom of Hydra magnipapillata which belongs to an extended gene family

Glasser, Eliezra; Rachamim, Tamar; Aharonovich, Dikla; Sher, Daniel

doi:10.1016/j.toxicon.2014.04.004

Cited by 30 publications

(53 citation statements)

References 65 publications

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“…Although HALT-1 is structurally similar to other actinoporins, a recent study showed that this toxin produced a different pore size from EqtII and did not use sphingomyelin as membrane target (Glasser et al 2014). These findings may not be surprising, since HALT-1 and EqtII share only 30% similarity in protein sequence and several amino acid residues known to be involved in sphingomyelin binding in equinatoxin and sticholysin are not conserved in HALT-1 (Liew et al 2015).…”

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

“…For example, six Hydra actinoporin-like toxins (HALTs) were identified in the genome of Hydra magnipapillata (Glasser et al 2014). The amino acid sequences of these toxins share 30% identity with those of actinoporins from sea anemones (Glasser et al 2014). In addition, HALT-1 showed haemolytic and cytolytic activity towards red blood cells and HeLa cells (Glasser et al 2014;Liew et al 2015).…”

Section: Introductionmentioning

confidence: 99%

“…The amino acid sequences of these toxins share 30% identity with those of actinoporins from sea anemones (Glasser et al 2014). In addition, HALT-1 showed haemolytic and cytolytic activity towards red blood cells and HeLa cells (Glasser et al 2014;Liew et al 2015). HALT-1 has a conserved cluster of aromatic amino acids and an amphiphilic N-terminus, which are proposed to play important roles in membrane binding and pore formation, respectively (Liew et al 2015).…”

Section: Introductionmentioning

confidence: 99%

“…Since the attempt to show sphingomyelin as an important membrane target site for HALT-1 was not successful (Glasser et al 2014) and there has been no information on membrane protein binding, we used a combination of GST affinity purification and SILAC based quantitative mass spectrometry to identify potential membrane proteins that bind to HALT-1.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1) using GST affinity purification and SILAC-based quantitative proteomics

Ameirika

Hong

Hwang

2017

Toxicon

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Hydra actinoporin-like toxin-1 (HALT-1) is a 20.8 kDa pore-forming toxin isolated from Hydra magnipapillata. HALT-1 shares structural similarity with actinoporins, a family that is well known for its haemolytic and cytolytic activity. However, the precise pore-forming mechanism of HALT-1 remains an open question since little is known about the specific target binding for HALT-1. For this reason, a comprehensive proteomic analysis was performed using affinity purification and SILAC-based mass spectrometry to identify potential protein-protein interactions between mammalian HeLa cell surface proteins and HALT-1. A total of 4 mammalian proteins was identified, of which only folate receptor alpha was further verified by ELISA. Our preliminary results highlight an alternative-binding mode of HALT-1 to the human plasma membrane. This is the first evidence showing that HALT-1, an actinoporin-like protein, binds to a membrane protein, the folate receptor alpha. This study would advance our understanding of the molecular basis of toxicity of pore-forming toxins and provide new insights in the production of more potent inhibitors for the toxin-membrane receptor interactions.3

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1) using GST affinity purification and SILAC-based quantitative proteomics

Ameirika

Hong

Hwang

2017

Toxicon

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Structures and functions of the membrane-damaging pore-forming proteins

Mondal¹,

Chattopadhyay²

2022

Advances in Protein Chemistry and Structural Biology

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Pore-forming toxins: Properties, diversity, and uses as tools to image sphingomyelin and ceramide phosphoethanolamine

Yamaji‐Hasegawa¹,

Hullin-Matsuda²,

Greimel³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Pore-forming toxins (PFTs) represent a unique class of highly specific lipid-binding proteins. The cytotoxicity of these compounds has been overcome through crystallographic structure and mutation studies, facilitating the development of non-toxic lipid probes. As a consequence, non-toxic PFTs have been utilized as highly specific probes to visualize the diversity and dynamics of lipid nanostructures in living and fixed cells. This review is focused on the application of PFTs and their non-toxic analogs as tools to visualize sphingomyelin and ceramide phosphoethanolamine, two major phosphosphingolipids in mammalian and insect cells, respectively. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.

show abstract

Hydra actinoporin-like toxin-1, an unusual hemolysin from the nematocyst venom of Hydra magnipapillata which belongs to an extended gene family

Cited by 30 publications

References 65 publications

Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1) using GST affinity purification and SILAC-based quantitative proteomics

Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1) using GST affinity purification and SILAC-based quantitative proteomics

Structures and functions of the membrane-damaging pore-forming proteins

Pore-forming toxins: Properties, diversity, and uses as tools to image sphingomyelin and ceramide phosphoethanolamine

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