Molecular cloning of toxins expressed by the venom gland of Lasiodora sp.

Vieira, André Luiz Gomes; Moura, Miguel; Baba, Elio H.; Chávez-Olórtegui, Carlos; Kalapothakis, Evanguedes; Castro, Ieso de Miranda

doi:10.1016/j.toxicon.2004.08.004

Cited by 12 publications

(7 citation statements)

References 11 publications

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“…The current literature includes studies about the toxins in Lasiodora sp. venom [49][50][51], but no investigation on serine protease inhibitors in hemocytes has been reported. EILaH is the first elastase inhibitor with bacteriostatic activity isolated from hemolymph cells of Lasiodora sp.…”

Section: Discussionmentioning

confidence: 99%

The first serine protease inhibitor from Lasiodora sp. (Araneae: Theraphosidae) hemocytes

Soares

Ferreira

Gomes

et al. 2011

Process Biochemistry

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This work reports, for the first time, the purification, characterization and antibacterial activity of an elastase inhibitor from Lasiodora sp. hemocytes (EILaH). The hemocyte extract inhibited chymotrypsin (22%), trypsin (44%), tissue plasminogen activator (52%), urokinase (58%) and human neutrophil elastase (99%). EILaH was purified by Trypsin-Sepharose column and RP-HPLC. SDS-PAGE of EILaH revealed a molecular mass of 8 kDa and MALDI-TOF mass spectrometry revealed a single molecular mass of 8274 Da. The amino terminal sequence determined was LPC(PF)PYQQELTC. The dissociation constant (K i) for human neutrophil elastase was 0.32 nM. Hemocyte extract exerted antibacterial effect on Bacillus subtilis and Enterococcus faecalis, while EILaH was only active against E. faecalis. Currently, Lasiodora sp. is undergoing a systematic review and this study contributes to molecular characterization of the genus. In addition, the results suggest that serine protease inhibitors expressed in Lasiodora sp. hemocytes may be involved in the defense against bacterial infection.

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Section: Discussionmentioning

confidence: 99%

The first serine protease inhibitor from Lasiodora sp. (Araneae: Theraphosidae) hemocytes

Soares

Ferreira

Gomes

et al. 2011

Process Biochemistry

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“…In 2004, Vieira et al [46] described LTx1, LTx2, and LTx3 (Table 1) from a Lasiodora sp. venom gland cDNA library.…”

Section: Lasiodora Spmentioning

confidence: 99%

Brazilian Theraphosidae: a toxicological point of view

Macedo

Costa

Souza

et al. 2021

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Spiders very commonly express many paralogues of each toxin. For example, Vieira et al (2004) reported three cysteine-rich peptides (LTx1, LTx2 and LTx3) in the venom gland of tarantula Lasiodora sp. that differ from each other in only one to three amino acid residues.…”

Section: Knottin Peptides In Other Loxosceles Speciesmentioning

confidence: 99%

Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus

Matsubara

Meissner

Herzig

et al. 2016

Insect Molecular Biology

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Loxosceles intermedia venom comprises a complex mixture of proteins, glycoproteins and low molecular mass peptides that act synergistically to immobilize envenomed prey. Analysis of a venom-gland transcriptome from L. intermedia revealed that knottins, also known as inhibitor cystine knot peptides, are the most abundant class of toxins expressed in this species. Knottin peptides contain a particular arrangement of intramolecular disulphide bonds, and these peptides typically act upon ion channels or receptors in the insect nervous system, triggering paralysis or other lethal effects. Herein, we focused on a knottin peptide with 53 amino acid residues from L. intermedia venom. The recombinant peptide, named U -sicaritoxin-Li1b (Li1b), was obtained by expression in the periplasm of Escherichia coli. The recombinant peptide induced irreversible flaccid paralysis in sheep blowflies. We screened for knottin-encoding sequences in total RNA extracts from two other Loxosceles species, Loxosceles gaucho and Loxosceles laeta, which revealed that knottin peptides constitute a conserved family of toxins in the Loxosceles genus. The insecticidal activity of U -SCTX-Li1b, together with the large number of knottin peptides encoded in Loxosceles venom glands, suggests that studies of these venoms might facilitate future biotechnological applications of these toxins.

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Molecular cloning of toxins expressed by the venom gland of Lasiodora sp.

Cited by 12 publications

References 11 publications

The first serine protease inhibitor from Lasiodora sp. (Araneae: Theraphosidae) hemocytes

The first serine protease inhibitor from Lasiodora sp. (Araneae: Theraphosidae) hemocytes

Brazilian Theraphosidae: a toxicological point of view

Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus

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