LALLT (Loxosceles Allergen-Like Toxin) from the venom of Loxosceles intermedia: Recombinant expression in insect cells and characterization as a molecule with allergenic properties

Prospective Use of Brown Spider Venom Toxins as Therapeutic and Biotechnological Inputs

“…The sera of horses that received only rCpLi on immunizations performed around 50% of reduction in dermonecrosis (Figueiredo et al, 2014). As mentioned earlier, loxoscelic venoms have other proteins that play a role in loxoscelism, i.e., metalloproteinases, serine proteases, hyaluronidases, TCTP and allergens (Feitosa et al, 1998;Veiga et al, 2000;Da Silveira et al, 2007;Trevisan-Silva et al, 2010;Ferrer et al, 2013;Justa et al, 2020;De-Bona et al, 2021). Thus, the inclusion of these toxins in the production of sera turns out to be a strategy to enhance the efficacy of antivenoms.…”

“…A Translationally Controlled Tumor Protein (TCTP) is also part of the venom, and acts as a histamine-releasing factor. Together with an allergen from the cysteine-rich secretory protein (CRISP) family, TCTP contributes to the allergic and inflammatory response of cutaneous loxoscelism (Sade et al, 2012;Boia-ferreira et al, 2019;Justa et al, 2020). A serine protease inhibitor from the Serpin superfamily was also described in a Loxosceles venom and, although its role as a toxin remains to be elucidated, the biological activities of this inhibitor indicate a great potential for drug development (Graeff et al, 2019).…”

“…General data acquired from venom gland transcriptomes and venom proteomes elucidated the toxins' expression profile of many Loxosceles species (Machado et al, 2005;Fernandes-Pedrosa et al, 2008;Dos Santos et al, 2009;Gremski et al, 2010;Trevisan-Silva et al, 2017;Calabria et al, 2019). In addition, these screening efforts allowed the description of coding sequences of less expressed toxins, which enabled the production of these molecules as recombinant proteins (Sade et al, 2012;Ferrer et al, 2013;Graeff et al, 2019;Justa et al, 2020;De-Bona et al, 2021). In fact, some toxins, such as wild-type and mutated/inactive phospholipases D and astacin-like metalloproteases were recombinantly expressed before the first screening reports (Fernandes Pedrosa et al, 2002;Kalapothakis et al, 2002;Chaim et al, 2006;Da Silveira et al, 2007;Kusma et al, 2008).…”

“…In fact, some toxins, such as wild-type and mutated/inactive phospholipases D and astacin-like metalloproteases were recombinantly expressed before the first screening reports (Fernandes Pedrosa et al, 2002;Kalapothakis et al, 2002;Chaim et al, 2006;Da Silveira et al, 2007;Kusma et al, 2008). However, the production of other recombinant proteins, i.e., hyaluronidases, TCTP, ICK peptides, allergen and serpin, was only possible after the initial descriptions of their coding sequences (Sade et al, 2012;Ferrer et al, 2013;Matsubara et al, 2017;Graeff et al, 2019;Justa et al, 2020). Recombinant chimeric proteins consisting of Loxosceles toxins' epitopes were also produced (Mendes et al, 2013;Lima et al, 2018;Souza et al, 2018;Calabria et al, 2019).…”

“…Recombinant chimeric proteins consisting of Loxosceles toxins' epitopes were also produced (Mendes et al, 2013;Lima et al, 2018;Souza et al, 2018;Calabria et al, 2019). The expression model differs for each recombinant Loxosceles toxin since some of them are produced as soluble and active proteins by prokaryotic expression systems, while others require a more complex model to achieve the desired production protocol (Boia-ferreira et al, 2019;Graeff et al, 2019;Gremski et al, 2020;Justa et al, 2020;De-Bona et al, 2021). As the purification of toxins from Brown spider venoms usually yields tiny amounts of proteins, the production of recombinant toxins allowed their further characterization.…”