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

Author

Luiza Helena Gremski, Fernando Hitomi Matsubara, Nayanne Louise Costacurta Polli, Bruno Cesar Antunes, Pedro Henrique de Caires Schluga, Hanna Câmara da Justa, João Carlos Minozzo, Ana Carolina Martins Wille, Andrea Senff-Ribeiro, and Silvio Sanches Veiga

Subjects
Loxosceles, proteins, peptides, recombinant proteins, venom, Biology (General), QH301-705.5
Abstract

Brown spider (genus Loxosceles) venoms are mainly composed of protein toxins used for predation and defense. Bites of these spiders most commonly produce a local dermonecrotic lesion with gravitational spread, edema and hemorrhage, which together are defined as cutaneous loxoscelism. Systemic loxoscelism, such as hematological abnormalities and renal injury, are less frequent but more lethal. Some Loxosceles venom toxins have already been isolated and extensively studied, such as phospholipases D (PLDs), which have been recombinantly expressed and were proven to reproduce toxic activities associated to the whole venom. PLDs have a notable potential to be engineered and converted in non-toxic antigens to produce a new generation of antivenoms or vaccines. PLDs also can serve as tools to discover inhibitors to be used as therapeutic agents. Other Loxosceles toxins have been identified and functionally characterized, such as hyaluronidases, allergen factor, serpin, TCTP and knottins (ICK peptides). All these toxins were produced as recombinant molecules and are biologically active molecules that can be used as tools for the potential development of chemical candidates to tackle many medical and biological threats, acting, for instance, as antitumoral, insecticides, analgesic, antigens for allergy tests and biochemical reagents for cell studies. In addition, these recombinant toxins may be useful to develop a rational therapy for loxoscelism. This review summarizes the main candidates for the development of drugs and biotechnological inputs that have been described in Brown spider venoms.

Published
2021
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2. Recombinant Protein Containing B-Cell Epitopes of Different Loxosceles Spider Toxins Generates Neutralizing Antibodies in Immunized Rabbits

Author

Carlos Chávez-Olórtegui, Sabrina de Almeida Lima, Silvio Sanches Veiga, João Carlos Minozzo, Dilza Trevisan-Silva, T.M. Mendes, Clara Guerra-Duarte, Luís F.M. Figueiredo, Fernanda Costal-Oliveira, Ricardo Andrez Machado de Ávila, Evanguedes Kalapothakis, Daysiane de Oliveira, and Valéria Pereira Ferrer

Subjects
0301 basic medicine, lcsh:Immunologic diseases. Allergy, multiepitopic recombinant protein, Immunogen, Spider Venoms, Antivenom, Immunology, Venom, Biology, complex mixtures, Epitope, Microbiology, 03 medical and health sciences, Antigen, sphingomyelinase D, medicine, Immunology and Allergy, Animals, Original Research, Mice, Inbred BALB C, 030102 biochemistry & molecular biology, Linear epitope, astacin-like metalloprotease hyaluronidase, Phosphoric Diester Hydrolases, medicine.disease, B-cell epitope, Antibodies, Neutralizing, Loxoscelism, Recombinant Proteins, 030104 developmental biology, Loxosceles spider venom, Epitopes, B-Lymphocyte, Female, Immunization, Rabbits, lcsh:RC581-607
Abstract

Loxoscelism is the most important form of araneism in South America. The treatment of these accidents uses heterologous antivenoms obtained from immunization of production animals with crude loxoscelic venom. Due to the scarcity of this immunogen, new alternatives for its substitution in antivenom production are of medical interest. In the present work, three linear epitopes for Loxosceles astacin-like protease 1 (LALP-1) (SLGRGCTDFGTILHE, ENNTRTIGPFDYDSIMLYGAY, and KLYKCPPVNPYPGGIRPYVNV) and two for hyaluronidase (LiHYAL) (NGGIPQLGDLKAHLEKSAVDI and ILDKSATGLRIIDWEAWR) from Loxosceles intermedia spider venom were identified by SPOT-synthesis technique. One formerly characterized linear epitope (DFSGPYLPSLPTLDA) of sphingomyelinase D (SMase D) SMase-I from Loxosceles laeta was also chosen to constitute a new recombinant multiepitopic protein. These epitopes were combined with a previously produced chimeric multiepitopic protein (rCpLi) composed by linear and conformational B-cell epitopes from SMase D from L. intermedia venom, generating a new recombinant multiepitopic protein derived from loxoscelic toxins (rMEPLox). We demonstrated that rMEPLox is non-toxic and antibodies elicited in rabbits against this antigen present reactivity in ELISA and immunoblot assays with Brazilian L. intermedia, L. laeta, L. gaucho, and L. similis spider venoms. In vivo and in vitro neutralization assays showed that anti-rMEPLox antibodies can efficiently neutralize the sphingomyelinase, hyaluronidase, and metalloproteinase activity of L. intermedia venom. This study suggests that this multiepitopic protein can be a suitable candidate for experimental vaccination approaches or for antivenom production against Loxosceles spp. venoms.

Published
2018

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