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

V.21, 2015.

Review article - ISSN 1678-9199.

 

Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology

 
Karla C F Bordon1, Gisele A. Wiezel1, Fernanda G. Amorim1, Eliane C. Arantes1 

1 Department of Physics and Chemistry, School of Pharmaceutical Sciences of Ribeirão Preto, University of São Paulo (USP), Avenida do Café, s/n, Ribeirão Preto 14.040-903, SP, Brazil

 

ABSTRACT

Hyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications.

 

Key words: Hyaluronidase; Scorpion; Spider; Caterpillar; Hymenoptera; Insects; Cloning; Heterologous expression; PEGylation; Biotechnological applications

 

Received: February 2, 2015; Revised: October 8, 2015; Accepted: October 22, 2015

 

Corresponding author: Eliane C Arantes ecabraga@fcfrp.usp.br

 

Competing interests

The authors declare that they have no competing interests.

 

Authors' contributions

KCFB and ECA are the designers of the review. KCFB, GAW and FGA drafted the manuscript. ECA is the corresponding author and supervised and critically discussed the review. All authors read and approved the final manuscript.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.