Acta Scientific Microbiology

Review Article Volume 7 Issue 8

Arthropod Derived Venoms: Natural Source of Anti-HIV Drug Molecules: A Review

Ravi Kant Upadhyay*

Department of Zoology, Deen Dayal Upadhyaya Gorakhpur University, Gorakhpur, U.P., India

*Corresponding Author: Ravi Kant Upadhyay, Department of Zoology, Deen Dayal Upadhyaya Gorakhpur University, Gorakhpur, U.P., India.

Received: June 26, 2024; Published: July 28, 2024

Abstract

Present review article describes venom derived toxins from various arthropods and their therapeutic uses against various virus pathogens of human diseases. Arthropods mainly bees, wasps, hornets, scorpions, spiders, ticks and marine arthropods synthesize toxins which possess unique functional groups and display target specific receptor binding on pathogen surface. These toxins exhibit cytolytic activity against moat of microbial pathogens and kill them by penetrating their cell membrane and inhibit major cellular functions through channel binding and receptor interactions. They inhibit virus entry into host cells, and obstruct HIV virus replication. These highly selective, powerful short toxin peptides show multiple biological activities and are of great therapeutic value. These could be used for creation of new target-specific novel antiviral medications of great therapeutic value. This is possible by utilizing the structural and functional diversity of toxin peptides through the application of bio-informatics tools, methodologies, and approaches. These low cost novel toxin-antibiotics can be used to manage various viral infections.

Keywords: Arthropods; Animal Venom Toxins; Defense Molecules; Anti-HIV Therapeutics

References

  1. Galvin SR and Cohen MS. “The role of sexually transmitted diseases in HIV transmission”. Nature Reviews Microbiology2 (2004): 33-42.
  2. Batorsky R., et al. “The route of HIV escape from immune response targeting multiple sites is determined by the cost-benefit trade off of escape mutations”. PLOS Computational Biology10 (2014): e1003878.
  3. Cohen MS., et al. “Prevention of HIV-1 infection with early antiretroviral therapy”. The New England Journal of Medicine 365 (2011): 493-505.
  4. Yaacoub C., et al. “Bee Venom and Its Two Main Components-Melittin and Phospholipase A2-As Promising Antiviral Drug Candidates”. Pathogens11 (2023): 1354.
  5. Dragic T., et al. “HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5”. Nature6584 (1996): 667-73.
  6. Zhou W., et al. “Antiviral activity and specific modes of action of bacterial prodigiosin against Bombyx mori nucleopolyhedrovirus in vitro”. Applied Microbiology and Biotechnology 100 (2016): 3979-3988.
  7. Prevot PP., et al. “Exosites Mediate the Anti-Inflammatory Effects of a Multifunctional Serpin From the Saliva of the Tick Ixodes Ricinus”. FEBS Journal12 (2009): 3235-3246.
  8. Carmo AC., et al. “Expression of an antiviral protein from Lonomia obliquehemolymph in baculovirus/insect cell system”. Antiviral Research 94 (2012): 126-130.
  9. Manjunatha GKS., et al. “Identification of In-Vitro Red Fluorescent Protein with Antipathogenic Activity from the Midgut of the Silkworm (Bombyx Mori L.)”. Protein and Peptide Letters 25 (2018): 302-313.
  10. Wang F., et al. “In vitro anti-influenza activity of a protein-enriched fraction from larvae of the housefly (Muscadomestica)”. Pharm Biology 51 (2013): 405-410.
  11. Nakazawa H., et al. “Antiviral activity of a serine protease from the digestive juice of Bombyxmori larvae against nucleopolyhedrovirus”.Virology 321 (2004): 154-162.
  12. Greco KN., et al. “Antiviral activity of the hemolymph of Lonomia obliqua (Lepidoptera: Saturniidae)”. Antiviral Research 84 (2009): 84-90.
  13. Liao HJ, et al. “Reversal of the antiviral activity of ribavirin against Sindbis virus in albopictus mosquito cells”. Antiviral Research 22 (1993): 285-294.
  14. Singh CP., et al. “Characterization of antiviral and antibacterial activity of Bombyx mori seroin proteins”. Cell Microbiology 16 (2014): 1354-1365.
  15. Carpena M., et al. “Bee Venom: An Updating Review of Its Bioactive Molecules and Its Health Applications”. Nutrients 12 (2020): 3360.
  16. Petricevich VL. “Scorpion venom and the inflammatory response”. Mediators Inflammatory (2010): 903295.
  17. Catterall WA. “Cellular and molecular biology of voltage-gated sodium channels”. Physiological Reviews 4 (1992): S15-S48.
  18. Marcotte P., et al. “Effects of Tityus serrulatus scorpion toxin γ on voltage-gated Na+channels”. Circulation Research 3 (1997): 363-369. 
  19. Ding J., et al. “Scorpion venoms as a potential source of novel cancer therapeutic compounds”. Experimental Biology and Medicine (Maywood) 239 (2014): 387-393.
  20. Silva EC., et al. “Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum”. Toxicon 54 (2009): 252-261.
  21. Sample CJ., et al. “A mastoparan-derived peptide has broad-spectrum antiviral activity against enveloped viruses”. Peptides 48 (2013): 96-105.
  22. Chen Y., et al. “Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7”. PLoS One 7 (2012): e34947.
  23. Couto J, et al. “Anti-plasmodial activity of tick defensins in a mouse model of malaria”. Ticks Tick Borne Disease 9 (2018): 844-849.
  24. Zabihollahi R., et al. “Venom Components of Iranian Scorpion Hemiscorpius lepturus Inhibit the Growth and Replication of Human Immunodeficiency Virus 1 (HIV-1)”. Iranian Biomedical Journal5 (2016): 259-265.
  25. Miller C., et al. “Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle”. Nature6000 (1985): 316-318.
  26. Chicchi GG., et al. “Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom”. Journal of Biological Chemistry21 (1988): 10192-7.
  27. Drakopoulou E., et al. “Engineering a CD4 mimetic inhibiting the binding of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein gp120 to human lymphocyte CD4 by the transfer of a CD4 functional site to a small natural scaffold”. Letters in Peptide Science2 (1998): 241-245.
  28. Li C., et al. “Phage randomization in a charybdotoxin scaffold leads to CD4-mimetic recognition motifs that bind HIV-1 envelope through non-aromatic sequences”. Journal of Peptide Research6 (2001): 507-18.
  29. Choi WT., et al. “Unique ligand binding sites on CXCR4 probed by a chemical biology approach: implications for the design of selective human immunodeficiency virus type 1 inhibitors”. Journal of Virology24 (2005): 15398-15404.
  30. Huang CC., et al. “Scorpion-toxin mimics of CD4 in complex with human immunodeficiency virus gp120 crystal structures, molecular mimicry, and neutralization breadth”. Structure5 (2005): 755-768.
  31. Chen Y., et al. “Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7”. PLoS One4 (2012): e34947.
  32. Li Q., et al. “Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses”. Peptides7 (2011): 1518-1525.
  33. Kwong PD., et al. “Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody”. Nature6686 (1998): 648-659.
  34. Hong W., et al. “Inhibitory activity and mechanism of two scorpion venom peptides against herpes simplex virus type 1”. Antiviral Research 102 (2014): 1-10.
  35. Ojeda PG., et al. “Chlorotoxin: structure, activity, and potential uses in cancer therapy”. Biopolymers1 (2016): 25-36.
  36. Uddin MB., et al. “Inhibitory effects of bee venom and its components against viruses in vitro and in vivo”. Journal of Microbiology 54 (2016): 853-866.
  37. Lee WR., et al. “The protective effects of melittin on Propionibacterium acnes-induced inflammatory responses in vitro and in vivo”. Journal of Investigative Dermatology 134 (2014): 1922-1930.
  38. Sarhan M, et al. “Potent virucidal activity of honeybee Apismellifera" venom against Hepatitis C Virus”. Toxicon 188 (2020): 55-64.
  39. Goswami S and Chowdhury JP. “Antiviral attributes of bee venom as a possible therapeutic approach against SARS-CoV-2 infection”. Future Virology (2023): 10.2217/fvl-2023-0127.
  40. Cortegiani A., et al.“A systematic review on the efficacy and safety of chloroquine for the treatment of COVID-19”. Journal of Critical Care 57 (2020): 279-283
  41. Baghian A and Kousoulas KG. “Role of the Na+,K+pump in herpes simplex type 1-induced cell fusion: melittin causes specific reversion of syncytial mutants with the syn1 mutation to syn+ (wild-type) phenotype”. Virology 2 (1993): 548-556.
  42. Yasin B., et al. “Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides”. European Journal of Clinical Microbiology and Infectious Diseases 3 (2000): 187-194.
  43. Baghian A., et al. “An amphipathic alpha-helical synthetic peptide analogue of melittin inhibits herpes simplex virus-1 (HSV-1)-induced cell fusion and virus spread”. Peptides 18 (1997): 177-183.
  44. Wachinger M., et al. “Influence of amphipathic peptides on the HIV-1 production in persistently infected T lymphoma cells”. FEBS Letter 309 (1992): 235-241.
  45. Memariani H., et al. “Melittin: a venom-derived peptide with promising anti-viral properties”. European Journal of Clinical Microbiology and Infectious Diseases1 (2020): 5-17.
  46. Fenard D., et al. “A peptide derived from bee venom-secreted phospholipase A2 inhibits replication of T-cell tropic HIV-1 strains via interaction with the CXCR4 chemokine receptor”. Molecular Pharmacology2 (2000): 341-347.
  47. Hirai Y., et al. “A new mast cell degranulating peptide “mastoparan” in the venom of Vespula lewisii”. Chem Pharm Bull (Tokyo).8 (1979): 1942-1944.
  48. Leite NB., et al. “The effect of acidic residues and amphipathicity on the lytic activities of mastoparan peptides studied by fluorescence and CD spectroscopy”. Amino Acids1 (2011): 91-100.
  49. Marcos JF., et al. “Inhibition of a plant virus infection by analogs of melittin”. Proceedings of the National Academy of Sciences (PNAS) 92.26 (1995): 12466-12469.
  50. Bachis A., et al. “M-tropic HIV envelope protein gp120 exhibits a different neuropathological profile than T-tropic gp120 in rat striatum”. European Journal of Neuroscience4 (2010): 570-578.
  51. Fenard D., et al. “Secreted phospholipases A (2), a new class of HIV inhibitors that block virus entry into host cells”. Journal of Clinical Investigation5 (1999): 611-618.
  52. Wickline SA., et al. “Nanoparticulate-based contraceptive/anti-HIV. Composition and methods”. 2012. Patent US20120100186 A1. Washington University (2012).
  53. Moreno M, Giralt E. “Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: melittin, apamin and mastoparan”. Toxins (Basel)4 (2015): 1126-1150.
  54. de Azevedo RA., et al. “Mastoparan induces apoptosis in B16F10-Nex2 melanoma cells via the intrinsic mitochondrial pathway and displays antitumor activity in vivo”. Peptides 68 (2015):
  55. Higashijima T., et al. “Mastoparan, a Peptide Toxin from Wasp Venom, Mimics Receptors by Activating GTP-binding Regulatory Proteins (G Proteins)”. The Journal of Biological Chemistry14 (1988): 6491-6494.
  56. Rocha T., et al. “Myotoxic Effects of Mastoparan from Polybia paulista (Hymenoptera, Epiponini) Wasp Venom in Mice Skeletal Muscle”. Toxicon 50 (2007): 589-599.
  57. Rivers DB., et al. “Venom from the Ectoparasite Wasp Nasonia vitripennis Increases Na+ Influx and Activates Phospholipase C and Phospholipase A2 De‐ pendent Signal Transduction Pathways in Cultured Insect Cells”. Toxicon 40 (2002): 9.
  58. Hirata Y., et al. “Identification of a 97-kDa mastoparan-binding protein involving in Ca (2+) release from skeletal muscle sarcoplasmic reticulum”. Molecular Pharmacology 57 (2000): 1235-1242.
  59. Hirata Y., et al. “Mastoparan binds to glycogen phosphorylase to regulate sarcoplasmic reticular Ca2+ release in skeletal muscle”. Biochemistry Journal (2003);371 (Pt 1): 81-8.
  60. Karst H., et al. “Philanthotoxin inhibits Ca2+ currents in rat hippocampal CA1 neurons”. European Journal of Pharmacology 270 (1994): 357-360.
  61. Chahdi A., et al. “Mastoparan Selectively Activates Phospholipase D2 in Cell Membranes”. The Journal of Biological Chemistry 278 (2003): 12039-12045.
  62. Jones D., et al. “Phospholipase D and Membrane Traffic: Potential Roles in Regulated Exocytosis, Membrane Delivery and Vesicle Budding”. Biochimica et Biophysica Acta 1439 (1999): 229-244.
  63. Duncan AM., et al. “Kinins in Humans”. American Journal of Physiology—Regulatory, Integrative and Comparative Physiology 278 (2000): R897-904.
  64. Akef HM. “Anticancer, antimicrobial, and analgesic activities of spider venoms”. Toxicology Research (Camb).3 (2018): 381-395.
  65. Vassilevski AA., et al. “Molecular diversity of spider venom”. Biochemistry (Mosc)13 (1999): 1505-1534.
  66. Ji M., et al. “An Antiviral Peptide from Alopecosa nagpagSpider Targets NS2B-NS3 Protease of Flaviviruses”. Toxins (Basel)10 (2019): 584.
  67. Liang S. “An overview of peptide toxins from the venom of the Chinese bird spider Selenocosmia huwena Wang [=Ornithoctonus huwena (Wang)]”. Toxicon5 (2004): 575-585.
  68. Peng K., et al. “Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena”. Journal of Biological Chemistry49 (2002): 47564-47571.
  69. Rothan HA., et al. “Inhibitory effects of a peptide-fusion protein (Latarcin-PAP1-Thanatin) against chikungunya virus”. Antiviral Research 1 (2014): 173-180. 
  70. Sukmarini, L. “Antiviral Peptides (AVPs) of Marine Origin as Propitious Therapeutic Drug Candidates for the Treatment of Human Viruses”. Molecules27 (2022):
  71. Ford PW., et al. “Papuamides A-D, “HIV-inhibitory and cytotoxic depsipeptides from the sponges Theonella mirabilis and Thenonella swinhoei collected in Papua New Guinea”. Journal of the American Chemical Society 121 (1999): 5899-5909.
  72. Manohar M., et al. “Silver Nanoparticle Conjugated Marine Invertebrate Antimicrobial Peptides (AgNPs-Amps) against Gram-Negative ESKAPE Pathogens”. International Journal of Research and Analytical Reviews 6 (2019): 264-287.
  73. Mengyao Ji., et al. “An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B-NS3 Protease of Flaviviruses”. Toxins10 (2019): 584.

Citation

Citation: Ravi Kant Upadhyay. “Arthropod Derived Venoms: Natural Source of Anti-HIV Drug Molecules: A Review".Acta Scientific Microbiology 7.8 (2024): 165-176.

Copyright

Copyright: © 2024 Ravi Kant Upadhyay. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.




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