Vol. 7 No. 2 (2004)
Narrative Review

An Evaluation of Human Immunodeficiency Virus Pathogenicity and Treatment Using Glycobiology

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  • Aleksandra M. Leligdowicz
Aleksandra M. Leligdowicz
McGill University Faculty of Medicine
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DOI: https://doi.org/10.26443/mjm.v7i2.784

Published 2020-12-01

Keywords

  • Human Immunodeficiency Virus,
  • Glycobiology,
  • HIV,
  • Therapy

How to Cite

1.
Leligdowicz AM. An Evaluation of Human Immunodeficiency Virus Pathogenicity and Treatment Using Glycobiology. McGill J Med [Internet]. 2020 Dec. 1 [cited 2025 Oct. 6];7(2). Available from: https://mjm.mcgill.ca/article/view/784
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References

  1. International AIDS Vaccine Initiative. http://iavi.org ; 2002.
  2. Bloom, DE. Something to be done: treating HIV/AIDS. River Path Associates. Science 288(5474):2171-3; 2000. 3. Ratner L. Glucosidase Inhibitors for Treatment of HIV-1 Infection. Aids Research and Human Retroviruses 8:165-173; 1992.
  3. Lehninger Albert L, Nelson David L, Cox Michael M. Principles of Biochemistry, 2nd edition. New York, NY: Worth Publishers, 1993.
  4. Gilbert PB, McKeague IW, Eisen G, Mullins C, Gueye-NDiaye A, Mboup S, Kanke PJ. Comparison of HIV-1 and HIV-2 Infectivity from a prospective cohort study in Senegal. Statist. Med 22:573-593; 2003.
  5. Pal R, Hoke, GM, Sarngadharan MG. Role of gp41 Glycosylation Sites in the Biological Activity of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein. Virology 242:338-345; 1998.
  6. Biller M, Bolmstedt A, Hemming A, Olofsson S. Simplified procedure for fractionation and structural characterization of complex mixtures of N-linked glycans, released from HIV-1 gp120 and other highly glycosylated viral proteins. J Virol Methods 76:87-100; 1998.
  7. Botarelli P, Houlden BA, Haigwood NL, Servis C, Montagna D, Abrignani S. N-glycosylation of HIV-gp120 may constrain recognition by T lymphocytes. J Immunol 147:3128-3132; 1991.
  8. Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M. Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. J Acquir Immune Defic Syndr 2:163-169; 1989.
  9. AVERT, AIDS Virus Education and Research Trust. www.avert.org/virus.htm ; 2002.
  10. Howard Hughes Medical Institute. Key HIV Protein Structure Solved. http://www.hhmi.org/news/keyhiv.html ; 1997.
  11. Zhu X, Borchers C, Bienstock RJ, Tomer KB. Mass Spectrometric Characterization of the Glycosylation Pattern of HIV-gp120 Expressed in CHO Cells. Biochemistry 9:11195;11204; 2000.
  12. Mizuochi T, Matthews TJ, Kato M., Hamako J, Titani K, Solomon J, Feizi T. Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N- acetylglucosamine residues. J Biol Chem 265:8519-8524; 1990.
  13. Fenouillet E, Jones I, Powell B, Schmitt D, Kieny MP, Gluckman JC. Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain. J Viro, 67:150-160; 1993.
  14. Pal R, Hoke GM, Sarngadharan MG. The role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 86:3384-3388; 1989.
  15. De Clercq E. New developments in anti-HIV chemotherapy. Curr Med Chem 8:1543-72; 2001.
  16. Tierney M, Pottage J, Kessler H, et al. The tolerability and pharmacokinetics of N-butyl-deoxynojirimycin in patients with advanced HIV disease (ACTG 100). The AIDS Clinical Trials Group (ACTG) of the National Institute of Allergy and Infectious Diseases. J Acquir Immune Defic Syndr Hum Retrovirol 10:549-553; 1995.
  17. Bewley CA, Otero-Quintero S. The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120. J Am Chem Soc 123:38923-902; 2001.
  18. Bolmstedt AJ, O'Keefe BR, Shenoy SR McMahon JB, Boyd MR. Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner. Mol Pharmacol 59:949-954; 2001.
  19. Mizuochi T, Nakata M. New anti-HIV drug which binds the oligosaccharides of HIV envelope glycoprotein. Nippon Rinsho 53:2340-2349;1995.
  20. Manca F. Galactose receptors and presentation of HIV envelope glycoprotein to specific human T cells. J Immunol 148:2278- 2282; 1992.
  21. Newburg DS, Linhardt RJ, Ampofo SA, Yolken RH Human Milk Glycosaminoglycans Inhibit HIV Glycoprotein gp120 Binding to Its Host Cell CD4 Receptor. J Ntr 125:419-423; 1995.
  22. Medical microbiology, Glycosaminoglycans. http://www.indstate.edu/thcme/mwking/glycans.html ; 2001.