Document 0075
 DOCN  M9480075
 TI    Alkaloidal glycosidase inhibitors (AGIs) as the cause of sporadic
       scrapie, and the potential treatment of both transmissible spongiform
       encephalopathies (TSEs) and human immunodeficiency virus (HIV)
       infection.
 DT    9410
 AU    Dealler S; York District Hospital Microbiology Department, UK.
 SO    Med Hypotheses. 1994 Feb;42(2):69-75. Unique Identifier : AIDSLINE
       MED/94293839
 AB    AGIs are produced by plants and microorgansims in the environment. They
       are absorbed from the gut, distributed throughout the body and are
       concentrated inside cells. AGIs alter the glycan chains of cellular
       glycoproteins (CGP) during their formation so that the same CGP produced
       by different clones of cells (and hence with different glycan chains)
       becomes structurally the same. Prion protein (PrP), a CGP, is rendered
       indestructable to cellular mechanisms (as PrPi) by the TSE infective
       process; it is suggested that AGIs could both cause and prevent this by
       altering the primary structure of PrP. HIV envelope protein, gp120,
       carries glycan chains that are decided by the clone of the cells by
       which it is produced. Each cellular clone would be expected to add a
       specific group of glycan chains, making the gp120 antigenically
       separate. As HIV infection progresses, infected clone numbers rise, the
       antigenic diversity of gp120 may rise as would antibody production,
       trying to keep pace. Antigenically stimulated CD4+ cells carrying HIV
       genes, increase HIV production with gp120 antigenically different from
       its stimulant. AGIs prevent the glycan diversity and may prevent the
       extension of HIV infection.
 DE    Alkaloids/*PHARMACOLOGY  Animal  Antigenic Variation/DRUG EFFECTS
       Creutzfeldt-Jakob Syndrome/ETIOLOGY  Glycoside Hydrolases/*ANTAGONISTS &
       INHIB  Glycosylation  Human  HIV Envelope Protein
       gp120/IMMUNOLOGY/METABOLISM  HIV Infections/DRUG THERAPY
       HIV-1/IMMUNOLOGY  Models, Biological  Prion Diseases/DRUG THERAPY
       Prions/CHEMISTRY/METABOLISM  Scrapie/*ETIOLOGY  JOURNAL ARTICLE  REVIEW
       REVIEW, TUTORIAL

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).