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Human Submandibular Saliva Inhibits Human Immunodeficiency Virus Type 1 Infection by Displacing Envelope Glycoprotein gp120 from the Virus
Author(s) -
Thandavarayan Nagashunmugam,
Daniel Malamud,
Cheryl Davis,
William R. Abrams,
Harvey M. Friedman
Publication year - 1998
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/314511
Subject(s) - saliva , glycoprotein , virus , infectivity , mucin , biology , centrifugation , virology , in vitro , agglutinin , submandibular gland , wheat germ agglutinin , viral envelope , microbiology and biotechnology , biochemistry , lectin , endocrinology
Human submandibular saliva reduces human immunodeficiency virus type 1 (HIV-1) infection in vitro. To define the mechanism of inhibition, virus was incubated with saliva or medium, velocity sucrose gradient centrifugation was performed, and fractions were analyzed for p24 and gp120. The results show that after incubation with saliva, the envelope glycoprotein was displaced from both a laboratory-adapted and a low-passage clinical HIV-1 isolate. To identify the salivary protein(s) responsible, submandibular saliva was fractionated by anion- exchange chromatography. Protein fractions containing anti-HIV activity were assayed for their ability to strip gp120 from virus. The partially purified active fractions contained two high-molecular-weight sialyated glycoproteins identified as salivary agglutinin and mucin, as well as several lower-molecular-weight proteins. It thus appears that specific salivary proteins interact with HIV-1 to strip gp120 from the virus with a resultant decrease in infectivity.

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