• Login
    View Item 
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Human Milk Glycosaminoglycans Inhibit HIV Glycoprotein GP120 Binding to Its Host Cell CD4 Receptor

    Author
    Newburg, D.S.; Linhardt, Robert J.; Ampofo, S.A.; Yolken, R.H.
    ORCID
    https://orcid.org/0000-0003-2219-5833
    Thumbnail
    Other Contributors
    Date Issued
    1995
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    Human Milk Glycosaminoglycans Inhibit HIV Glycoprotein GP120 Binding to Its Host Cell CD4 Receptor D.S. Newburg, R.J. Linhardt, S.A. Ampofo, R.H. Yolken, Journal of Nutrition, 125, 419-424, 1995.
    Metadata
    Show full item record
    URI
    https://doi.org/10.1093/jn/125.3.419; https://hdl.handle.net/20.500.13015/5959
    Abstract
    The binding of the HIV envelope glycoprotein, gp120, to its host cell receptor, CD4, is inhibited in a solid phase assay by a glycosaminoglycan of human milk; this binding is the essential first step in HIV infectivity. The human milk glycosaminoglycans were identified in this study. Pooled, fractionated human milk contained dermatan sulfate, heparin, heparan sulfate, and chondroitin sulfate. The ability of this glycosaminoglycan fraction to inhibit binding was unaffected by digestion with lytic enzymes specific for heparin, heparan sulfate and dermatan sulfate, but was lost when the milk fraction was treated with lytic enzymes specific for chondroitin sulfate. Furthermore, a purified milk fraction with high specific inhibitory activity contained chondroitin sulfate but not other glycosaminoglycans. This indicates that the ability of human milk to inhibit gp120 binding to CD4 may be attributed to chondroitin sulfate or to a chondroitin sulfate-like moiety rather than to other components of human milk. We speculate that this human milk glycosaminoglycan could limit the rate of postnatal vertical transmission of HIV in breast-fed infants of HIV-infected mothers.;
    Description
    Journal of Nutrition, 125, 419-424; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
    Access
    Collections
    • Linhardt Research Labs Papers

    Browse

    All of DSpace@RPICommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    Login

    DSpace software copyright © 2002-2022  DuraSpace
    Contact Us | Send Feedback
    DSpace Express is a service operated by 
    Atmire NV