A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus

In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV- infected H9 cells and HIV-infected cells from the monocyte cell line U937. These result...

Descripción completa

Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189190/
https://www.ncbi.nlm.nih.gov/pubmed/2909656
_version_ 1782146584325128192
collection PubMed
description In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV- infected H9 cells and HIV-infected cells from the monocyte cell line U937. These results indicate MBP most likely recognizes high mannose glycans known to be present on gp120 in the domain that is recognized by CD4 and thereby inhibits viral entry to susceptible cells. In support of this contention, recombinant gp120 binds directly to MBP; the binding is saturable, mannan inhibitable, removed by N-glycanase treatment, and dependent on divalent cations.
format Text
id pubmed-2189190
institution National Center for Biotechnology Information
language English
publishDate 1989
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21891902008-04-17 A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus J Exp Med Articles In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV- infected H9 cells and HIV-infected cells from the monocyte cell line U937. These results indicate MBP most likely recognizes high mannose glycans known to be present on gp120 in the domain that is recognized by CD4 and thereby inhibits viral entry to susceptible cells. In support of this contention, recombinant gp120 binds directly to MBP; the binding is saturable, mannan inhibitable, removed by N-glycanase treatment, and dependent on divalent cations. The Rockefeller University Press 1989-01-01 /pmc/articles/PMC2189190/ /pubmed/2909656 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title_full A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title_fullStr A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title_full_unstemmed A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title_short A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
title_sort human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189190/
https://www.ncbi.nlm.nih.gov/pubmed/2909656

Ejemplares similares