About: Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins

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About: Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins
Creator	Schaal, Heiner Schreiber, Michael Schwalbe, Birco Kirst, Martin Polzer, Svenja Van Yperen, Melanie
Source	PMC
abstract	BACKGROUND: Myeloperoxidase (MPO), an important element of the microbicidal activity of neutrophils, generates hypochlorous acid (HOCl) from H(2)O(2 )and chloride, which is released into body fluids. Besides its direct microbicidal activity, HOCl can react with amino acid residues and HOCl-modified proteins can be detected in vivo. FINDINGS: This report is based on binding studies of HOCl-modified serum albumins to HIV-1 gp120 and three different neutralization assays using infectious virus. The binding studies were carried out by surface plasmon resonance spectroscopy and by standard ELISA techniques. Virus neutralization assays were carried out using HIV-1 NL4-3 virus and recombinant strains with CXCR4 and CCR5 coreceptor usage. Viral infection was monitored by a standard p24 or X-gal staining assay. Our data demonstrate that HOCl-modified mouse-, bovine- and human serum albumins all bind to the HIV-1 NL4-3 gp120 (LAV) glycoprotein in contrast to non-modified albumin. Binding of HOCl-modified albumin to gp120 correlated to the blockade of CD4 as well as that of V3 loop specific monoclonal antibody binding. In neutralization experiments, HOCl-modified serum albumins inhibited replication and syncytium formation of the X4- and R5-tropic NL4-3 isolates in a dose dependent manner. CONCLUSIONS: Our data indicate that HOCl-modified serum albumin veils the binding site for CD4 and the V3 loop on gp120. Such masking of the viral gp120/gp41 envelope complex might be a simple but promising strategy to inactivate HIV-1 and therefore prevent infection when HOCl-modified serum albumin is applied, for example, as a topical microbicide.
has issue date	2010-06-02(xsd:dateTime)
bibo:doi	10.1186/1756-0500-3-155
bibo:pmid	20525179
has license	cc-by
sha1sum (hex)	1831b9b4ecd716560e565ea11c0ad1a01dbc9314
schema:url	https://doi.org/10.1186/1756-0500-3-155
resource representing a document's title	Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins
has PubMed Central identifier	PMC2887905
has PubMed identifier	20525179
schema:publication	BMC Res Notes
resource representing a document's body	covid:1831b9b4ecd716560e565ea11c0ad1a01dbc9314#body_text
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