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M94A3329.TXT
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Document 3329
DOCN M94A3329
TI Laminin and fibronectin interfere with the binding of HIV-1 gp120/160 to
CD4.
DT 9412
AU Bozzini S; Falcone V; Conaldi PG; Visai L; Dolei A; Speziale P; Toniolo
A; Dept. of Biochemistry, University of Pavia, Italy.
SO Int Conf AIDS. 1994 Aug 7-12;10(1):100 (abstract no. PA0018). Unique
Identifier : AIDSLINE ICA10/94369246
AB OBJECTIVE: In vitro experiments indicate that not yet defined host
components may hinder the early interactions of HIV-1 with target cells.
We checked whether human extracellular matrix proteins could bind HIV-1
env glycoproteins thus preventing virus-receptor interaction, or
facilitating infection by trapping the virus in the immediate proximity
of cell membranes. METHODS: Radiolabeled recombinant gp160, gp120 and
gp41 were tested for their ability to bind solid phase-immobilized
extracellular matrix proteins. Fibronectin fragments were obtained by
trypsin/thermolysin digestion. The effect of extracellular matrix
proteins on the interaction of env glycoproteins with CD4 was evaluated
by radiometric or immunoenzymatic assay. RESULTS: HIV-1 gp120/160 bind
to fibronectin, laminin and vitronectin, but not to fibrinogen, fetuin,
alpha-1-acid glycoprotein. Both gp120 and gp160 bind to the
heparin-binding domain of fibronectin, whereas gp160 interacts also with
the DNA-binding domain. Western blot analysis of fibronectin fragments
showed that gp120 and gp160 recognize selectively the intact protein and
two 30KDa bands corresponding to the above mentioned domains. Binding to
intact fibronectin and to the heparin-binding domain is inhibited in a
dose-dependent manner by heparins, heparan sulphate, antibody
recognizing the heparin-binding domain, and unlabeled viral proteins.
The interaction of gp120/160 with fibronectin, vitronectin, laminin, and
their fragments interfered with the binding of these env proteins to
CD4. The gp120/160-CD4 interaction was inhibited by 50% to 75%.
DISCUSSION AND CONCLUSION: The results indicate that gp120/160 bind to
selected extracellular matrix proteins suggesting a potential role of
these tissue components in modulating the early virus-cell interactions.
DE Antigens, CD4/*METABOLISM Binding Sites Cell
Membrane/METABOLISM/MICROBIOLOGY Fibronectins/*METABOLISM Gene
Products, env/METABOLISM Human HIV Envelope Protein gp120/METABOLISM
HIV Envelope Protein gp41/METABOLISM HIV-1/*METABOLISM In Vitro
Laminin/*METABOLISM Protein Binding Protein Precursors/METABOLISM
Recombinant Proteins/METABOLISM Support, Non-U.S. Gov't MEETING
ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).