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J Biol Chem, Vol. 275, Issue 13, 9120-9130, March 31, 2000
From the Department of Biology, Massachusetts Institute of
Technology, Cambridge, Massachusetts 02139
The murine class B, type I scavenger receptor
(mSR-BI) is a receptor for both high density lipoprotein (HDL) and low
density lipoprotein (LDL) and mediates selective, rather than
endocytic, uptake of lipoprotein lipid. We have developed a
"retrovirus library-based activity dissection" method to generate
mSR-BI mutants in which some, but not all, of the activities of this
multifunctional protein have been disrupted. This method employs three
techniques: 1) efficient in vitro cDNA mutagenesis
(here error-prone PCR was used), 2) efficient retroviral delivery and
high expression of single mutant cDNAs into individual cells, and
3) isolation of infected cells expressing the desired mutant phenotype
using high sensitivity positive/negative screening by two-color
fluorescence-activated cell sorting. A set of mutants, all having
arginine substitutions at two common sites (positions 402 or 401 and
position 418), were isolated and characterized. Mutation at either site
alone did not generate as strong a mutant phenotype (loss of DiI uptake from DiI-HDL) as did the double mutations. "Activity-dissected" double mutants were as effective as wild-type mSR-BI in functioning as
LDL receptors, mediating high affinity LDL binding and uptake of
metabolically active cholesterol from LDL, but they lost most of their
corresponding HDL receptor activity. Thus, these mutants provide
support for the proposal that the interaction of SR-BI with HDL differs
from that with LDL. Examination of the in vivo function of
such mutants may provide insights into the differential roles of the
LDL and HDL receptor activities of SR-BI in normal lipoprotein
metabolism and in SR-BI's ability to protect against atherosclerosis.
Dissociation of the High Density Lipoprotein and Low Density
Lipoprotein Binding Activities of Murine Scavenger Receptor Class B
Type I (mSR-BI) Using Retrovirus Library-based Activity
Dissection*
,
*
This work was supported in part by National Institutes of
Health Grants HL41484 and HL52212.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Postdoctoral Fellow of the American Heart Association, New England
Affiliate, Inc.
§
National Institutes of Health National Research Service Award
Postdoctoral Fellow.
¶
To whom correspondence should be addressed: Rm. 68-483, Biology Dept., Massachusetts Inst. of Technology, Cambridge, MA 02139. Tel.: 617-253-6793; Fax: 617-258-5851; E-mail: krieger@mit.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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