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Title: Recombinant soluble adenovirus receptor

Abstract

Disclosed are isolated polypeptides from human CAR (coxsackievirus and adenovirus receptor) protein which bind adenovirus. Specifically disclosed are amino acid sequences which corresponds to adenovirus binding domain D1 and the entire extracellular domain of human CAR protein comprising D1 and D2. In other aspects, the disclosure relates to nucleic acid sequences encoding these domains as well as expression vectors which encode the domains and bacterial cells containing such vectors. Also disclosed is an isolated fusion protein comprised of the D1 polypeptide sequence fused to a polypeptide sequence which facilitates folding of D1 into a functional, soluble domain when expressed in bacteria. The functional D1 domain finds application for example in a therapeutic method for treating a patient infected with a virus which binds to D1, and also in a method for identifying an antiviral compound which interferes with viral attachment. Also included is a method for specifically targeting a cell for infection by a virus which binds to D1.

Inventors:
 [1]
  1. East Setauket, NY
Issue Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States)
OSTI Identifier:
874466
Patent Number(s):
6395875
Assignee:
Brookhaven Science Associates LLC (Upton, NY)
Patent Classifications (CPCs):
C - CHEMISTRY C07 - ORGANIC CHEMISTRY C07K - PEPTIDES
A - HUMAN NECESSITIES A61 - MEDICAL OR VETERINARY SCIENCE A61K - PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
DOE Contract Number:  
AC02-98CH10886
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
recombinant; soluble; adenovirus; receptor; disclosed; isolated; polypeptides; human; car; coxsackievirus; protein; bind; specifically; amino; acid; sequences; corresponds; binding; domain; d1; entire; extracellular; comprising; d2; aspects; disclosure; relates; nucleic; encoding; domains; expression; vectors; encode; bacterial; cells; containing; fusion; comprised; polypeptide; sequence; fused; facilitates; folding; functional; expressed; bacteria; application; example; therapeutic; method; treating; patient; infected; virus; binds; identifying; antiviral; compound; interferes; viral; attachment; included; targeting; cell; infection; nucleic acid; amino acid; acid sequence; binding domain; isolated polypeptide; specifically disclosed; /530/

Citation Formats

Freimuth, Paul I. Recombinant soluble adenovirus receptor. United States: N. p., 2002. Web.
Freimuth, Paul I. Recombinant soluble adenovirus receptor. United States.
Freimuth, Paul I. Tue . "Recombinant soluble adenovirus receptor". United States. https://www.osti.gov/servlets/purl/874466.
@article{osti_874466,
title = {Recombinant soluble adenovirus receptor},
author = {Freimuth, Paul I},
abstractNote = {Disclosed are isolated polypeptides from human CAR (coxsackievirus and adenovirus receptor) protein which bind adenovirus. Specifically disclosed are amino acid sequences which corresponds to adenovirus binding domain D1 and the entire extracellular domain of human CAR protein comprising D1 and D2. In other aspects, the disclosure relates to nucleic acid sequences encoding these domains as well as expression vectors which encode the domains and bacterial cells containing such vectors. Also disclosed is an isolated fusion protein comprised of the D1 polypeptide sequence fused to a polypeptide sequence which facilitates folding of D1 into a functional, soluble domain when expressed in bacteria. The functional D1 domain finds application for example in a therapeutic method for treating a patient infected with a virus which binds to D1, and also in a method for identifying an antiviral compound which interferes with viral attachment. Also included is a method for specifically targeting a cell for infection by a virus which binds to D1.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2002},
month = {1}
}

Works referenced in this record:

The Immunoglobulin Fold
journal, September 1994


HCAR and MCAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
journal, April 1997


Human adenovirus-host cell interactions: comparative study with members of subgroups B and C.
journal, January 1990


Unrelated animal viruses share receptors
journal, February 1976


Crystal structure of the receptor-binding domain of adenovirus type 5 fiberprotein at 1.7 Å resolution
journal, December 1994