Functional domains of the poliovirus receptor

Journal Article · Wed May 15 00:00:00 EDT 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.88.10.4104· OSTI ID:6057499

Koike, Satoshi; Ise, Iku; Nomoto, Akio ^[1]

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1. Tokyo Metropolitan Institute of Medical Science (Japan)

A number of mutant cDNAs of the human poliovirus receptor were constructed to identify essential regions of the molecule as the receptor. All mutant cDNAs carrying the sequence coding for the entire N-terminal immunoglobulin-like domain (domain I) confer permissiveness for poliovirus to mouse L cells, but a mutant cDNA lacking the sequence for domain I does not. The transformants permissive for poliovirus were able to bind the virus and were also recognized by monoclonal antibody D171, which competes with poliovirus for the cellular receptor. These results strongly suggest that the poliovirus binding site resides in domain I of the receptor. Mutant cDNAs for the sequence encoding the intracellular peptide were also constructed and expressed in mouse L cells. Susceptibility of these cells to poliovirus revealed that the entire putative cytoplasmic domain is not essential for virus infection. Thus, the cytoplasmic domain of the molecule appears not to play a role in the penetration of poliovirus.

• OSTI ID: 6057499
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:10; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
POLIO VIRUS
RECEPTORS
RECOMBINANT DNA
DNA SEQUENCING
CELL TRANSFORMATIONS
IMMUNOGLOBULINS
INFECTIOUS DISEASES
MONOCLONAL ANTIBODIES
MUTANTS
ANTIBODIES
DISEASES
DNA
GLOBULINS
MEMBRANE PROTEINS
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
VIRUSES
550200* - Biochemistry