Document Detail


Enterovirus 70 receptor utilization is controlled by capsid residues that also regulate host range and cytopathogenicity.
MedLine Citation:
PMID:  17537857     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Enterovirus type 70, an etiologic agent of acute hemorrhagic conjunctivitis, may bind different cellular receptors depending on cell type. To understand how EV70-receptor interaction is controlled, we studied two variants of the virus with distinct receptor utilization. EV70-Rmk, derived by passage in rhesus monkey kidney cells, replicates poorly in HeLa cells and does not cause cytopathic effects. Decay accelerating factor (DAF) is not a cell receptor for EV70-Rmk. Passage of EV70-Rmk in HeLa cells lead to isolation of EV70-Dne, which does not replicate in rhesus monkey kidney cells but grows to high titers in HeLa cells and causes cytopathic effects. DAF is sufficient for cell entry of EV70-Dne. EV70-Rmk replicates in human eye and brain-derived cell lines, whereas the Dne strain replicates only in HeLa cells and in conjunctiva-derived 15C4 cells. The two EV70 strains differ by five amino acid changes in the viral capsid. Single substitution of four of the five EV70-Rmk amino acids with the residue from EV70-Dne leads to lytic replication in HeLa cells. Conversely, substitution of any of the five EV70-Dne amino acids with the EV70-Rmk amino acid does not alter replication in HeLa cells. Three of these capsid amino acids are predicted to be located in the canyon encircling the fivefold axis of symmetry, one amino acid is found at the fivefold axis of symmetry, and one is located the interior of the capsid. The five EV70 residues define a region of the capsid that controls viral host range, DAF utilization, and cytopathogenicity.
Authors:
Melissa Stewart Kim; Vincent R Racaniello
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2007-05-30
Journal Detail:
Title:  Journal of virology     Volume:  81     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-07-26     Completed Date:  2007-09-13     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8648-55     Citation Subset:  IM    
Affiliation:
Department of Microbiology, Columbia University College of Physicians & Surgeons, 701 W. 168th Street, New York, NY 10032, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / chemistry,  genetics
Animals
Antigens, CD55 / metabolism
Capsid / chemistry*,  metabolism
Capsid Proteins / chemistry*,  metabolism
Enterovirus D, Human / chemistry,  genetics,  physiology*
HeLa Cells
Humans
Macaca mulatta
Molecular Sequence Data
Protein Conformation
Receptors, Virus / antagonists & inhibitors,  metabolism*
Virus Attachment*
Virus Replication
Grant Support
ID/Acronym/Agency:
AI 20017/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Antigens, CD55; 0/Capsid Proteins; 0/Receptors, Virus
Comments/Corrections

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